Structural Delineation of a Quaternary, Cleavage-Dependent Epitope at the gp41-gp120 Interface on Intact HIV-1 Env Trimers

All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we define and structurally characterize a unique epitope on Env that is recognized by a recently discovered family of human monoclonal antibodi...

Full description

Saved in:

Bibliographic Details
Published in	Immunity (Cambridge, Mass.) Vol. 40; no. 5; pp. 669 - 680
Main Authors	Blattner, Claudia, Lee, Jeong Hyun, Sliepen, Kwinten, Derking, Ronald, Falkowska, Emilia, de la Peña, Alba Torrents, Cupo, Albert, Julien, Jean-Philippe, van Gils, Marit, Lee, Peter S., Peng, Wenjie, Paulson, James C., Poignard, Pascal, Burton, Dennis R., Moore, John P., Sanders, Rogier W., Wilson, Ian A., Ward, Andrew B.
Format	Journal Article
Language	English
Published	United States Elsevier Inc 15.05.2014 Elsevier Limited
Subjects	Acquired immune deficiency syndrome AIDS Antibodies, Monoclonal - immunology Antibodies, Monoclonal - ultrastructure Antibodies, Neutralizing - immunology Antibodies, Neutralizing - ultrastructure Binding Sites, Antibody - immunology Cell Line Chemical bonds Colleges & universities Councils Crystallization Crystallography, X-Ray env Gene Products, Human Immunodeficiency Virus - immunology Epitopes - immunology Grants HEK293 Cells HIV Antibodies - immunology HIV Antibodies - ultrastructure HIV Envelope Protein gp120 - immunology HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp41 - metabolism HIV Infections - immunology HIV Infections - prevention & control HIV-1 - immunology Human immunodeficiency virus 1 Humans Medical research Microscopy Molecular Sequence Data Polysaccharides - immunology Protein Structure, Quaternary Proteins Scholarships & fellowships Vaccines Viral infections California
Online Access	Get full text
ISSN	1074-7613 1097-4180 1097-4180
DOI	10.1016/j.immuni.2014.04.008

Cover

Abstract	All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we define and structurally characterize a unique epitope on Env that is recognized by a recently discovered family of human monoclonal antibodies (PGT151–PGT158). The PGT151 epitope is comprised of residues and glycans at the interface of gp41 and gp120 within a single protomer and glycans from both subunits of a second protomer and represents a neutralizing epitope that is dependent on both gp120 and gp41. Because PGT151 binds only to properly formed, cleaved trimers, this distinctive property, and its ability to stabilize Env trimers, has enabled the successful purification of mature, cleaved Env trimers from the cell surface as a complex with PGT151. Here we compare the structural and functional properties of membrane-extracted Env trimers from several clades with those of the soluble, cleaved SOSIP gp140 trimer. [Display omitted] •PGT151 binds an interprotomer epitope formed by gp41 and gp120 on cleaved Env trimers•The PGT151 epitope does not overlap with any other epitope described so far•PGT151 enables isolation of functional cleaved Env from the cell membrane•Membrane-extracted and soluble SOSIP.664 Env trimers are structurally similar
AbstractList	All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we define and structurally characterize a unique epitope on Env that is recognized by a recently discovered family of human monoclonal antibodies (PGT151-PGT158). The PGT151 epitope is comprised of residues and glycans at the interface of gp41 and gp120 within a single protomer and glycans from both subunits of a second protomer and represents a neutralizing epitope that is dependent on both gp120 and gp41. Because PGT151 binds only to properly formed, cleaved trimers, this distinctive property, and its ability to stabilize Env trimers, has enabled the successful purification of mature, cleaved Env trimers from the cell surface as a complex with PGT151. Here we compare the structural and functional properties of membrane-extracted Env trimers from several clades with those of the soluble, cleaved SOSIP gp140 trimer. All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we define and structurally characterize a unique epitope on Env that is recognized by a recently discovered family of human monoclonal antibodies (PGT151–PGT158). The PGT151 epitope is comprised of residues and glycans at the interface of gp41 and gp120 within a single protomer and glycans from both subunits of a second protomer and represents a neutralizing epitope that is dependent on both gp120 and gp41. Because PGT151 binds only to properly formed, cleaved trimers, this distinctive property, and its ability to stabilize Env trimers, has enabled the successful purification of mature, cleaved Env trimers from the cell surface as a complex with PGT151. Here we compare the structural and functional properties of membrane-extracted Env trimers from several clades with those of the soluble, cleaved SOSIP gp140 trimer. [Display omitted] •PGT151 binds an interprotomer epitope formed by gp41 and gp120 on cleaved Env trimers•The PGT151 epitope does not overlap with any other epitope described so far•PGT151 enables isolation of functional cleaved Env from the cell membrane•Membrane-extracted and soluble SOSIP.664 Env trimers are structurally similar All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we define and structurally characterize a unique epitope on Env that is recognized by a recently discovered family of human monoclonal antibodies (PGT151-PGT158). The PGT151 epitope is comprised of residues and glycans at the interface of gp41 and gp120 within a single protomer and glycans from both subunits of a second protomer and represents a neutralizing epitope that is dependent on both gp120 and gp41. Because PGT151 binds only to properly formed, cleaved trimers, this distinctive property, and its ability to stabilize Env trimers, has enabled the successful purification of mature, cleaved Env trimers from the cell surface as a complex with PGT151. Here we compare the structural and functional properties of membrane-extracted Env trimers from several clades with those of the soluble, cleaved SOSIP gp140 trimer.All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we define and structurally characterize a unique epitope on Env that is recognized by a recently discovered family of human monoclonal antibodies (PGT151-PGT158). The PGT151 epitope is comprised of residues and glycans at the interface of gp41 and gp120 within a single protomer and glycans from both subunits of a second protomer and represents a neutralizing epitope that is dependent on both gp120 and gp41. Because PGT151 binds only to properly formed, cleaved trimers, this distinctive property, and its ability to stabilize Env trimers, has enabled the successful purification of mature, cleaved Env trimers from the cell surface as a complex with PGT151. Here we compare the structural and functional properties of membrane-extracted Env trimers from several clades with those of the soluble, cleaved SOSIP gp140 trimer. All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we define and structurally characterize a unique epitope on Env that is recognized by a recently discovered family of human monoclonal antibodies (PGT151-158). The PGT151 epitope is comprised of residues and glycans at the interface of gp41 and gp120 within a single protomer and glycans from both subunits of a second protomer and represents a neutralizing epitope that is dependent on both gp120 and gp41. As PGT151 binds only to properly formed, cleaved trimers, this distinctive property, and its ability to stabilize Env trimers, has enabled the successful purification of mature, cleaved Env trimers from the cell surface as a complex with PGT151. Here we compare the structural and functional properties of membrane-extracted Env trimers from several clades with those of the soluble, cleaved SOSIP gp140 trimer.
Author	Lee, Peter S. Wilson, Ian A. Peng, Wenjie Cupo, Albert van Gils, Marit Paulson, James C. Julien, Jean-Philippe Sanders, Rogier W. de la Peña, Alba Torrents Lee, Jeong Hyun Moore, John P. Burton, Dennis R. Falkowska, Emilia Blattner, Claudia Sliepen, Kwinten Derking, Ronald Ward, Andrew B. Poignard, Pascal
AuthorAffiliation	6 Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA 10 Ragon Institute of MGH, MIT, and Harvard, Cambridge, MA 02129, USA 3 Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, The Scripps Research Institute, La Jolla, CA 92037, USA 7 Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA 8 Department of Medical Microbiology, Academic Medical Center, Amsterdam, Netherlands 9 Weill Medical College of Cornell University, New York, NY 10021, USA 4 Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA 5 Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA 2 IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA 1 Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
