Aspergillus fumigatus secretes a protease(s) that displays in silico binding affinity towards the SARS-CoV-2 spike protein and mediates SARS-CoV-2 pseudovirion entry into HEK-293T cells

Background The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infecti...

Full description

Saved in:
Bibliographic Details
Published inVirology journal Vol. 21; no. 1; p. 58
Main Authors Mjokane, Nozethu, Akintemi, Eric O., Sabiu, Saheed, Gcilitshana, Onele M. N., Albertyn, Jacobus, Pohl, Carolina H., Sebolai, Olihile M.
Format Journal Article
LanguageEnglish
Published London BioMed Central 06.03.2024
BioMed Central Ltd
BMC
Subjects
Online AccessGet full text
ISSN1743-422X
1743-422X
DOI10.1186/s12985-024-02331-z

Cover

Abstract Background The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus ( A. ) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein. Methods The supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein. Results We show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions. Conclusion These results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.
AbstractList The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein. The supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein. We show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions. These results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.
The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein. The supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein. We show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions. These results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.
Background The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus ( A. ) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein. Methods The supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein. Results We show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions. Conclusion These results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.
The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein.BACKGROUNDThe novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein.The supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein.METHODSThe supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein.We show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions.RESULTSWe show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions.These results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.CONCLUSIONThese results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.
Abstract Background The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein. Methods The supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein. Results We show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions. Conclusion These results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.
BACKGROUND: The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein. METHODS: The supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein. RESULTS: We show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions. CONCLUSION: These results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.
Background The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein. Methods The supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein. Results We show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions. Conclusion These results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development. Keywords: Aspergillus (A) fumigatus, A. Fumigatus alkaline protease 1, Haddock, HEK-293T cells, SARS-CoV-2 spike protein, Supernatant, Transduction
BackgroundThe novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the COVID-19 clinical control case studies showed that this disease could also manifest in patients with underlying microbial infections such as aspergillosis. The current study aimed to determine if the Aspergillus (A.) fumigatus culture media (i.e., supernatant) possessed protease activity that was sufficient to activate the SARS-CoV-2 spike protein.MethodsThe supernatant was first analysed for protease activity. Thereafter, it was assessed to determine if it possessed proteolytic activity to cleave a fluorogenic mimetic peptide of the SARS-CoV-2 spike protein that contained the S1/S2 site and a full-length spike protein contained in a SARS-CoV-2 pseudovirion. To complement this, a computer-based tool, HADDOCK, was used to predict if A. fumigatus alkaline protease 1 could bind to the SARS-CoV-2 spike protein.ResultsWe show that the supernatant possessed proteolytic activity, and analyses of the molecular docking parameters revealed that A. fumigatus alkaline protease 1 could bind to the spike protein. To confirm the in silico data, it was imperative to provide experimental evidence for enzymatic activity. Here, it was noted that the A. fumigatus supernatant cleaved the mimetic peptide as well as transduced the HEK-293T cells with SARS-CoV-2 pseudovirions.ConclusionThese results suggest that A. fumigatus secretes a protease(s) that activates the SARS-CoV-2 spike protein. Importantly, should these two infectious agents co-occur, there is the potential for A. fumigatus to activate the SARS-CoV-2 spike protein, thus aggravating COVID-19 development.
ArticleNumber 58
Audience Academic
Author Pohl, Carolina H.
Gcilitshana, Onele M. N.
Akintemi, Eric O.
Sebolai, Olihile M.
Mjokane, Nozethu
Albertyn, Jacobus
Sabiu, Saheed
Author_xml – sequence: 1
  givenname: Nozethu
  surname: Mjokane
  fullname: Mjokane, Nozethu
  organization: Department of Microbiology and Biochemistry, University of the Free State
– sequence: 2
  givenname: Eric O.
  surname: Akintemi
  fullname: Akintemi, Eric O.
  organization: Department of Microbiology and Biochemistry, University of the Free State
– sequence: 3
  givenname: Saheed
  surname: Sabiu
  fullname: Sabiu, Saheed
  organization: Department of Biotechnology and Food Science, Faculty of Applied Science, Durban University of Technology
– sequence: 4
  givenname: Onele M. N.
  surname: Gcilitshana
  fullname: Gcilitshana, Onele M. N.
  organization: Department of Microbiology and Biochemistry, University of the Free State
– sequence: 5
  givenname: Jacobus
  surname: Albertyn
  fullname: Albertyn, Jacobus
  organization: Department of Microbiology and Biochemistry, University of the Free State
– sequence: 6
  givenname: Carolina H.
  surname: Pohl
  fullname: Pohl, Carolina H.
  organization: Department of Microbiology and Biochemistry, University of the Free State
– sequence: 7
  givenname: Olihile M.
  surname: Sebolai
  fullname: Sebolai, Olihile M.
  email: sebolaiom@ufs.ac.za
  organization: Department of Microbiology and Biochemistry, University of the Free State
BackLink https://www.ncbi.nlm.nih.gov/pubmed/38448991$$D View this record in MEDLINE/PubMed
BookMark eNqFk99P1TAUxxeDEbj6D_hgmvgCD8P-2tY-mRuCQiQxAWJ8a3q3s1HcbUfboZf_zP_OjovANUazNGvaz_fbntNzdrMt6yxk2WuCDwgR5btAqBRFjilPgzGS3z7LdkjFWc4p_br1ZL6d7YZwhTGjZSVfZNtMcC6kJDvZz3kYwHem78eA2nFpOh3TLEDtIUJAGg3eRdAB9sI-ipc6osaEodergIxFwfSmdmhhbGNsh3TbGmviCkX3XfsmJAGg8_nZeX7ovuQUhcF8g7VjEmvboCU0Rk8HPaGGAGPjbow3ziKw0a_SUdGh46NPOZXsAtXQ9-Fl9rzVfYBX9_9ZdvHh6OLwOD_9_PHkcH6a1yUtY17KshGScUl4yyVuWkE0K8oWM9JUQjNcy5rLRVlgAK4roDXQYkEbjhe8AGCz7GRt2zh9pQZvltqvlNNG3S043ynto6l7UFUlW03lopYF5lARQXVRptdpasKZkDx5vV97DeMiBV5Psel-w3Rzx5pL1bkbRbAkEuPJYe_ewbvrEUJUSxOmdGgLbgyKkYKVRSlE8V-USk6JKEQ1oW__QK_c6G3KaqImN4ar8pHqdArW2NalO9aTqZpXIkXKWaqwWXbwFyp9DSxTqVhoTVrfEOxvCBIT4Ufs9BiCOjk_22TfPE3gQ-Z-13MC6BqovQvBQ_uAEKymplHrplHpWdRd06jbJGJrUUiw7cA_hv8P1S_-ExfH
Cites_doi 10.1148/radiol.2020200274
10.1128/cmr.00094-21
10.1111/j.1538-7836.2003.00421.x
10.1371/journal.ppat.1009225
10.3389/fddsv.2022.899239
10.1002/anie.200604205
10.1021/acs.jpclett.0c01698
10.3390/jof6020088
10.1021/acs.jmedchem.1c00518
10.1021/ja026939x
10.3791/58892
10.1016/j.cell.2021.08.016
10.1016/j.abb.2009.05.013
10.1021/acs.jproteome.0c00430
10.1016/j.jtcme.2021.01.006
10.1016/j.isci.2020.101212
10.1016/j.fgb.2015.02.006
10.3389/fcimb.2020.587269
10.1136/bmj.p1041
10.3390/biology10100966
10.1086/420850
10.1016/j.jmii.2020.09.004
10.1126/science.2683070
10.3389/fimmu.2022.1080822
10.1016/j.micpath.2021.104941
10.3389/fimmu.2020.01041
10.1083/jcb.111.6.2851
10.1016/j.micinf.2009.07.002
10.2108/zsj.20.1183
10.3389/fmed.2021.681469
10.1016/j.funbio.2012.07.004
10.3390/metabo12100982
10.3390/cells11030437
10.1002/emp2.12034
ContentType Journal Article
Copyright The Author(s) 2024
2024. The Author(s).
COPYRIGHT 2024 BioMed Central Ltd.
2024. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
Copyright_xml – notice: The Author(s) 2024
– notice: 2024. The Author(s).
– notice: COPYRIGHT 2024 BioMed Central Ltd.
– notice: 2024. This work is licensed under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.
DBID C6C
AAYXX
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
ISR
3V.
7U9
7X7
7XB
88E
8FI
8FJ
8FK
ABUWG
AFKRA
AZQEC
BENPR
CCPQU
DWQXO
FYUFA
GHDGH
H94
K9.