AuthorAffiliation_xml	– name: 3 Center for HIV/AIDS Vaccine Immunology and Immunogen Discovery, The Scripps Research Institute, La Jolla, CA 92037, USA – name: 4 Department of Immunology and Microbial Science, The Scripps Research Institute, La Jolla, CA 92037, USA – name: 7 Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – name: 2 IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA – name: 6 Department of Chemical Physiology, The Scripps Research Institute, La Jolla, CA 92037, USA – name: 8 Department of Medical Microbiology, Academic Medical Center, Amsterdam, Netherlands – name: 10 Ragon Institute of MGH, MIT, and Harvard, Cambridge, MA 02129, USA – name: 1 Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – name: 5 Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – name: 9 Weill Medical College of Cornell University, New York, NY 10021, USA
Author_xml	– sequence: 1 givenname: Claudia surname: Blattner fullname: Blattner, Claudia organization: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 2 givenname: Jeong Hyun surname: Lee fullname: Lee, Jeong Hyun organization: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 3 givenname: Kwinten surname: Sliepen fullname: Sliepen, Kwinten organization: Department of Medical Microbiology, Academic Medical Center, 1105 AZ Amsterdam, the Netherlands – sequence: 4 givenname: Ronald surname: Derking fullname: Derking, Ronald organization: Department of Medical Microbiology, Academic Medical Center, 1105 AZ Amsterdam, the Netherlands – sequence: 5 givenname: Emilia surname: Falkowska fullname: Falkowska, Emilia organization: IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 6 givenname: Alba Torrents surname: de la Peña fullname: de la Peña, Alba Torrents organization: Department of Medical Microbiology, Academic Medical Center, 1105 AZ Amsterdam, the Netherlands – sequence: 7 givenname: Albert surname: Cupo fullname: Cupo, Albert organization: Weill Medical College of Cornell University, New York, NY 10021, USA – sequence: 8 givenname: Jean-Philippe surname: Julien fullname: Julien, Jean-Philippe organization: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 9 givenname: Marit surname: van Gils fullname: van Gils, Marit organization: Department of Medical Microbiology, Academic Medical Center, 1105 AZ Amsterdam, the Netherlands – sequence: 10 givenname: Peter S. surname: Lee fullname: Lee, Peter S. organization: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 11 givenname: Wenjie surname: Peng fullname: Peng, Wenjie organization: Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 12 givenname: James C. surname: Paulson fullname: Paulson, James C. organization: Department of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 13 givenname: Pascal surname: Poignard fullname: Poignard, Pascal organization: IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 14 givenname: Dennis R. surname: Burton fullname: Burton, Dennis R. organization: IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 15 givenname: John P. surname: Moore fullname: Moore, John P. organization: Weill Medical College of Cornell University, New York, NY 10021, USA – sequence: 16 givenname: Rogier W. surname: Sanders fullname: Sanders, Rogier W. organization: Department of Medical Microbiology, Academic Medical Center, 1105 AZ Amsterdam, the Netherlands – sequence: 17 givenname: Ian A. surname: Wilson fullname: Wilson, Ian A. email: wilson@scripps.edu organization: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA – sequence: 18 givenname: Andrew B. surname: Ward fullname: Ward, Andrew B. email: abward@scripps.edu organization: Department of Integrative Structural and Computational Biology, The Scripps Research Institute, La Jolla, CA 92037, USA
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/24768348$$D View this record in MEDLINE/PubMed
BookMark	eNqNUl2L1DAULbLifug_EAn44oMdb9q0aX0QZHZ0BxZEXH0NaXpnNkObdNN0ZP313tlZF90HmXAhCTnncO65OU2OnHeYJC85zDjw8t1mZvt-cnaWARczoILqSXLCoZap4BUc7c5SpLLk-XFyOo4bIGBRw7PkOBOyrHJRnSS_vsUwmTgF3bFz7KxDHa13zK-YZl8nHTE4HW7fsnmHeqvXmJ7jgK5FF9lisNEPyHRk8RrZehA8XQ88A7Z0xFtpg4yk6KJNZBfLHylnC7dlV8H2GMbnydOV7kZ8cb-fJd8_La7mF-nll8_L-cfL1JRcxpQ851mLrRYtrSJrGtFqXeUlAIratAKKqi1LmYHUjRFclA2WUAtY1VllZJ6fJcVed3KDvv2pu04N5IC6UhzULku1Ufss1S5LBVRQEe_DnjdMTY-toZYppQeu11b9--LstVr7rSJHErgkgTf3AsHfTDhG1dvRYNdph34aFS9EXtcVQH0ANCt5JguREfT1I-jGTzSk7g4lqjqnH0CoV3-bf3D9Z_IEEHuACX4cA64ODeX9I5qx8e7LUAS2OzBRpHFvLQY1GovOYGsDmqhab_8v8Buo8-xu
CitedBy_id	crossref_primary_10_1016_j_celrep_2022_110485 crossref_primary_10_1038_nmicrobiol_2016_199 crossref_primary_10_1038_s41598_020_59711_y crossref_primary_10_1128_JVI_01369_20 crossref_primary_10_1371_journal_ppat_1008026 crossref_primary_10_1016_j_celrep_2019_04_082 crossref_primary_10_1016_j_isci_2023_107403 crossref_primary_10_1128_JVI_01426_20 crossref_primary_10_1126_scitranslmed_aaj1928 crossref_primary_10_3389_fpubh_2017_00032 crossref_primary_10_3390_v12020163 crossref_primary_10_1016_j_cell_2016_04_050 crossref_primary_10_1186_s12977_016_0312_7 crossref_primary_10_1074_jbc_M117_776419 crossref_primary_10_1021_acs_jproteome_7b00639 crossref_primary_10_3390_v11080705 crossref_primary_10_1016_j_celrep_2017_02_003 crossref_primary_10_1128_jvi_01604_22 crossref_primary_10_1128_mBio_00036_17 crossref_primary_10_3389_fimmu_2024_1443377 crossref_primary_10_1002_bit_26498 crossref_primary_10_1073_pnas_1415789111 crossref_primary_10_1128_JVI_02213_14 crossref_primary_10_1038_ni_3158 crossref_primary_10_1126_sciadv_aau6769 crossref_primary_10_3390_v10060333 crossref_primary_10_1186_s12977_015_0210_4 crossref_primary_10_1038_s41594_022_00852_1 crossref_primary_10_1016_j_antiviral_2015_02_006 crossref_primary_10_1111_febs_13530 crossref_primary_10_1016_j_celrep_2018_05_046 crossref_primary_10_1074_jbc_RA118_004579 crossref_primary_10_1371_journal_ppat_1004570 crossref_primary_10_1097_QAI_0000000000000854 crossref_primary_10_1126_science_aac4223 crossref_primary_10_1038_s41426_018_0175_1 crossref_primary_10_1038_s41591_018_0042_6 crossref_primary_10_3389_fimmu_2021_708227 crossref_primary_10_1016_j_virol_2014_06_006 crossref_primary_10_1038_ncomms9167 crossref_primary_10_1128_JVI_01953_15 crossref_primary_10_1021_acsinfecdis_7b00192 crossref_primary_10_1016_j_immuni_2018_07_009 crossref_primary_10_1371_journal_pone_0181886 crossref_primary_10_1371_journal_ppat_1007159 crossref_primary_10_1586_14760584_2016_1129905 crossref_primary_10_1016_j_isci_2020_101711 crossref_primary_10_1128_mBio_01598_16 crossref_primary_10_1016_j_chom_2017_05_003 crossref_primary_10_1371_journal_ppat_1005537 crossref_primary_10_1371_journal_ppat_1006986 crossref_primary_10_1073_pnas_2112887119 crossref_primary_10_1177_2515135520957763 crossref_primary_10_1016_j_bbagen_2020_129733 crossref_primary_10_1016_j_smim_2021_101470 crossref_primary_10_1128_MMBR_00024_15 crossref_primary_10_1038_nature13808 crossref_primary_10_1016_j_virol_2015_08_002 crossref_primary_10_1146_annurev_immunol_041015_055515 crossref_primary_10_1371_journal_ppat_1007024 crossref_primary_10_1016_j_vaccine_2018_01_081 crossref_primary_10_1016_j_chembiol_2022_03_009 crossref_primary_10_1093_nar_gkv404 crossref_primary_10_1016_j_celrep_2020_107981 crossref_primary_10_1093_glycob_cww031 crossref_primary_10_1016_j_tim_2014_12_007 crossref_primary_10_1016_j_chom_2023_06_006 crossref_primary_10_7554_eLife_65005 crossref_primary_10_1016_j_antiviral_2021_105085 crossref_primary_10_1371_journal_ppat_1006614 crossref_primary_10_1016_j_virol_2017_07_001 crossref_primary_10_1093_infdis_jiw555 crossref_primary_10_3390_vaccines9070774 crossref_primary_10_1128_JVI_02083_14 crossref_primary_10_3390_v13071405 crossref_primary_10_1371_journal_ppat_1005520 crossref_primary_10_1097_QAD_0000000000002011 crossref_primary_10_1186_s12977_023_00624_9 crossref_primary_10_1016_j_coi_2016_05_013 crossref_primary_10_1186_s12985_024_02394_y crossref_primary_10_3390_biom5042919 crossref_primary_10_1016_j_cell_2015_11_056 crossref_primary_10_1016_j_cell_2015_08_035 crossref_primary_10_1016_j_virol_2016_01_002 crossref_primary_10_1128_JVI_02321_15 crossref_primary_10_1128_jvi_00767_22 crossref_primary_10_1021_jasms_1c00211 crossref_primary_10_2174_1568026623666221019110334 crossref_primary_10_1126_science_aaa9804 crossref_primary_10_1002_cbic_202200236 crossref_primary_10_1186_s12977_018_0431_4 crossref_primary_10_1080_19420862_2021_1979800 crossref_primary_10_3389_fimmu_2014_00417 crossref_primary_10_1016_j_jmb_2019_04_016 crossref_primary_10_1128_JVI_01861_19 crossref_primary_10_1097_QAD_0000000000001177 crossref_primary_10_1016_j_coi_2020_03_013 crossref_primary_10_1016_j_vaccine_2016_08_089 crossref_primary_10_1128_JVI_00862_17 crossref_primary_10_1016_j_immuni_2017_04_011 crossref_primary_10_1016_j_molimm_2015_12_002 