M0S
M1P
PHGZM
PHGZT
PIMPY
PJZUB
PKEHL
PPXIY
PQEST
PQQKQ
PQUKI
7X8
7S9
L.6
5PM
DOA
DOI 10.1186/s12985-024-02331-z
DatabaseName Springer Nature OA Free Journals
CrossRef
Medline
MEDLINE
MEDLINE (Ovid)
MEDLINE
MEDLINE
PubMed
Gale In Context: Science
ProQuest Central (Corporate)
Virology and AIDS Abstracts
Health & Medical Collection
ProQuest Central (purchase pre-March 2016)
Medical Database (Alumni Edition)
Hospital Premium Collection
Hospital Premium Collection (Alumni Edition)
ProQuest Central (Alumni) (purchase pre-March 2016)
ProQuest Central (Alumni)
ProQuest Central UK/Ireland
ProQuest Central Essentials
ProQuest Central
ProQuest One Community College
ProQuest Central
Health Research Premium Collection
Health Research Premium Collection (Alumni)
AIDS and Cancer Research Abstracts
ProQuest Health & Medical Complete (Alumni)
Health & Medical Collection (Alumni)
Medical Database
ProQuest Central Premium
ProQuest One Academic (New)
ProQuest Publicly Available Content Database
ProQuest Health & Medical Research Collection
ProQuest One Academic Middle East (New)
ProQuest One Health & Nursing
ProQuest One Academic Eastern Edition (DO NOT USE)
ProQuest One Academic
ProQuest One Academic UKI Edition
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
PubMed Central (Full Participant titles)
DOAJ Directory of Open Access Journals
DatabaseTitle CrossRef
MEDLINE
Medline Complete
MEDLINE with Full Text
PubMed
MEDLINE (Ovid)
Publicly Available Content Database
ProQuest One Academic Middle East (New)
ProQuest Central Essentials
ProQuest Health & Medical Complete (Alumni)
ProQuest Central (Alumni Edition)
ProQuest One Community College
ProQuest One Health & Nursing
ProQuest Central
Health Research Premium Collection
Health and Medicine Complete (Alumni Edition)
ProQuest Central Korea
Health & Medical Research Collection
AIDS and Cancer Research Abstracts
ProQuest Central (New)
ProQuest Medical Library (Alumni)
Virology and AIDS Abstracts
ProQuest One Academic Eastern Edition
ProQuest Hospital Collection
Health Research Premium Collection (Alumni)
ProQuest Hospital Collection (Alumni)
ProQuest Health & Medical Complete
ProQuest Medical Library
ProQuest One Academic UKI Edition
ProQuest One Academic
ProQuest One Academic (New)
ProQuest Central (Alumni)
MEDLINE - Academic
AGRICOLA
AGRICOLA - Academic
DatabaseTitleList
MEDLINE


MEDLINE - Academic

AGRICOLA

Publicly Available Content Database
Database_xml – sequence: 1
  dbid: C6C
  name: Springer Nature OA Free Journals
  url: http://www.springeropen.com/
  sourceTypes: Publisher
– sequence: 2
  dbid: DOA
  name: DOAJ Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 3
  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: 4
  dbid: EIF
  name: MEDLINE
  url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search
  sourceTypes: Index Database
– sequence: 5
  dbid: BENPR
  name: ProQuest Central
  url: http://www.proquest.com/pqcentral?accountid=15518
  sourceTypes: Aggregation Database
DeliveryMethod fulltext_linktorsrc
Discipline Medicine
Biology
EISSN 1743-422X
EndPage 58
ExternalDocumentID oai_doaj_org_article_779fa29bc9504e7182a56024dc143894
PMC10919004
A785604300
38448991
10_1186_s12985_024_02331_z
Genre Journal Article
GeographicLocations United States
South Africa
United States--US
Germany
GeographicLocations_xml – name: South Africa
– name: United States
– name: United States--US
– name: Germany
GrantInformation_xml – fundername: National Research Foundation of South Africa
  grantid: grant no. 137965
– fundername: Poliomyelitis Research Foundation of South Africa
  grantid: grant no. 23/78
– fundername: Medical Research Council of South Africa
  grantid: SIR grant
GroupedDBID ---
0R~
123
29Q
2WC
53G
5VS
7X7
88E
8FI
8FJ
AAFWJ
AAHBH
AAJSJ
AASML
ABDBF
ABUWG
ACGFO
ACGFS
ACIHN
ACMJI
ACPRK
ACUHS
ADBBV
ADRAZ
ADUKV
AEAQA
AENEX
AFKRA
AFPKN
AHBYD
AHMBA
AHYZX
ALMA_UNASSIGNED_HOLDINGS
AMKLP
AMTXH
AOIJS
BAPOH
BAWUL
BCNDV
BENPR
BFQNJ
BMC
BPHCQ
BVXVI
C6C
CCPQU
CS3
DIK
E3Z
EAD
EAP
EAS
EBD
EBLON
EBS
EMB
EMK
EMOBN
ESX
F5P
FYUFA
GROUPED_DOAJ
GX1
HMCUK
HYE
IAO
IGS
IHR
INH
INR
ISR
ITC
KQ8
LGEZI
LOTEE
M1P
M48
M~E
NADUK
NXXTH
O5R
O5S
OK1
OVT
P2P
PGMZT
PHGZM
PHGZT
PIMPY
PJZUB
PPXIY
PQQKQ
PROAC
PSQYO
PUEGO
RBZ
RNS
ROL
RPM
RSV
SBL
SOJ
SV3
TR2
TUS
UKHRP
WOQ
WOW
XSB
AAYXX
ALIPV
CITATION
CGR
CUY
CVF
ECM
EIF
NPM
PMFND
3V.
7U9
7XB
8FK
AZQEC
DWQXO
H94
K9.
PKEHL
PQEST
PQUKI
7X8
7S9
L.6
5PM
ID FETCH-LOGICAL-c626t-696d8934914f490df81a356f031d78a30c9c49b650ee4a7e2ce25b2d40b45ee3
IEDL.DBID M48
ISSN 1743-422X
IngestDate Wed Aug 27 01:30:10 EDT 2025
Thu Aug 21 18:35:34 EDT 2025
Sun Aug 24 03:58:41 EDT 2025
Fri Sep 05 05:54:30 EDT 2025
Sat Jul 26 00:08:21 EDT 2025
Tue Jun 17 22:15:45 EDT 2025
Tue Jun 10 21:13:46 EDT 2025
Fri Jun 27 06:04:54 EDT 2025
Mon Jul 21 06:05:22 EDT 2025
Tue Jul 01 01:44:49 EDT 2025
Sat Sep 06 07:30:03 EDT 2025
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Issue 1
Keywords Haddock
HEK-293T cells
SARS-CoV-2 spike protein
Transduction
alkaline protease 1
Supernatant
A. Fumigatus alkaline protease 1
Aspergillus (A) fumigatus
Language English
License 2024. The Author(s).
Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c626t-696d8934914f490df81a356f031d78a30c9c49b650ee4a7e2ce25b2d40b45ee3
Notes ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 14
content type line 23
OpenAccessLink https://doi.org/10.1186/s12985-024-02331-z
PMID 38448991
PQID 2956883076
PQPubID 55248
PageCount 1
ParticipantIDs doaj_primary_oai_doaj_org_article_779fa29bc9504e7182a56024dc143894
pubmedcentral_primary_oai_pubmedcentral_nih_gov_10919004
proquest_miscellaneous_3153656885
proquest_miscellaneous_2942185875
proquest_journals_2956883076
gale_infotracmisc_A785604300
gale_infotracacademiconefile_A785604300
gale_incontextgauss_ISR_A785604300
pubmed_primary_38448991
crossref_primary_10_1186_s12985_024_02331_z
springer_journals_10_1186_s12985_024_02331_z
ProviderPackageCode CITATION
AAYXX
PublicationCentury 2000
PublicationDate 2024-03-06
PublicationDateYYYYMMDD 2024-03-06
PublicationDate_xml – month: 03
  year: 2024
  text: 2024-03-06
  day: 06
PublicationDecade 2020
PublicationPlace London
PublicationPlace_xml – name: London
– name: England
PublicationTitle Virology journal
PublicationTitleAbbrev Virol J
PublicationTitleAlternate Virol J
PublicationYear 2024
Publisher BioMed Central
BioMed Central Ltd
BMC
Publisher_xml – name: BioMed Central
– name: BioMed Central Ltd
– name: BMC
References B Luan (2331_CR17) 2020; 19
MD Toscano (2331_CR18) 2007; 46
N Vankadari (2331_CR30) 2020; 11
N Mjokane (2331_CR35) 2022; 11
D Venkateswarlu (2331_CR33) 2003; 1
M Dadashi (2331_CR4) 2021; 8
N Mjokane (2331_CR34) 2021; 10
PA Bresnahan (2331_CR22) 1990; 111
JA Jaimes (2331_CR25) 2019; 143
F Rahman (2331_CR32) 2021; 11
J Wang (2331_CR20) 2015; 76
JA Jaimes (2331_CR26) 2020; 23
S Tanaka (2331_CR21) 2003; 20
B Sposito (2331_CR6) 2021; 184
J Yee (2331_CR1) 2020; 1
F Salazar (2331_CR7) 2022; 35
JO Aribisala (2331_CR23) 2022; 12
2331_CR27
F Song (2331_CR2) 2020; 295
2331_CR11
E Farnell (2331_CR13) 2012; 116
J Wise (2331_CR28) 2023; 381
BO Villoutreix (2331_CR36) 2022; 2
C Dominguez (2331_CR24) 2003; 125
RS Fuller (2331_CR19) 1989; 246
EEA Osman (2331_CR31) 2021; 65
J Bigot (2331_CR10) 2020; 11
N Murgolo (2331_CR15) 2021; 17
CC Lai (2331_CR29) 2021; 54
2331_CR8
TV Kogan (2331_CR12) 2004; 189
2331_CR3
MN Hoque (2331_CR5) 2021; 156
V Balloy (2331_CR9) 2009; 11
KM Druey (2331_CR14) 2020; 6
MY Wang (2331_CR16) 2020; 10
References_xml – volume: 295
  start-page: 210
  year: 2020
  ident: 2331_CR2
  publication-title: Radiol
  doi: 10.1148/radiol.2020200274
– volume: 35
  start-page: e00094
  year: 2022
  ident: 2331_CR7
  publication-title: Clin Microbiol Rev
  doi: 10.1128/cmr.00094-21
– volume: 1
  start-page: 2577
  year: 2003
  ident: 2331_CR33
  publication-title: J Thromb Haemost
  doi: 10.1111/j.1538-7836.2003.00421.x
– volume: 17
  start-page: e1009225
  year: 2021
  ident: 2331_CR15
  publication-title: PLoS Pathog
  doi: 10.1371/journal.ppat.1009225
– volume: 2
  start-page: 1
  year: 2022
  ident: 2331_CR36
  publication-title: Frontiers
  doi: 10.3389/fddsv.2022.899239
– volume: 46
  start-page: 3212
  year: 2007
  ident: 2331_CR18
  publication-title: Angew Chem Int Ed
  doi: 10.1002/anie.200604205
– volume: 11
  start-page: 6655
  year: 2020
  ident: 2331_CR30
  publication-title: J Phys Chem Lett
  doi: 10.1021/acs.jpclett.0c01698
– volume: 6
  start-page: 88
  year: 2020
  ident: 2331_CR14
  publication-title: J Fungi
  doi: 10.3390/jof6020088
– volume: 65
  start-page: 2747
  year: 2021
  ident: 2331_CR31
  publication-title: J Med Chem
  doi: 10.1021/acs.jmedchem.1c00518
– volume: 125
  start-page: 1731
  year: 2003
  ident: 2331_CR24