crossref_primary_10_1128_JVI_00277_18 crossref_primary_10_1016_j_immuni_2018_02_013 crossref_primary_10_1021_acs_jpcb_0c11516 crossref_primary_10_1128_mBio_00296_15 crossref_primary_10_3390_vaccines4010002 crossref_primary_10_3389_fimmu_2016_00661 crossref_primary_10_1371_journal_ppat_1007920 crossref_primary_10_1371_journal_pone_0193773 crossref_primary_10_4049_jimmunol_1402344 crossref_primary_10_1134_S0026893316030110 crossref_primary_10_1016_j_immuni_2014_04_009 crossref_primary_10_1371_journal_ppat_1005989 crossref_primary_10_1016_j_vaccine_2015_08_012 crossref_primary_10_1128_jvi_01878_21 crossref_primary_10_1371_journal_pone_0128823 crossref_primary_10_1155_2015_560347 crossref_primary_10_1016_j_cell_2019_06_030 crossref_primary_10_1016_j_celrep_2017_11_016 crossref_primary_10_1038_nprot_2018_024 crossref_primary_10_1186_s12977_018_0439_9 crossref_primary_10_1038_ncomms12041 crossref_primary_10_1038_ncomms12040 crossref_primary_10_1080_21645515_2016_1232785 crossref_primary_10_1016_j_str_2020_04_022 crossref_primary_10_1128_jvi_01668_21 crossref_primary_10_1186_s12977_018_0443_0 crossref_primary_10_1371_journal_ppat_1004767 crossref_primary_10_1016_j_chembiol_2023_12_017 crossref_primary_10_1089_aid_2014_0319 crossref_primary_10_3390_ijms17111901 crossref_primary_10_1074_jbc_M115_656611 crossref_primary_10_1128_JVI_01012_16 crossref_primary_10_1016_j_bbagen_2019_05_012 crossref_primary_10_1371_journal_ppat_1011601 crossref_primary_10_1586_14760584_2015_1027690 crossref_primary_10_1016_j_coviro_2015_03_013 crossref_primary_10_3390_vaccines10111916 crossref_primary_10_1038_s41594_023_01062_z crossref_primary_10_1016_j_celrep_2018_08_051 crossref_primary_10_1371_journal_ppat_1009526 crossref_primary_10_2139_ssrn_4199639 crossref_primary_10_1016_j_celrep_2015_03_047 crossref_primary_10_1038_srep36685 crossref_primary_10_1126_science_aad2450 crossref_primary_10_1128_JVI_01705_14 crossref_primary_10_1111_imr_12507 crossref_primary_10_1038_emi_2017_18 crossref_primary_10_1111_imr_12515 crossref_primary_10_1128_JVI_03738_14 crossref_primary_10_1038_nature13601 crossref_primary_10_1128_jvi_00592_23 crossref_primary_10_1016_j_xcrm_2021_100314 crossref_primary_10_3390_vaccines9030239 crossref_primary_10_1097_COH_0000000000000153 crossref_primary_10_1128_JVI_01653_15 crossref_primary_10_1038_nm_3598 crossref_primary_10_1016_j_coi_2016_06_002 crossref_primary_10_1128_JVI_02652_15 crossref_primary_10_1146_annurev_biophys_060414_034156 crossref_primary_10_1038_s41598_017_00935_w crossref_primary_10_1074_jbc_M116_725614 crossref_primary_10_1074_jbc_M117_788919 crossref_primary_10_1128_JVI_01894_16 crossref_primary_10_1016_j_immuni_2017_03_017 crossref_primary_10_1128_JVI_00304_19 crossref_primary_10_1016_j_it_2014_08_007 crossref_primary_10_1107_S1399004715013917 crossref_primary_10_1371_journal_ppat_1005035 crossref_primary_10_1128_JVI_01779_17 crossref_primary_10_1371_journal_pone_0117227 crossref_primary_10_1016_j_cell_2016_05_024 crossref_primary_10_3390_v12111210 crossref_primary_10_1128_JVI_03090_15 crossref_primary_10_1038_s44298_024_00082_w crossref_primary_10_1016_j_vaccine_2019_01_048 crossref_primary_10_1128_JVI_01190_15 crossref_primary_10_1038_s41467_023_37742_z crossref_primary_10_1371_journal_ppat_1009624 crossref_primary_10_1172_JCI82057 crossref_primary_10_1016_j_immuni_2023_01_013 crossref_primary_10_1038_ncomms11544 crossref_primary_10_1371_journal_pone_0170672 crossref_primary_10_1186_s12977_018_0453_y crossref_primary_10_1371_journal_ppat_1004973 crossref_primary_10_1371_journal_ppat_1006114 crossref_primary_10_1016_j_chom_2019_04_011 crossref_primary_10_1016_j_virol_2015_09_010 crossref_primary_10_1016_j_celrep_2016_07_074 crossref_primary_10_1371_journal_ppat_1009185 crossref_primary_10_1371_journal_ppat_1007431 crossref_primary_10_1016_j_sbi_2017_03_008 crossref_primary_10_1038_ncomms9443 crossref_primary_10_1038_ncomms7144 crossref_primary_10_1016_j_isci_2024_108877 crossref_primary_10_1038_ncomms8479 crossref_primary_10_1093_glycob_cwu123 crossref_primary_10_3389_fimmu_2019_02793 crossref_primary_10_1128_JVI_03473_14 crossref_primary_10_1016_j_cell_2024_10_003 crossref_primary_10_1128_JVI_03136_14 crossref_primary_10_1128_mBio_01674_18 crossref_primary_10_1016_j_coviro_2015_04_002 crossref_primary_10_3390_ijms231810767 crossref_primary_10_1128_JVI_03451_14 crossref_primary_10_1016_j_celrep_2023_112755 crossref_primary_10_1128_JVI_01709_18 crossref_primary_10_1371_journal_pone_0106597 crossref_primary_10_1038_nrd_2016_173 crossref_primary_10_1016_j_celrep_2020_107583 crossref_primary_10_1016_j_isci_2024_110141 crossref_primary_10_1128_jvi_00710_23 crossref_primary_10_1016_j_jmb_2017_12_010 crossref_primary_10_1089_aid_2018_0102 crossref_primary_10_1038_s42003_024_06659_8 crossref_primary_10_1038_ncomms14954 crossref_primary_10_1142_S0219720018400073 crossref_primary_10_1371_journal_pone_0208345 crossref_primary_10_1128_JVI_00958_20 crossref_primary_10_1074_jbc_RA117_000537 crossref_primary_10_1097_COH_0000000000000148 crossref_primary_10_3389_fimmu_2014_00250 crossref_primary_10_1016_j_tibs_2014_12_006 crossref_primary_10_1089_aid_2015_0135 crossref_primary_10_1016_j_tim_2017_10_007 crossref_primary_10_3390_v13091774 crossref_primary_10_1007_s11033_023_08474_6 crossref_primary_10_1016_j_immuni_2016_06_026 crossref_primary_10_1007_s11427_015_4852_1 crossref_primary_10_1016_j_immuni_2016_04_016 crossref_primary_10_1038_nchembio_1685 crossref_primary_10_1371_journal_ppat_1005233 crossref_primary_10_1074_jbc_RA117_000709 crossref_primary_10_1371_journal_ppat_1005110 crossref_primary_10_1111_odi_12481 crossref_primary_10_1016_j_celrep_2015_05_017 crossref_primary_10_1038_s41467_021_26846_z crossref_primary_10_1097_COH_0000000000000360 crossref_primary_10_1126_scitranslmed_aad5752 crossref_primary_10_1038_s41467_018_06121_4 crossref_primary_10_1128_JVI_00148_20 crossref_primary_10_1128_jvi_01857_22 crossref_primary_10_1371_journal_pone_0122443 crossref_primary_10_1073_pnas_1507793112 crossref_primary_10_1371_journal_ppat_1004932 crossref_primary_10_17537_2019_14_430 crossref_primary_10_3389_fimmu_2019_02968 crossref_primary_10_1128_JVI_00094_21 crossref_primary_10_1128_JVI_00412_15 crossref_primary_10_1371_journal_ppat_1008171 crossref_primary_10_1097_COH_0000000000000368 crossref_primary_10_1016_j_it_2016_01_007 crossref_primary_10_1016_S2352_3018_18_30174_7 crossref_primary_10_1128_jvi_01594_23 crossref_primary_10_1016_j_celrep_2016_02_058 crossref_primary_10_1080_14760584_2019_1690458 crossref_primary_10_1371_journal_pone_0158861 crossref_primary_10_3390_v14010129 crossref_primary_10_1021_acscentsci_8b00588 crossref_primary_10_1517_14712598_2015_1021328 crossref_primary_10_1016_j_celrep_2018_07_080 crossref_primary_10_12688_f1000research_7254_1 crossref_primary_10_1371_journal_pone_0233577 crossref_primary_10_1371_journal_pone_0122111 crossref_primary_10_1038_s41467_019_08738_5 crossref_primary_10_1111_imr_12484 crossref_primary_10_1016_j_isci_2022_105473 crossref_primary_10_1111_imr_12481 crossref_primary_10_1111_pbi_12963 crossref_primary_10_1080_19420862_2017_1364824 crossref_primary_10_1186_s12977_019_0493_y crossref_primary_10_1016_j_celrep_2021_108933 crossref_primary_10_1016_j_tim_2020_03_007 crossref_primary_10_1126_science_aab1253 crossref_primary_10_1073_pnas_1700634114 crossref_primary_10_1016_j_crmeth_2023_100509 crossref_primary_10_1128_JVI_00230_15 crossref_primary_10_1126_science_aae0474 crossref_primary_10_1016_j_tim_2022_02_004 crossref_primary_10_1038_s41541_024_00918_9 crossref_primary_10_1126_scitranslmed_adh9039
Cites_doi	10.1371/journal.ppat.1003618 10.1016/j.immuni.2012.08.012 10.1089/08892220260387959 10.1016/S0076-6879(97)76066-X 10.1038/nature12746 10.1016/j.chom.2012.09.008 10.1126/science.1178746 10.1371/journal.ppat.1003342 10.1089/0889222041524544 10.1128/JVI.01543-12 10.1128/JVI.67.11.6642-6647.1993 10.1073/pnas.1314351110 10.1038/nature10660 10.1126/science.1245625 10.1038/nsmb.2594 10.1021/pr9002728 10.1038/nature11544 10.1128/JVI.76.17.8875-8889.2002 10.1016/j.jmb.2005.02.031 10.1126/science.7973652 10.1126/science.1207532 10.1016/j.antiviral.2003.09.009 10.1016/j.jsb.2007.03.005 10.1093/emboj/17.16.4572 10.1038/nature12744 10.1126/science.1225416 10.1128/JVI.67.7.3978-3988.1993 10.1006/jsbi.1999.4174 10.1126/science.1192819 10.1093/bioinformatics/bti1140 10.1038/nature10696 10.1126/science.1213256 10.1126/science.1207227 10.1016/j.immuni.2014.04.009 10.1128/JVI.00110-09 10.1073/pnas.1217537110 10.1038/nature11604 10.1038/nature07159 10.1038/nature10373 10.1107/S0907444909052925 10.1128/JVI.01222-13 10.1073/pnas.1315295110 10.1371/journal.pone.0044241 10.1128/JVI.75.22.10892-10905.2001 10.1126/science.1241144 10.1016/j.virol.2004.10.042 10.1107/S0907444904019158 10.1107/S0907444906045975 10.1084/jem.20120423 10.1126/science.1245627 10.1016/j.jsb.2006.05.009