  publication-title: J Am Chem Soc
  doi: 10.1021/ja026939x
– volume: 143
  start-page: 358892
  year: 2019
  ident: 2331_CR25
  publication-title: J Vis Exp
  doi: 10.3791/58892
– volume: 184
  start-page: 4953
  year: 2021
  ident: 2331_CR6
  publication-title: Cell
  doi: 10.1016/j.cell.2021.08.016
– ident: 2331_CR27
  doi: 10.1016/j.abb.2009.05.013
– volume: 19
  start-page: 4316
  year: 2020
  ident: 2331_CR17
  publication-title: J Proteome Res
  doi: 10.1021/acs.jproteome.0c00430
– volume: 11
  start-page: 173
  year: 2021
  ident: 2331_CR32
  publication-title: J Tradit Complement Med
  doi: 10.1016/j.jtcme.2021.01.006
– ident: 2331_CR3
– volume: 23
  start-page: 101212
  year: 2020
  ident: 2331_CR26
  publication-title: iScience
  doi: 10.1016/j.isci.2020.101212
– volume: 76
  start-page: 57
  year: 2015
  ident: 2331_CR20
  publication-title: Fungal Genet Biol
  doi: 10.1016/j.fgb.2015.02.006
– volume: 10
  start-page: 587269
  year: 2020
  ident: 2331_CR16
  publication-title: Front Cell Infect Microbiol
  doi: 10.3389/fcimb.2020.587269
– volume: 381
  start-page: 1041
  year: 2023
  ident: 2331_CR28
  publication-title: BMJ
  doi: 10.1136/bmj.p1041
– volume: 10
  start-page: 966
  year: 2021
  ident: 2331_CR34
  publication-title: Biology
  doi: 10.3390/biology10100966
– volume: 189
  start-page: 1965
  year: 2004
  ident: 2331_CR12
  publication-title: J Infect Dis
  doi: 10.1086/420850
– volume: 54
  start-page: 46
  year: 2021
  ident: 2331_CR29
  publication-title: J Microbiol Immunol Infect
  doi: 10.1016/j.jmii.2020.09.004
– volume: 246
  start-page: 482
  year: 1989
  ident: 2331_CR19
  publication-title: Science
  doi: 10.1126/science.2683070
– ident: 2331_CR8
  doi: 10.3389/fimmu.2022.1080822
– volume: 156
  start-page: 104941
  year: 2021
  ident: 2331_CR5
  publication-title: Microb Pathog
  doi: 10.1016/j.micpath.2021.104941
– volume: 11
  start-page: 1041
  year: 2020
  ident: 2331_CR10
  publication-title: Front Immunol
  doi: 10.3389/fimmu.2020.01041
– volume: 111
  start-page: 2851
  year: 1990
  ident: 2331_CR22
  publication-title: J Cell Biol
  doi: 10.1083/jcb.111.6.2851
– volume: 11
  start-page: 919
  year: 2009
  ident: 2331_CR9
  publication-title: Microbes Infect
  doi: 10.1016/j.micinf.2009.07.002
– ident: 2331_CR11
– volume: 20
  start-page: 1183
  year: 2003
  ident: 2331_CR21
  publication-title: Zoolog Sci
  doi: 10.2108/zsj.20.1183
– volume: 8
  start-page: 681469
  year: 2021
  ident: 2331_CR4
  publication-title: Front Med
  doi: 10.3389/fmed.2021.681469
– volume: 116
  start-page: 1003
  year: 2012
  ident: 2331_CR13
  publication-title: Fungal Biol
  doi: 10.1016/j.funbio.2012.07.004
– volume: 12
  start-page: 982
  year: 2022
  ident: 2331_CR23
  publication-title: Metabolites
  doi: 10.3390/metabo12100982
– volume: 11
  start-page: 437
  year: 2022
  ident: 2331_CR35
  publication-title: Cells
  doi: 10.3390/cells11030437
– volume: 1
  start-page: 63
  year: 2020
  ident: 2331_CR1
  publication-title: J Am Coll Emerg Physicians Open
  doi: 10.1002/emp2.12034
SSID ssj0032679
Score 2.3845832
Snippet Background The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2)....
The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2). Data from the...
Background The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2)....
BackgroundThe novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2)....
BACKGROUND: The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2)....
Abstract Background The novel coronavirus disease of 2019 (COVID-19) is an infectious disease caused by severe acute respiratory syndrome coronavirus-2...
SourceID doaj
pubmedcentral
proquest
gale
pubmed
crossref
springer
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
Publisher
StartPage 58
SubjectTerms A. Fumigatus alkaline protease 1
Amino acids
Analysis
Aspergillosis
Aspergillus (A) fumigatus
Aspergillus fumigatus
Biomedical and Life Sciences
Biomedicine
Case studies
Cell culture
Communicable diseases
computer simulation
Coronaviruses
Coronaviruses: emerging and re-emerging pathogens in humans and animals
COVID-19
COVID-19 infection
Culture media
Enzymatic activity
enzyme activity
Fungal infections
Fungi
Glycoproteins
Haddock
Health aspects
HEK-293T cells
HEK293 Cells
Humans
Infectious diseases
Ligands
Medical research
Medicine, Experimental
Molecular Docking Simulation
Peptide Hydrolases
Peptides
Pharmaceutical industry
Proteases
Protein binding
proteinases
Proteins
Proteolysis
Reagents
SARS-CoV-2
SARS-CoV-2 spike protein
Severe acute respiratory syndrome
Severe acute respiratory syndrome coronavirus 2
Spike Glycoprotein, Coronavirus
Spike protein
Supernatant
T cells
Virology
Virulence
SummonAdditionalLinks – databaseName: DOAJ Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV1Lb9QwELZQJRAXBOUVKMggJEAQ1UmcxD4uVasFBIfugnqzHMduoy7Jqk6Qtv-Mf8fYyS6boooLh5VW8TgPz3ge8sw3CL3iYFRKzWSoTUZCyg0PuSmiMCryjGiuOevRPr9m02_000l6stXqy-WE9fDA_cLt5zk3MuaF4imhGjRpLMFIx7RUvnG3RwIlnKyDqV4Hg0-S83WJDMv2LVg15iqRKfySJAovR2bIo_X_rZO3jNLVhMkrp6beGB3dRXcGLxJP-re_h27oehfd7PtKrnbRrS_Difl99GvioMBPq8Wis9h0PxyiBvyzzlsELxNL7JEawJa9sW9xeyZbXFZ2uZAri6sa22oBooKLyhe_YGlMBTpghVufbWthgsazyfEsPGi-hzG2y-pc93eEybIusa9McQ_aolpa3ZXNz-oCZAL7zibwqLbB08PPIfgFc-xOE-wDND86nB9Mw6FdQ6ggKmrDjGcleD-UR9RQTkrDIpmkmQG1UeZMJkRxRXkBLqHWVOY6VjpOi7ikpKCp1slDtFM3tX7s0q3gWpwTYyJJc1IULFVUJeCOmCJTpQrQuzXzxLIH5RA-mGGZ6FktgNXCs1pcBuiD4--G0gFq-wsgZmIQM_EvMQvQSycdwkFm1C4n51R21oqPs2MxyRmQ0oSQAL0eiEwDcqLkUOIAX-VQtkaUeyNK2NNqPLwWQjHoFCtiV9nJQCdnAXqxGXYzXZ5crZvO0VDw2VIIQq-nScDIZe5WQPOol-vN2iQMwnUIGQLERhI_WrzxSF2deVRyhzDLQeUG6P16c_x59-u58-R_cOcpuh37ze06leyhnfai08_AWWyL514v_AZBiWNq
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: Health & Medical Collection
  dbid: 7X7
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwfV1Zb9QwELagCMQLgnIFCjIICRC1msM5_ISWqlUBwUNb0L5ZjmO3EUuy1Fmk9p_x75hxstumqDystIrHuWY88008ByGvBBiVyhSKGZuFjAsrmLBlxKIyz0IjjCj6ap9fs71v_NM0nQ4f3NwQVrnUiV5RV63Gb-RbMea1FSCR2fv5L4Zdo3B3dWihcZ3ciACJYOuGfLpyuACZ-Fp7CLoZj-PpMmmmyLYc2LkCc5M5_JIkYmcjw-Tr9_-rpS-YqcshlJf2Ub152r1L7gy4kk56QbhHrplmndzsO02erpNbX4Y99PvkzwSLgx_Vs9nCUbv4iTU24J9D_Ai4kyrqazeAdXvj3tLuWHW0qt18pk4drRvq6hkIDy1rnw5DlbU1aIVT2vn4WwcTDD2Y7B-w7fY7i6mb1z9Mf0aYrJqK-lwVvNAFqrkzi6r9XZ-AlFDf6wQu1bV0b-czA6RwSHF_wT0gh7s7h9t7bGjgwDT4SR3LRFYBHuIi4paLsLJFpJI0s6BIqrxQSaiF5qIEkGgMV7mJtYnTMq54WPLUmOQhWWvaxjzGACw4FuehtZHieViWRaq5TgCg2DLTlQ7IuyXz5Lwv0yG9e1Nksme1BFZLz2p5FpAPyN8VJZbY9gfakyM5rFiZ58KqWJRapCE3YMJjBegw5pX2HeN5QF6idEgsotFglM6RWjgnPx7sy0leAClPwjAgrwci24KcaDUkPcBTYd2tEeXGiBJWuR4PL4VQDlrGyfM1EZAXq2GciZFzjWkXSMMBxaXgll5Nk4DZy_BUQPOol-vVu0kKcODBiQhIMZL40csbjzT1sa9TjjVnBSjhgGwuF8f5vV_NnSf_f9Sn5Hbsly12Jdkga93JwjwDYNiVz_3q_wsdE15J