ContentType	Journal Article
Copyright	2014 Elsevier Inc. Copyright © 2014 Elsevier Inc. All rights reserved. Copyright Elsevier Limited May 15, 2014 2014 Elsevier Inc. All rights reserved. 2014
Copyright_xml	– notice: 2014 Elsevier Inc. – notice: Copyright © 2014 Elsevier Inc. All rights reserved. – notice: Copyright Elsevier Limited May 15, 2014 – notice: 2014 Elsevier Inc. All rights reserved. 2014
DBID	6I. AAFTH AAYXX CITATION CGR CUY CVF ECM EIF NPM 7QL 7QP 7QR 7T5 7T7 7TK 7TM 7U9 8FD C1K FR3 H94 K9. M7N NAPCQ P64 RC3 7X8 5PM ADTOC UNPAY
DOI	10.1016/j.immuni.2014.04.008
DatabaseName	ScienceDirect Open Access Titles Elsevier:ScienceDirect:Open Access CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Bacteriology Abstracts (Microbiology B) Calcium & Calcified Tissue Abstracts Chemoreception Abstracts Immunology Abstracts Industrial and Applied Microbiology Abstracts (Microbiology A) Neurosciences Abstracts Nucleic Acids Abstracts Virology and AIDS Abstracts Technology Research Database Environmental Sciences and Pollution Management Engineering Research Database AIDS and Cancer Research Abstracts ProQuest Health & Medical Complete (Alumni) Algology Mycology and Protozoology Abstracts (Microbiology C) Nursing & Allied Health Premium Biotechnology and BioEngineering Abstracts Genetics Abstracts MEDLINE - Academic PubMed Central (Full Participant titles) Unpaywall for CDI: Periodical Content Unpaywall
DatabaseTitle	CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Virology and AIDS Abstracts Technology Research Database Nucleic Acids Abstracts ProQuest Health & Medical Complete (Alumni) Neurosciences Abstracts Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management Nursing & Allied Health Premium Genetics Abstracts Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) AIDS and Cancer Research Abstracts Chemoreception Abstracts Immunology Abstracts Engineering Research Database Industrial and Applied Microbiology Abstracts (Microbiology A) Calcium & Calcified Tissue Abstracts MEDLINE - Academic
DatabaseTitleList	AIDS and Cancer Research Abstracts MEDLINE - Academic MEDLINE Virology and AIDS Abstracts
Database_xml	– sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database – sequence: 3 dbid: UNPAY name: Unpaywall url: https://proxy.k.utb.cz/login?url=https://unpaywall.org/ sourceTypes: Open Access Repository
DeliveryMethod	fulltext_linktorsrc
Discipline	Medicine Biology
EISSN	1097-4180
EndPage	680
ExternalDocumentID	10.1016/j.immuni.2014.04.008 PMC4057017 3305263181 24768348 10_1016_j_immuni_2014_04_008 S1074761314001228
Genre	Research Support, Non-U.S. Gov't Journal Article Research Support, N.I.H., Extramural
GeographicLocations	California
GeographicLocations_xml	– name: California
GrantInformation_xml	– fundername: NIAID NIH HHS grantid: P30 AI036214 – fundername: NIAID NIH HHS grantid: UM1 AI100663 – fundername: NIGMS NIH HHS grantid: P41 GM103310 – fundername: NIAID NIH HHS grantid: P01 AI082362 – fundername: NIAID NIH HHS grantid: R01 AI084817 – fundername: NIAID NIH HHS grantid: R56 AI084817 – fundername: NIGMS NIH HHS grantid: GM103310
GroupedDBID	--- --K -DZ 0R~ 1RT 1~5 2WC 3V. 4.4 457 4G. 53G 5GY 5VS 62- 6I. 7-5 7RV 7X7 8C1 8FE 8FH AACTN AAEDT AAEDW AAFTH AAIAV AAKRW AAQFI AAUCE AAVLU AAXJY AAXUO ABMAC ABMWF ABOCM ABVKL ACGFO ACGFS ACIWK ACPRK ADBBV ADEZE ADFRT ADJPV AEFWE AENEX AEXQZ AFKRA AFRAH AFTJW AGGSO AGHFR AGKMS AHMBA AITUG ALKID ALMA_UNASSIGNED_HOLDINGS AMRAJ ASPBG AVWKF AZFZN BAWUL BBNVY BENPR BHPHI BKEYQ BPHCQ BVXVI C45 CS3 DIK DU5 E3Z EBS EJD F5P FCP FDB FIRID HCIFZ IH2 IHE IXB J1W JIG LK8 LX5 M2O M3Z M41 M7P N9A NCXOZ O-L O9- OK1 OVD P2P PQQKQ PROAC RCE RIG ROL RPZ SCP SES SSZ TEORI TR2 WQ6 ZA5 .55 .GJ 29I AAIKJ AALRI AAMRU AAQXK AAYWO AAYXX ABDGV ABJNI ABWVN ACRPL ACVFH ADCNI ADMUD ADNMO ADVLN AEUPX AFPUW AGQPQ AHHHB AIGII AKAPO AKBMS AKRWK AKYEP APXCP CITATION EFKBS FEDTE FGOYB G-2 HVGLF HZ~ OHT OZT R2- UHS X7M Y6R ZGI CGR CUY CVF ECM EIF NPM 7QL 7QP 7QR 7T5 7T7 7TK 7TM 7U9 8FD C1K FR3 H94 K9. M7N NAPCQ P64 RC3 7X8 5PM ADTOC AGCQF UNPAY
ID	FETCH-LOGICAL-c617t-14532deda4dddd52bb4daa83600e49cd4058d667207abc4146be60940f928c733
IEDL.DBID	IXB
ISSN	1074-7613 1097-4180
IngestDate	Tue Aug 26 13:34:39 EDT 2025 Tue Sep 30 16:18:06 EDT 2025 Thu Oct 02 09:56:25 EDT 2025 Sun Sep 28 00:31:28 EDT 2025 Tue Oct 07 06:36:30 EDT 2025 Thu Apr 03 07:05:26 EDT 2025 Wed Oct 01 04:51:51 EDT 2025 Thu Apr 24 22:55:27 EDT 2025 Fri Feb 23 02:28:37 EST 2024
IsDoiOpenAccess	true
IsOpenAccess	true
IsPeerReviewed	true
IsScholarly	true
Issue	5
Language	English
License	http://www.elsevier.com/open-access/userlicense/1.0 Copyright © 2014 Elsevier Inc. All rights reserved.
LinkModel	DirectLink
MergedId	FETCHMERGED-LOGICAL-c617t-14532deda4dddd52bb4daa83600e49cd4058d667207abc4146be60940f928c733
Notes	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 ObjectType-Article-2 ObjectType-Feature-1 These authors contributed equally to this work
OpenAccessLink	https://www.sciencedirect.com/science/article/pii/S1074761314001228
PMID	24768348
PQID	1524893097
PQPubID	2031079
PageCount	12
ParticipantIDs	unpaywall_primary_10_1016_j_immuni_2014_04_008 pubmedcentral_primary_oai_pubmedcentral_nih_gov_4057017 proquest_miscellaneous_1543998009 proquest_miscellaneous_1526127542 proquest_journals_1524893097 pubmed_primary_24768348 crossref_primary_10_1016_j_immuni_2014_04_008 crossref_citationtrail_10_1016_j_immuni_2014_04_008 elsevier_sciencedirect_doi_10_1016_j_immuni_2014_04_008
ProviderPackageCode	CITATION AAYXX
PublicationCentury	2000
PublicationDate	2014-05-15
PublicationDateYYYYMMDD	2014-05-15
PublicationDate_xml	– month: 05 year: 2014 text: 2014-05-15 day: 15
PublicationDecade	2010
PublicationPlace	United States
PublicationPlace_xml	– name: United States – name: Cambridge
PublicationTitle	Immunity (Cambridge, Mass.)
PublicationTitleAlternate	Immunity
PublicationYear	2014
Publisher	Elsevier Inc Elsevier Limited
Publisher_xml	– name: Elsevier Inc – name: Elsevier Limited
References	Klein, Mouquet, Dosenovic, Scheid, Scharf, Nussenzweig (bib19) 2013; 341 Lyumkis, Julien, de Val, Cupo, Potter, Klasse, Burton, Sanders, Moore, Carragher (bib25) 2013; 342 Thali, Moore, Furman, Charles, Ho, Robinson, Sodroski (bib42) 1993; 67 Yoshioka, Pulokas, Fellmann, Potter, Milligan, Carragher (bib47) 2007; 159 Adams, Afonine, Bunkóczi, Chen, Davis, Echols, Headd, Hung, Kapral, Grosse-Kunstleve (bib1) 2010; 66 Khayat, Lee, Julien, Cupo, Klasse, Sanders, Moore, Wilson, Ward (bib16) 2013; 87 Horwitz, Halper-Stromberg, Mouquet, Gitlin, Tretiakova, Eisenreich, Malbec, Gravemann, Billerbeck, Dorner (bib11) 2013; 110 Liu, Bartesaghi, Borgnia, Sapiro, Subramaniam (bib23) 2008; 455 Scheres, Valle, Carazo (bib37) 2005; 21 Zwick, Labrijn, Wang, Spenlehauer, Saphire, Binley, Moore, Stiegler, Katinger, Burton, Parren (bib51) 2001; 75 Julien, Lee, Cupo, Murin, Derking, Hoffenberg, Caulfield, King, Marozsan, Klasse (bib14) 2013; 110 McLellan, Pancera, Carrico, Gorman, Julien, Khayat, Louder, Pejchal, Sastry, Dai (bib27) 2011; 480 McCoy (bib26) 2007; 63 Julien, Sok, Khayat, Lee, Doores, Walker, Ramos, Diwanji, Pejchal, Cupo (bib15) 2013; 9 Emsley, Cowtan (bib8) 2004; 60 Klein, Gaebler, Mouquet, Sather, Lehmann, Scheid, Kraft, Liu, Pietzsch, Hurley (bib17) 2012; 209 Sanders, Busser, Moore, Lu, Berkhout (bib34) 2004; 20 Xiang, Doka, Choudhary, Sodroski, Robinson (bib46) 2002; 18 Zhang, Yuan, Li, Rosa Borges, Watkins, Guenaga, Yang, Wang, Wilson, Li (bib49) 2012; 7 Muster, Steindl, Purtscher, Trkola, Klima, Himmler, Rüker, Katinger (bib28) 1993; 67 Sanders, Vesanen, Schuelke, Master, Schiffner, Kalyanaraman, Paluch, Berkhout, Maddon, Olson (bib33) 2002; 76 Scheid, Mouquet, Ueberheide, Diskin, Klein, Oliveira, Pietzsch, Fenyo, Abadir, Velinzon (bib36) 2011; 333 Kong, Lee, Doores, Murin, Julien, McBride, Liu, Marozsan, Cupo, Klasse (bib20) 2013; 20 Zhang, Shu, Sidorov, Dimitrov (bib48) 2004; 61 Pancera, Wyatt (bib30) 2005; 332 Pejchal, Doores, Walker, Khayat, Huang, Wang, Stanfield, Julien, Ramos, Crispin (bib31) 2011; 334 Shingai, Nishimura, Klein, Mouquet, Donau, Plishka, Buckler-White, Seaman, Piatak, Lifson (bib39) 2013; 503 Zhou, Georgiev, Wu, Yang, Dai, Finzi, Kwon, Scheid, Shi, Xu (bib50) 2010; 329 Li, O’Dell, Wilson, Wu, Schmidt, Hogerkorp, Louder, Longo, Poulsen, Guenaga (bib22) 2012; 86 Huang, Ofek, Laub, Louder, Doria-Rose, Longo, Imamichi, Bailer, Chakrabarti, Sharma (bib12) 2012; 491 Simek, Rida, Priddy, Pung, Carrow, Laufer, Lehrman, Boaz, Tarragona-Fiol, Miiro (bib40) 2009; 83 Tang, Peng, Baldwin, Mann, Jiang, Rees, Ludtke (bib41) 2007; 157 Caffrey, Cai, Kaufman, Stahl, Wingfield, Covell, Gronenborn, Clore (bib7) 1998; 17 Burton, Poignard, Stanfield, Wilson (bib6) 2012; 337 Wu, Zhou, Zhu, Zhang, Georgiev, Wang, Chen, Longo, Louder, McKee (bib45) 2011; 333 