  priority: 102
  providerName: ProQuest
– databaseName: Springer Nature OA Free Journals
  dbid: C6C
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1bb9MwFLZgCMQLgnELDGQQEiCIyMVx7MdSbRogeFgL2pvlOPYWUZJqTpC6f8a_49hJSzPYAw-Vqvg4aXNun2Wf7yD0gkNSKTWToTY0Cgk3POSmiMO4yGmkueasZ_v8Qg-_ko_H2fFAk-NqYbb372NG31nIR8zVEBP4pGkcnl9F1zIIvM6ap3S6jrqAQnK-Lor557xR4vH8_H9H4a00dPGI5IV9Up9-Dm6jWwNuxJNe0XfQFV3vout9J8nVLrrxedgjv4t-TRz590m1WHQWm-6H49CAb9bhQ8CVWGLPzQDZ65V9jdtT2eKyssuFXFlc1dhWCzAOXFS-3AVLYyrw-hVu_flaCxM0nk2OZuG0-RYm2C6r77q_I0yWdYl9LYp70JbU0uqubH5WZ2AF2PcygUe1DT7c_xQCEphjt39g76H5wf58ehgODRpCBeugNqScloB3CI-JITwqDYtlmlEDgaLMmUwjxRXhBYBArYnMdaJ0khVJSaKCZFqn99FO3dT6oTtgBdeSPDImliSPioJliqgUAIgpqCpVgN6slSeWPQ2H8MsXRkWvagGqFl7V4jxA751-N5KOQttfAMsSg0eKPOdGJrxQPIuIhhSdSEB_CSmV7whPAvTcWYdwJBm1O4VzIjtrxYfZkZjkDERJGkUBejkImQbsRMmhqAH-lePVGknujSTBi9V4eG2EYogiViSulpNBFKYBerYZdjPdybhaN52TIYDSMlh2Xi6TQlqj7lYg86C36827SRks0GGRECA2svjRyxuP1NWp5yF3nLIcgmyA3q6d489vv1w7j_5P_DG6mXg3dl1I9tBOe9bpJwAE2-KpjwC_AdAWVZ0
  priority: 102
  providerName: Springer Nature
Title Aspergillus fumigatus secretes a protease(s) that displays in silico binding affinity towards the SARS-CoV-2 spike protein and mediates SARS-CoV-2 pseudovirion entry into HEK-293T cells
URI https://link.springer.com/article/10.1186/s12985-024-02331-z
https://www.ncbi.nlm.nih.gov/pubmed/38448991
https://www.proquest.com/docview/2956883076
https://www.proquest.com/docview/2942185875
https://www.proquest.com/docview/3153656885
https://pubmed.ncbi.nlm.nih.gov/PMC10919004
https://doaj.org/article/779fa29bc9504e7182a56024dc143894
Volume 21
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjR3bbtMw1NpFIF4QjFtgVAYh8QAZuTgXPyDUVZ1KERNqO9Q3y0nsLqIkpU4R3YfxfRw7aVnGJvFQtbKPndbnXp8LQq8oKJVMxNwWMnRsQiW1qUxc202i0BFU0Liu9nkaDs7IcBpMd9Cm3VFzgOpa1073kzpbzo9-_Vh_AIZ_bxg-Dt8p0FmxzjMm8PJ9177YRfvmvkiH8pHtrQJYKqb2njbCbeJ5000SzbV7tBSVqef_r9S-pLauhlReuVc16urkHrrb2Jm4WxPGfbQjigN0q-48uT5Atz83d-oP0O-uLhY-y-fzlcJy9V3X3IBPStuTYIdijk0tB9B2uDrnFc5ytZjztcJ5gVU-B0rCSW5yYzCXMgcRscaVCcZVsEDgcXc0tnvlV9vDapF_E_V2sJgXGTaJK_opl6AWSqyy8me-BJLBpvEJPKoq8aD_yQazYYL1ZYN6iCYn_UlvYDfdHOwUnKbKDmmYgXFEqEskoU4mY5f7QShBqmRRzH0npSmhCViMQhAeCS8VXpB4GXESEgjhP0J7RVmIJzoaC8a8yJHS5SRykiQOUpL6YK3IJEyz1EJvNphji7pmBzO-ThyyGs8M8MwMntmFhY41creQut62GSiXM9awL4siKrlHk5QGDhGgzz0OpqJHstS0jycWeqlJg-mKGoUO2ZnxlVLs43jEulEMoMR3HAu9boBkCUSS8iYDAn6VLsLVgjxsQQLLp-3pDQWyDccwTyd-xiCyQwu92E7rlTqMrhDlSsMQMOkC8FFvhvFBB4Z6K4B5XBP19mz8GLx58CgsFLfIvXV47ZkiPzdFy3UBWgoS2UJvN5zx97vfjJ2n_31mz9Adz7Cv7lZyiPaq5Uo8B4OxSjpoN5pGHbTf7Q7HQ3g_7p9-GcFoL-x1zJ8wHSMn_gBGIGrU