Walker, Phogat, Chan-Hui, Wagner, Phung, Goss, Wrin, Simek, Fling, Mitcham (bib43) 2009; 326 Go, Chang, Liao, Sutherland, Alam, Haynes, Desaire (bib10) 2009; 8 Kwong, Mascola (bib21) 2012; 37 Burton, Pyati, Koduri, Sharp, Thornton, Parren, Sawyer, Hendry, Dunlop, Nara (bib4) 1994; 266 Burton, Ahmed, Barouch, Butera, Crotty, Godzik, Kaufmann, McElrath, Nussenzweig, Pulendran (bib5) 2012; 12 Julien, Cupo, Sok, Stanfield, Lyumkis, Deller, Klasse, Burton, Sanders, Moore (bib13) 2013; 342 Ringe, Sanders, Yasmeen, Kim, Lee, Cupo, Korzun, Derking, van Montfort, Julien (bib32) 2013; 110 Falkowska, Le, Ramos, Doores, Lee, Blattner, Ramirez, Derking, van Gils, Liang (bib9) 2014; 40 Ludtke, Baldwin, Chiu (bib24) 1999; 128 Barouch, Whitney, Moldt, Klein, Oliveira, Liu, Stephenson, Chang, Shekhar, Gupta (bib3) 2013; 503 Sanders, Derking, Cupo, Julien, Yasmeen, de Val, Kim, Blattner, de la Peña, Korzun (bib35) 2013; 9 Walker, Huber, Doores, Falkowska, Pejchal, Julien, Wang, Ramos, Chan-Hui, Moyle (bib44) 2011; 477 Otwinowski, Minor (bib29) 1997; 276 Scheres, Valle, Nuñez, Sorzano, Marabini, Herman, Carazo (bib38) 2005; 348 Klein, Halper-Stromberg, Horwitz, Gruell, Scheid, Bournazos, Mouquet, Spatz, Diskin, Abadir (bib18) 2012; 492 Balazs, Chen, Hong, Rao, Yang, Baltimore (bib2) 2012; 481 Pejchal (10.1016/j.immuni.2014.04.008_bib31) 2011; 334 Falkowska (10.1016/j.immuni.2014.04.008_bib9) 2014; 40 Burton (10.1016/j.immuni.2014.04.008_bib5) 2012; 12 Klein (10.1016/j.immuni.2014.04.008_bib18) 2012; 492 Caffrey (10.1016/j.immuni.2014.04.008_bib7) 1998; 17 Julien (10.1016/j.immuni.2014.04.008_bib13) 2013; 342 Ludtke (10.1016/j.immuni.2014.04.008_bib24) 1999; 128 Horwitz (10.1016/j.immuni.2014.04.008_bib11) 2013; 110 Shingai (10.1016/j.immuni.2014.04.008_bib39) 2013; 503 Zwick (10.1016/j.immuni.2014.04.008_bib51) 2001; 75 Lyumkis (10.1016/j.immuni.2014.04.008_bib25) 2013; 342 Pancera (10.1016/j.immuni.2014.04.008_bib30) 2005; 332 Barouch (10.1016/j.immuni.2014.04.008_bib3) 2013; 503 Zhou (10.1016/j.immuni.2014.04.008_bib50) 2010; 329 Scheid (10.1016/j.immuni.2014.04.008_bib36) 2011; 333 Tang (10.1016/j.immuni.2014.04.008_bib41) 2007; 157 Klein (10.1016/j.immuni.2014.04.008_bib17) 2012; 209 Wu (10.1016/j.immuni.2014.04.008_bib45) 2011; 333 Ringe (10.1016/j.immuni.2014.04.008_bib32) 2013; 110 Sanders (10.1016/j.immuni.2014.04.008_bib35) 2013; 9 Balazs (10.1016/j.immuni.2014.04.008_bib2) 2012; 481 Walker (10.1016/j.immuni.2014.04.008_bib44) 2011; 477 Go (10.1016/j.immuni.2014.04.008_bib10) 2009; 8 Burton (10.1016/j.immuni.2014.04.008_bib4) 1994; 266 Liu (10.1016/j.immuni.2014.04.008_bib23) 2008; 455 Julien (10.1016/j.immuni.2014.04.008_bib14) 2013; 110 McLellan (10.1016/j.immuni.2014.04.008_bib27) 2011; 480 Yoshioka (10.1016/j.immuni.2014.04.008_bib47) 2007; 159 Thali (10.1016/j.immuni.2014.04.008_bib42) 1993; 67 Adams (10.1016/j.immuni.2014.04.008_bib1) 2010; 66 Khayat (10.1016/j.immuni.2014.04.008_bib16) 2013; 87 Klein (10.1016/j.immuni.2014.04.008_bib19) 2013; 341 Muster (10.1016/j.immuni.2014.04.008_bib28) 1993; 67 Sanders (10.1016/j.immuni.2014.04.008_bib34) 2004; 20 Walker (10.1016/j.immuni.2014.04.008_bib43) 2009; 326 Julien (10.1016/j.immuni.2014.04.008_bib15) 2013; 9 Xiang (10.1016/j.immuni.2014.04.008_bib46) 2002; 18 Zhang (10.1016/j.immuni.2014.04.008_bib49) 2012; 7 Otwinowski (10.1016/j.immuni.2014.04.008_bib29) 1997; 276 Kwong (10.1016/j.immuni.2014.04.008_bib21) 2012; 37 Scheres (10.1016/j.immuni.2014.04.008_bib37) 2005; 21 Emsley (10.1016/j.immuni.2014.04.008_bib8) 2004; 60 Huang (10.1016/j.immuni.2014.04.008_bib12) 2012; 491 Simek (10.1016/j.immuni.2014.04.008_bib40) 2009; 83 Zhang (10.1016/j.immuni.2014.04.008_bib48) 2004; 61 Burton (10.1016/j.immuni.2014.04.008_bib6) 2012; 337 Sanders (10.1016/j.immuni.2014.04.008_bib33) 2002; 76 Li (10.1016/j.immuni.2014.04.008_bib22) 2012; 86 McCoy (10.1016/j.immuni.2014.04.008_bib26) 2007; 63 Kong (10.1016/j.immuni.2014.04.008_bib20) 2013; 20 Scheres (10.1016/j.immuni.2014.04.008_bib38) 2005; 348
References_xml	– volume: 266 start-page: 1024 year: 1994 end-page: 1027 ident: bib4 article-title: Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody publication-title: Science – volume: 87 start-page: 9865 year: 2013 end-page: 9872 ident: bib16 article-title: Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers publication-title: J. Virol. – volume: 61 start-page: 161 year: 2004 end-page: 164 ident: bib48 article-title: Identification of a novel CD4i human monoclonal antibody Fab that neutralizes HIV-1 primary isolates from different clades publication-title: Antiviral Res. – volume: 18 start-page: 1207 year: 2002 end-page: 1217 ident: bib46 article-title: Characterization of CD4-induced epitopes on the HIV type 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies publication-title: AIDS Res. Hum. Retroviruses – volume: 503 start-page: 277 year: 2013 end-page: 280 ident: bib39 article-title: Antibody-mediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia publication-title: Nature – volume: 40 year: 2014 ident: bib9 article-title: Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved Envelope trimers publication-title: Immunity – volume: 491 start-page: 406 year: 2012 end-page: 412 ident: bib12 article-title: Broad and potent neutralization of HIV-1 by a gp41-specific human antibody publication-title: Nature – volume: 37 start-page: 412 year: 2012 end-page: 425 ident: bib21 article-title: Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies publication-title: Immunity – volume: 337 start-page: 183 year: 2012 end-page: 186 ident: bib6 article-title: Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses publication-title: Science – volume: 334 start-page: 1097 year: 2011 end-page: 1103 ident: bib31 article-title: A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield publication-title: Science – volume: 333 start-page: 1593 year: 2011 end-page: 1602 ident: bib45 article-title: Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing publication-title: Science – volume: 110 start-page: 16538 year: 2013 end-page: 16543 ident: bib11 article-title: HIV-1 suppression and durable control by combining single broadly neutralizing antibodies and antiretroviral drugs in humanized mice publication-title: Proc. Natl. Acad. Sci. USA – volume: 76 start-page: 8875 year: 2002 end-page: 8889 ident: bib33 article-title: Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1 publication-title: J. Virol. – volume: 348 start-page: 139 year: 2005 end-page: 149 ident: bib38 article-title: Maximum-likelihood multi-reference refinement for electron microscopy images publication-title: J. Mol. Biol. – volume: 128 start-page: 82 year: 1999 end-page: 97 ident: bib24 article-title: EMAN: semiautomated software for high-resolution single-particle reconstructions publication-title: J. Struct. Biol. – volume: 9 start-page: e1003342 year: 2013 ident: bib15 article-title: Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans publication-title: PLoS Pathog. – volume: 477 start-page: 466 year: 2011 end-page: 470 ident: bib44 article-title: Broad neutralization coverage of HIV by multiple highly potent antibodies publication-title: Nature – volume: 7 start-page: e44241 year: 2012 ident: bib49 article-title: Identification and characterization of a broadly cross-reactive HIV-1 human monoclonal antibody that binds to both gp120 and gp41 publication-title: PLoS ONE – volume: 20 start-page: 742 year: 2004 end-page: 749 ident: bib34 article-title: Evolutionary repair of HIV type 1 gp41 with a kink in the N-terminal helix leads to restoration of the six-helix bundle structure publication-title: AIDS Res. Hum. Retroviruses – volume: 63 start-page: 32 year: 2007 end-page: 41 ident: bib26 article-title: Solving structures of protein complexes by molecular replacement with Phaser publication-title: Acta Crystallogr. D Biol. Crystallogr. – volume: 110 start-page: 4351 year: 2013 end-page: 4356 ident: bib14 article-title: Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9 publication-title: Proc. Natl. Acad. Sci. USA – volume: 333 start-page: 1633 year: 2011 end-page: 1637 ident: bib36 article-title: Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding publication-title: Science – volume: 341 start-page: 1199 year: 2013 end-page: 1204 ident: bib19 article-title: Antibodies in HIV-1 vaccine development and therapy publication-title: Science – volume: 110 start-page: 18256 year: 2013 end-page: 18261 ident: bib32 article-title: Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation publication-title: Proc. Natl. Acad. Sci. USA – volume: 17 start-page: 4572 year: 1998 end-page: 4584 ident: bib7 article-title: Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41 publication-title: EMBO J. – volume: 60 start-page: 2126 year: 2004 end-page: 2132 ident: bib8 article-title: Coot: model-building tools for molecular graphics publication-title: Acta Crystallogr. D Biol. Crystallogr. – volume: 455 start-page: 109 year: 2008 end-page: 113 ident: bib23 article-title: Molecular architecture of native HIV-1 gp120 trimers publication-title: Nature – volume: 332 start-page: 145 year: 2005 end-page: 156 ident: bib30 article-title: Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage publication-title: Virology – volume: 481 start-page: 81 year: 2012 end-page: 84 ident: bib2 article-title: Antibody-based protection against HIV infection by vectored immunoprophylaxis publication-title: Nature – volume: 326 start-page: 285 year: 2009 end-page: 289 ident: bib43 article-title: Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target publication-title: Science – volume: 66 start-page: 213 year: 2010 end-page: 221 ident: bib1 article-title: PHENIX: a comprehensive Python-based system for macromolecular structure solution publication-title: Acta Crystallogr. D Biol. Crystallogr. – volume: 492 start-page: 118 year: 2012 end-page: 122 ident: bib18 article-title: HIV therapy by a combination of broadly neutralizing antibodies in humanized mice publication-title: Nature – volume: 12 start-page: 396 year: 2012 end-page: 407 ident: bib5 article-title: A blueprint for HIV vaccine discovery publication-title: Cell Host Microbe – volume: 342 start-page: 1484 year: 2013 end-page: 1490 ident: bib25 article-title: Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer publication-title: Science – volume: 83 start-page: 7337 year: 2009 end-page: 7348 ident: bib40 article-title: Human immunodeficiency virus type 1 elite neutralizers: individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm publication-title: J. Virol. – volume: 276 start-page: 307 year: 1997 end-page: 326 ident: bib29 article-title: Processing of X-ray diffraction data collected in oscillation mode publication-title: Methods Enzymol. – volume: 503 start-page: 224 year: 2013 end-page: 228 ident: bib3 article-title: Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys publication-title: Nature – volume: 342 start-page: 1477 year: 2013 end-page: 1483 ident: bib13 article-title: Crystal structure of a soluble cleaved HIV-1 envelope trimer publication-title: Science – volume: 67 start-page: 3978 year: 1993 end-page: 3988 ident: bib42 article-title: Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding publication-title: J. Virol. – volume: 20 start-page: 796 year: 2013 end-page: 803 ident: bib20 article-title: Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120 publication-title: Nat. Struct. Mol. Biol. – volume: 329 start-page: 811 year: 2010 end-page: 817 ident: bib50 article-title: Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01 publication-title: Science – volume: 67 start-page: 6642 year: 1993 end-page: 6647 ident: bib28 article-title: A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1 publication-title: J. Virol. – volume: 157 start-page: 38 year: 2007 end-page: 46 ident: bib41 article-title: EMAN2: an extensible image processing suite for electron microscopy publication-title: J. Struct. Biol. – volume: 209 start-page: 1469 year: 2012 end-page: 1479 ident: bib17 article-title: Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein publication-title: J. Exp. Med. – volume: 9 start-page: e1003618 year: 2013 ident: bib35 article-title: A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies publication-title: PLoS Pathog. – volume: 75 start-page: 10892 year: 2001 end-page: 10905 ident: bib51 article-title: Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41 publication-title: J. Virol. – volume: 8 start-page: 4231 year: 2009 end-page: 4242 ident: bib10 article-title: Glycosylation site-specific analysis of clade C HIV-1 envelope proteins publication-title: J. Proteome Res. – volume: 86 start-page: 11231 year: 2012 end-page: 11241 ident: bib22 article-title: HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelope glycoproteins publication-title: J. Virol. – volume: 21 start-page: ii243 year: 2005 end-page: ii244 ident: bib37 article-title: Fast maximum-likelihood refinement of electron microscopy images publication-title: Bioinformatics – volume: 159 start-page: 335 year: 2007 end-page: 346 ident: bib47 article-title: Automation of random conical tilt and orthogonal tilt data collection using feature-based correlation publication-title: J. Struct. Biol. – volume: 480 start-page: 336 year: 2011 end-page: 343 ident: bib27 article-title: Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9 publication-title: Nature – volume: 9 start-page: e1003618 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib35 article-title: A next-generation cleaved, soluble HIV-1 Env Trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies publication-title: PLoS Pathog. doi: 10.1371/journal.ppat.1003618 – volume: 37 start-page: 412 year: 2012 ident: 10.1016/j.immuni.2014.04.008_bib21 article-title: Human antibodies that neutralize HIV-1: identification, structures, and B cell ontogenies publication-title: Immunity doi: 10.1016/j.immuni.2012.08.012 – volume: 18 start-page: 1207 year: 2002 ident: 10.1016/j.immuni.2014.04.008_bib46 article-title: Characterization of CD4-induced epitopes on the HIV type 1 gp120 envelope glycoprotein recognized by neutralizing human monoclonal antibodies publication-title: AIDS Res. Hum. Retroviruses doi: 10.1089/08892220260387959 – volume: 276 start-page: 307 year: 1997 ident: 10.1016/j.immuni.2014.04.008_bib29 article-title: Processing of X-ray diffraction data collected in oscillation mode publication-title: Methods Enzymol. doi: 10.1016/S0076-6879(97)76066-X – volume: 503 start-page: 277 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib39 article-title: Antibody-mediated immunotherapy of macaques chronically infected with SHIV suppresses viraemia publication-title: Nature doi: 10.1038/nature12746 – volume: 12 start-page: 396 year: 2012 ident: 10.1016/j.immuni.2014.04.008_bib5 article-title: A blueprint for HIV vaccine discovery publication-title: Cell Host Microbe doi: 10.1016/j.chom.2012.09.008 – volume: 326 start-page: 285 year: 2009 ident: 10.1016/j.immuni.2014.04.008_bib43 article-title: Broad and potent neutralizing antibodies from an African donor reveal a new HIV-1 vaccine target publication-title: Science doi: 10.1126/science.1178746 – volume: 9 start-page: e1003342 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib15 article-title: Broadly neutralizing antibody PGT121 allosterically modulates CD4 binding via recognition of the HIV-1 gp120 V3 base and multiple surrounding glycans publication-title: PLoS Pathog. doi: 10.1371/journal.ppat.1003342 – volume: 20 start-page: 742 year: 2004 ident: 10.1016/j.immuni.2014.04.008_bib34 article-title: Evolutionary repair of HIV type 1 gp41 with a kink in the N-terminal helix leads to restoration of the six-helix bundle structure publication-title: AIDS Res. Hum. Retroviruses doi: 10.1089/0889222041524544 – volume: 86 start-page: 11231 year: 2012 ident: 10.1016/j.immuni.2014.04.008_bib22 article-title: HIV-1 neutralizing antibodies display dual recognition of the primary and coreceptor binding sites and preferential binding to fully cleaved envelope glycoproteins publication-title: J. Virol. doi: 10.1128/JVI.01543-12 – volume: 67 start-page: 6642 year: 1993 ident: 10.1016/j.immuni.2014.04.008_bib28 article-title: A conserved neutralizing epitope on gp41 of human immunodeficiency virus type 1 publication-title: J. Virol. doi: 10.1128/JVI.67.11.6642-6647.1993 – volume: 110 start-page: 18256 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib32 article-title: Cleavage strongly influences whether soluble HIV-1 envelope glycoprotein trimers adopt a native-like conformation publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1314351110 – volume: 481 start-page: 81 year: 2012 ident: 10.1016/j.immuni.2014.04.008_bib2 article-title: Antibody-based protection against HIV infection by vectored immunoprophylaxis publication-title: Nature doi: 10.1038/nature10660 – volume: 342 start-page: 1477 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib13 article-title: Crystal structure of a soluble cleaved HIV-1 envelope trimer publication-title: Science doi: 10.1126/science.1245625 – volume: 20 start-page: 796 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib20 article-title: Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120 publication-title: Nat. Struct. Mol. Biol. doi: 10.1038/nsmb.2594 – volume: 8 start-page: 4231 year: 2009 ident: 10.1016/j.immuni.2014.04.008_bib10 article-title: Glycosylation site-specific analysis of clade C HIV-1 envelope proteins publication-title: J. Proteome Res. doi: 10.1021/pr9002728 – volume: 491 start-page: 406 year: 2012 ident: 10.1016/j.immuni.2014.04.008_bib12 article-title: Broad and potent neutralization