linkProvider Scholars Portal
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwtV1Lb9QwELZKKx4XBOUVKGAQiCKImnWchw8V2pZWW_oQ2i6oN8tJ7DZiSZY6C9r-Mw78N8ZO0jZF5dbDSqt4nNeMZz7Hnm8QesUgqGQyFq5UoedSppjLVNJze0kUepJJFtdsn3vh4Av9dBAczKE_bS6M2VbZ-kTrqLMyNd_IV4jJa4vBIsMPkx-uqRplVlfbEhqiKa2QrVqKsSaxY1vOfsEUTq9ufQR9vyZkc2O0PnCbKgNuCmC-ckMWZhC0KetRRZmXqbgn_CBUYO1ZFAvfS1lKWQJIRkoqIklSSYKEZNRLaCClD6e9hhao-X4yjxbWNvY-D9tQANDIkv0Z1O9SQg7arJ04XNEQaGOTHE3h5_s996QTGW0BgX_DxLk4eXEP54WFXBsfN--g2w2wxf3aEu-iOVksout1qcvZIrqx2yzi30O_-4ad_DAfj6caq-l3Q_IB_7QBsAB8scCWPALC67J-i6sjUeEs15OxmGmcF1jnY7BenOQ2HwcLpXJwSzNc2Q3AGjpIvN8f7rvr5VeXYD3Jv8n6jNBZFBm2yTLmQuekJlpOs_Jnfgxmim2xFbhUVeLBxrYLUGWEzQKHvo9GV6HbB2i-KAv5yOwAg2Mk8pTqCRp5SRIHKU19QEgqCdMsddC7Vnl8UvOEcDu_ikNeq5qDqrlVNT9x0JrR76mk4fi2B8rjQ964DB5FTAnCkpQFHpWAIYgAeEpoltqS9dRBL411cMPiUZhtQodiqjXf2h_yfhSDKPU9z0FvGiFVgp2kosm6gKcyxF8dyaWOJLiZtNvcGiFv3JzmZ4PSQS9Om01Ps3WvkOXUyFCAkQHMiy-X8SHuhuZUIPOwtuvTd-PHlMYwi3FQ3LH4zsvrthT5kSVKN6S3DKKAg963g-Ps3i_XzuP_P-pzdHMw2t3hO1t720_QLWKHsCmRsoTmq-OpfAootUqeNb4AI37F3ucvn2CgeQ
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3db9MwELdgExMvCMZXYIBBSIAgWj6cxH4sY1XXwYTWMu3NchK7iyhJVadI3X_Gf8fZSUsz2AMPlar4nLS5893v5LufEXrNIKjkkgpXqthzCVPMZSr1XT9NYk8yyWjD9nkSD76R4Xl0vtHFb6vdV1uSTU-DYWkq6_1ZrpolTuN9DVGKms5iAp8w9N3Lm2ibRoxB-rXd6w1Hw5U3BnSSsFWzzD9ndgKS5e3_2ztvhKerpZNX9k9tWOrfRXdaPIl7jQHcQzdkuYtuNSdMLnfRzpd27_w--tUzpOCTYjpdaKwWPwy3BnzTBjcC3sQCW84GiGpv9TtcX4ga54WeTcVS46LEupiC0eC0sG0wWChVgDdY4trW3WqYIPGodzpyD6ozN8B6VnyXzR1hsihzbHtUzIM2pGZaLvLqZzEH68D2jBN4VF3hweGxCwhhjM2-gn6Axv3D8cHAbQ9ucDPIj2o3ZnEOOIgwnyjCvFxRX4RRrMCB5AkVoZexjLAUwKGURCQyyGQQpUFOvJREUoYP0VZZlfKxKbyCa0HiKeULknhpSqOMZCEAE5XGWZ456P1KeXzW0HNwm9bQmDeq5qBqblXNLx300eh3LWmote2Faj7h7UrlScKUCFiascgjEkJ3IAAVBiTP7EnxxEGvjHVwQ55RmuqciVhozY9Gp7yXUBAloec56E0rpCqwk0y0zQ7wrwzfVkdyryMJqzvrDq-MkLfeRfPA9HhS8M6xg16uh81MUzFXymphZAigtwjS0etlQgh3sbkVyDxq7Hr9bkIKiTskDw6iHYvvvLzuSFlcWH5ywzXLwPk66MNqcfz57ddr58n_ib9AO18_9fnno5Pjp-h2YFe0OahkD23V84V8BlixTp-37uA3N39iSg
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=Aspergillus+fumigatus+secretes+a+protease+that+displays+in+silico+binding+affinity+towards+the+SARS-CoV-2+spike+protein+and+mediates+SARS-CoV-2+pseudovirion+entry+into+HEK-293T+cells&rft.jtitle=Virology+journal&rft.au=Mjokane%2C+Nozethu&rft.au=Akintemi%2C+Eric+O&rft.au=Sabiu%2C+Saheed&rft.au=Gcilitshana%2C+Onele+M.+N&rft.date=2024-03-06&rft.pub=BioMed+Central+Ltd&rft.issn=1743-422X&rft.eissn=1743-422X&rft.volume=21&rft.issue=1&rft_id=info:doi/10.1186%2Fs12985-024-02331-z&rft.externalDocID=A785604300
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1743-422X&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1743-422X&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1743-422X&client=summon