of HIV-1 by a gp41-specific human antibody publication-title: Nature doi: 10.1038/nature11544 – volume: 76 start-page: 8875 year: 2002 ident: 10.1016/j.immuni.2014.04.008_bib33 article-title: Stabilization of the soluble, cleaved, trimeric form of the envelope glycoprotein complex of human immunodeficiency virus type 1 publication-title: J. Virol. doi: 10.1128/JVI.76.17.8875-8889.2002 – volume: 348 start-page: 139 year: 2005 ident: 10.1016/j.immuni.2014.04.008_bib38 article-title: Maximum-likelihood multi-reference refinement for electron microscopy images publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2005.02.031 – volume: 266 start-page: 1024 year: 1994 ident: 10.1016/j.immuni.2014.04.008_bib4 article-title: Efficient neutralization of primary isolates of HIV-1 by a recombinant human monoclonal antibody publication-title: Science doi: 10.1126/science.7973652 – volume: 333 start-page: 1593 year: 2011 ident: 10.1016/j.immuni.2014.04.008_bib45 article-title: Focused evolution of HIV-1 neutralizing antibodies revealed by structures and deep sequencing publication-title: Science doi: 10.1126/science.1207532 – volume: 61 start-page: 161 year: 2004 ident: 10.1016/j.immuni.2014.04.008_bib48 article-title: Identification of a novel CD4i human monoclonal antibody Fab that neutralizes HIV-1 primary isolates from different clades publication-title: Antiviral Res. doi: 10.1016/j.antiviral.2003.09.009 – volume: 159 start-page: 335 year: 2007 ident: 10.1016/j.immuni.2014.04.008_bib47 article-title: Automation of random conical tilt and orthogonal tilt data collection using feature-based correlation publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2007.03.005 – volume: 17 start-page: 4572 year: 1998 ident: 10.1016/j.immuni.2014.04.008_bib7 article-title: Three-dimensional solution structure of the 44 kDa ectodomain of SIV gp41 publication-title: EMBO J. doi: 10.1093/emboj/17.16.4572 – volume: 503 start-page: 224 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib3 article-title: Therapeutic efficacy of potent neutralizing HIV-1-specific monoclonal antibodies in SHIV-infected rhesus monkeys publication-title: Nature doi: 10.1038/nature12744 – volume: 337 start-page: 183 year: 2012 ident: 10.1016/j.immuni.2014.04.008_bib6 article-title: Broadly neutralizing antibodies present new prospects to counter highly antigenically diverse viruses publication-title: Science doi: 10.1126/science.1225416 – volume: 67 start-page: 3978 year: 1993 ident: 10.1016/j.immuni.2014.04.008_bib42 article-title: Characterization of conserved human immunodeficiency virus type 1 gp120 neutralization epitopes exposed upon gp120-CD4 binding publication-title: J. Virol. doi: 10.1128/JVI.67.7.3978-3988.1993 – volume: 128 start-page: 82 year: 1999 ident: 10.1016/j.immuni.2014.04.008_bib24 article-title: EMAN: semiautomated software for high-resolution single-particle reconstructions publication-title: J. Struct. Biol. doi: 10.1006/jsbi.1999.4174 – volume: 329 start-page: 811 year: 2010 ident: 10.1016/j.immuni.2014.04.008_bib50 article-title: Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01 publication-title: Science doi: 10.1126/science.1192819 – volume: 21 start-page: ii243 issue: Suppl 2 year: 2005 ident: 10.1016/j.immuni.2014.04.008_bib37 article-title: Fast maximum-likelihood refinement of electron microscopy images publication-title: Bioinformatics doi: 10.1093/bioinformatics/bti1140 – volume: 480 start-page: 336 year: 2011 ident: 10.1016/j.immuni.2014.04.008_bib27 article-title: Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9 publication-title: Nature doi: 10.1038/nature10696 – volume: 334 start-page: 1097 year: 2011 ident: 10.1016/j.immuni.2014.04.008_bib31 article-title: A potent and broad neutralizing antibody recognizes and penetrates the HIV glycan shield publication-title: Science doi: 10.1126/science.1213256 – volume: 333 start-page: 1633 year: 2011 ident: 10.1016/j.immuni.2014.04.008_bib36 article-title: Sequence and structural convergence of broad and potent HIV antibodies that mimic CD4 binding publication-title: Science doi: 10.1126/science.1207227 – volume: 40 year: 2014 ident: 10.1016/j.immuni.2014.04.008_bib9 article-title: Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved Envelope trimers publication-title: Immunity doi: 10.1016/j.immuni.2014.04.009 – volume: 83 start-page: 7337 year: 2009 ident: 10.1016/j.immuni.2014.04.008_bib40 article-title: Human immunodeficiency virus type 1 elite neutralizers: individuals with broad and potent neutralizing activity identified by using a high-throughput neutralization assay together with an analytical selection algorithm publication-title: J. Virol. doi: 10.1128/JVI.00110-09 – volume: 110 start-page: 4351 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib14 article-title: Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9 publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1217537110 – volume: 492 start-page: 118 year: 2012 ident: 10.1016/j.immuni.2014.04.008_bib18 article-title: HIV therapy by a combination of broadly neutralizing antibodies in humanized mice publication-title: Nature doi: 10.1038/nature11604 – volume: 455 start-page: 109 year: 2008 ident: 10.1016/j.immuni.2014.04.008_bib23 article-title: Molecular architecture of native HIV-1 gp120 trimers publication-title: Nature doi: 10.1038/nature07159 – volume: 477 start-page: 466 year: 2011 ident: 10.1016/j.immuni.2014.04.008_bib44 article-title: Broad neutralization coverage of HIV by multiple highly potent antibodies publication-title: Nature doi: 10.1038/nature10373 – volume: 66 start-page: 213 year: 2010 ident: 10.1016/j.immuni.2014.04.008_bib1 article-title: PHENIX: a comprehensive Python-based system for macromolecular structure solution publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444909052925 – volume: 87 start-page: 9865 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib16 article-title: Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers publication-title: J. Virol. doi: 10.1128/JVI.01222-13 – volume: 110 start-page: 16538 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib11 article-title: HIV-1 suppression and durable control by combining single broadly neutralizing antibodies and antiretroviral drugs in humanized mice publication-title: Proc. Natl. Acad. Sci. USA doi: 10.1073/pnas.1315295110 – volume: 7 start-page: e44241 year: 2012 ident: 10.1016/j.immuni.2014.04.008_bib49 article-title: Identification and characterization of a broadly cross-reactive HIV-1 human monoclonal antibody that binds to both gp120 and gp41 publication-title: PLoS ONE doi: 10.1371/journal.pone.0044241 – volume: 75 start-page: 10892 year: 2001 ident: 10.1016/j.immuni.2014.04.008_bib51 article-title: Broadly neutralizing antibodies targeted to the membrane-proximal external region of human immunodeficiency virus type 1 glycoprotein gp41 publication-title: J. Virol. doi: 10.1128/JVI.75.22.10892-10905.2001 – volume: 341 start-page: 1199 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib19 article-title: Antibodies in HIV-1 vaccine development and therapy publication-title: Science doi: 10.1126/science.1241144 – volume: 332 start-page: 145 year: 2005 ident: 10.1016/j.immuni.2014.04.008_bib30 article-title: Selective recognition of oligomeric HIV-1 primary isolate envelope glycoproteins by potently neutralizing ligands requires efficient precursor cleavage publication-title: Virology doi: 10.1016/j.virol.2004.10.042 – volume: 60 start-page: 2126 year: 2004 ident: 10.1016/j.immuni.2014.04.008_bib8 article-title: Coot: model-building tools for molecular graphics publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444904019158 – volume: 63 start-page: 32 year: 2007 ident: 10.1016/j.immuni.2014.04.008_bib26 article-title: Solving structures of protein complexes by molecular replacement with Phaser publication-title: Acta Crystallogr. D Biol. Crystallogr. doi: 10.1107/S0907444906045975 – volume: 209 start-page: 1469 year: 2012 ident: 10.1016/j.immuni.2014.04.008_bib17 article-title: Broad neutralization by a combination of antibodies recognizing the CD4 binding site and a new conformational epitope on the HIV-1 envelope protein publication-title: J. Exp. Med. doi: 10.1084/jem.20120423 – volume: 342 start-page: 1484 year: 2013 ident: 10.1016/j.immuni.2014.04.008_bib25 article-title: Cryo-EM structure of a fully glycosylated soluble cleaved HIV-1 envelope trimer publication-title: Science doi: 10.1126/science.1245627 – volume: 157 start-page: 38 year: 2007 ident: 10.1016/j.immuni.2014.04.008_bib41 article-title: EMAN2: an extensible image processing suite for electron microscopy publication-title: J. Struct. Biol. doi: 10.1016/j.jsb.2006.05.009
SSID	ssj0014590
Score	2.583608
Snippet	All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we...
SourceID	unpaywall pubmedcentral proquest pubmed crossref elsevier
SourceType	Open Access Repository Aggregation Database Index Database Enrichment Source Publisher
StartPage	669
SubjectTerms	Acquired immune deficiency syndrome AIDS Antibodies, Monoclonal - immunology Antibodies, Monoclonal - ultrastructure Antibodies, Neutralizing - immunology Antibodies, Neutralizing - ultrastructure Binding Sites, Antibody - immunology Cell Line Chemical bonds Colleges & universities Councils Crystallization Crystallography, X-Ray env Gene Products, Human Immunodeficiency Virus - immunology Epitopes - immunology Grants HEK293 Cells HIV Antibodies - immunology HIV Antibodies - ultrastructure HIV Envelope Protein gp120 - immunology HIV Envelope Protein gp41 - immunology HIV Envelope Protein gp41 - metabolism HIV Infections - immunology HIV Infections - prevention & control HIV-1 - immunology Human immunodeficiency virus 1 Humans Medical research Microscopy Molecular Sequence Data Polysaccharides - immunology Protein Structure, Quaternary Proteins Scholarships & fellowships Vaccines Viral infections
SummonAdditionalLinks	– databaseName: Unpaywall dbid: UNPAY link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Lb9NAEB6VVDwuPEqBQEGLxJFN_Viv42PVpgpIrYA2qJys8e6mFCLHap2i9Ncz45eogmiJcrE8G9nO59lvdme-AXinnfW1076kiMeTincPMUaKWiNjaTqIbGx4Qf_gUI8n6uNJdLIGbeNCzqrkFevKRzfPbvuIkwYp3A4pGOCdoOF2Yad3YF1HRL97sD45_LTzrcst1H6dVJ_EUvlDry2Xq3K6zqqaC07oUpXAKTeV_Pt0tEo3V7Mm7y_yApe_cDb7Y0rafwRf2sKeOhPl52BRZgNztarzePu7fQwPG4Iqdmq7J7Dm8g24W7esXG7AvYNmM_4pXB1V2rOs2yH2uKy9pp9iPhUoPi-wWmo8X74XuzOHl-S35F7TcbcUo4I8SeEEloIYqDgtlC9PCz_wRLVEOUXjBP0UHaApxfjDV-mLUX4pjrkbwfnFJkz2R8e7Y9m0cpCGKFIpfRWFgXUWlaVPFGSZsohcQOI5lRhLtHFI2IgDL8bMKHLfmdMs7TdNgqGJw_AZ9PJ57l6ACNCGoYqcSwKO9wxqdNo4FWYYO4qJ-xC2_2hqGp1zbrcxS9uEth9pjYOUcZB69PVolOxGFbXOxw32cQuWtOEqNQdJaSq6YeRWi6208RcXKbEoVgEi0PbhbXea3nSGB-ZuvqhsNMvxq-BfNhxfUhCQ9OF5DdfudgJC1TBUfOnXgNwZsNL49TP52fdKcZxZPbnuPgw6yN_qKb383wGv4AEfcXqGH21Bj3DsXhPrK7M3zXv-G9KXUjg priority: 102 providerName: Unpaywall
Title	Structural Delineation of a Quaternary, Cleavage-Dependent Epitope at the gp41-gp120 Interface on Intact HIV-1 Env Trimers
URI	https://dx.doi.org/10.1016/j.immuni.2014.04.008 https://www.ncbi.nlm.nih.gov/pubmed/24768348 https://www.proquest.com/docview/1524893097 https://www.proquest.com/docview/1526127542 https://www.proquest.com/docview/1543998009 https://pubmed.ncbi.nlm.nih.gov/PMC4057017 http://www.cell.com/article/S1074761314001228/pdf
UnpaywallVersion	publishedVersion
Volume	40
hasFullText	1
inHoldings	1
isFullTextHit
isPrint
journalDatabaseRights	– providerCode: PRVESC databaseName: Elsevier Free Content customDbUrl: eissn: 1097-4180 dateEnd: 20241101 omitProxy: true ssIdentifier: ssj0014590 issn: 1074-7613 databaseCode: IXB dateStart: 19950101 isFulltext: true titleUrlDefault: https://www.sciencedirect.com providerName: Elsevier – providerCode: PRVBFR databaseName: Free Medical Journals customDbUrl: eissn: 1097-4180 dateEnd: 20241101 omitProxy: true ssIdentifier: ssj0014590 issn: 1074-7613 databaseCode: DIK dateStart: 19950101 isFulltext: true titleUrlDefault: http://www.freemedicaljournals.com providerName: Flying Publisher – providerCode: PRVLSH databaseName: Elsevier Journals customDbUrl: mediaType: online eissn: 1097-4180 dateEnd: 99991231 omitProxy: true ssIdentifier: ssj0014590 issn: 1074-7613 databaseCode: AKRWK dateStart: 19940401 isFulltext: true providerName: Library Specific Holdings
link	http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwELemoQEvaBtfhTEZiUdCE8dJmsfSdeqYNgFboTxZF8cdRVUabelQ-et35zgR1RBDRHlxY0fp-Xz-ne-LsTexyYPYxIGHGo_vSbIeQgKotUY6x-0gyhNNB_onp_FoLD9MoskGGzSxMORW6WR_LdOttHa_dB01u-Vs1j0jV0JUwkNUEcg-RAG_oexR-YajyfvWkiCj1G_9DrF3Ez5nfbxmNgaDHLykTXhKRSb_vD3dhp-3vSgfLIsSVj9hPv9tizrcZo8ctuT9-vN32IYpdtlWXW1ytcvunzg7-mP268ymjaWUG_yAItJr5MgXUw780xLsKeHl6i0fzA1co8jxDlyx3IoPSxQCpeFQcQSP_KKUgXdRBsLn9nRxCtpwfBU2QFd8dPTFC_iwuObnVEjg8uoJGx8Ozwcjz1Vh8DSim8pDCoYiNznIHK9IZJnMASj2wzcy1Tkivh5OayL8BDItUfJmJqasfNNU9HQShk_ZZrEozHPGBeRhKCNjUkGqmoYYTKyNDDNIDKqzHRY2xFfapSinShlz1fii_VD1lCmaMuXj7eMorx1V1ik67uifNPOq1lhN4S5yx8i9hg2UW-pXCgEQJfDx06TDXrePcZGS5QUKs1jaPjFl0pfib31INUT8nnbYs5qz2r8jkNF7yNz46Ws813agJOHrT4rZd5ssnAA5St0Oe9dy5z9R6cV_U-kle0gtcrEIoj22iQxtXiFyq7J9dq9__Pnr8b5dotgan37sf7sBJApD2Q
linkProvider	Elsevier
linkToHtml	http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwED-NIdheEIyPlW1gJB4JzYeTNI-j69TBOgmtQ32zLo47iqo02tKh8tdz53xo1RBDVH1pfa7S8_n8O98XwPvIZF5kIs8hi8d1JHsPMUayWkOd0XEQZrHmC_3RWTS8kJ8n4WQD-k0uDIdV1rq_0ulWW9ffdGtudovZrHvOoYRkhAdkIrB_qPcAHsqQ0Aln8U0-ta4EGSZuG3hI5E3-nA3ymtkkDI7wkrbiKXeZ_PP5dBd_3g2j3FrmBa5-4nx-64w6fgpPanApDqvnfwYbJt-BR1W7ydUOPB7VjvTn8Ovc1o3lmhviiFPSK-goFlOB4usS7TXh1eqD6M8N3pDOcY7qbrmlGBSkBQojsBSEHsVlIT3nsvB8V9jrxSlqI-in6APqUgxPvjmeGOQ3YsydBK6uX8DF8WDcHzp1GwZHE7wpHeJg4GcmQ5nRK_TTVGaInPzhGpnojCBfj9Y19t0YUy1J9aYm4rJ808Tv6TgIXsJmvsjNLggfsyCQoTGJz7aaxghNpI0MUowN2bMdCBrmK13XKOdWGXPVBKP9UNWSKV4y5dLbpVlOO6uoanTcQx8366rWZE3RMXLPzP1GDFS9168VISCu4OMmcQfetcO0S9n1grlZLC1NxKX0pf83GrYNCcAnHXhVSVb7d3yS9F4g-dHXZK4l4Crh6yP57LutFs6InNRuBz620vlPXHr931x6C1vD8ehUnZ6cfdmDbR7heAsv3IdNEm5zQDCuTN_YbfobKItDrA
linkToUnpaywall	http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Lb9NAEB6VVDwuPEqBQEGLxJFN_Viv42PVpgpIrYA2qJys8e6mFCLHap2i9Ncz45eogmiJcrE8G9nO59lvdme-AXinnfW1076kiMeTincPMUaKWiNjaTqIbGx4Qf_gUI8n6uNJdLIGbeNCzqrkFevKRzfPbvuIkwYp3A4pGOCdoOF2Yad3YF1HRL97sD45_LTzrcst1H6dVJ_EUvlDry2Xq3K6zqqaC07oUpXAKTeV_Pt0tEo3V7Mm7y_yApe_cDb7Y0rafwRf2sKeOhPl52BRZgNztarzePu7fQwPG4Iqdmq7J7Dm8g24W7esXG7AvYNmM_4pXB1V2rOs2yH2uKy9pp9iPhUoPi-wWmo8X74XuzOHl-S35F7TcbcUo4I8SeEEloIYqDgtlC9PCz_wRLVEOUXjBP0UHaApxfjDV-mLUX4pjrkbwfnFJkz2R8e7Y9m0cpCGKFIpfRWFgXUWlaVPFGSZsohcQOI5lRhLtHFI2IgDL8bMKHLfmdMs7TdNgqGJw_AZ9PJ57l6ACNCGoYqcSwKO9wxqdNo4FWYYO4qJ-xC2_2hqGp1zbrcxS9uEth9pjYOUcZB69PVolOxGFbXOxw32cQuWtOEqNQdJaSq6YeRWi6208RcXKbEoVgEi0PbhbXea3nSGB-ZuvqhsNMvxq-BfNhxfUhCQ9OF5DdfudgJC1TBUfOnXgNwZsNL49TP52fdKcZxZPbnuPgw6yN_qKb383wGv4AEfcXqGH21Bj3DsXhPrK7M3zXv-G9KXUjg
openUrl	ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Structural+Delineation+of+a+Quaternary%2C+Cleavage-Dependent+Epitope+at+the+gp41-gp120+Interface+on+Intact+HIV-1+Env+Trimers&rft.jtitle=Immunity+%28Cambridge%2C+Mass.%29&rft.au=Blattner%2C+Claudia&rft.au=Lee%2C+Jeong%C2%A0Hyun&rft.au=Sliepen%2C+Kwinten&rft.au=Derking%2C+Ronald&rft.date=2014-05-15&rft.issn=1074-7613&rft.volume=40&rft.issue=5&rft.spage=669&rft.epage=680&rft_id=info:doi/10.1016%2Fj.immuni.2014.04.008&rft.externalDBID=n%2Fa&rft.externalDocID=10_1016_j_immuni_2014_04_008
thumbnail_l	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1074-7613&client=summon
thumbnail_m	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1074-7613&client=summon
thumbnail_s	http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1074-7613&client=summon