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...
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Published in | Virology journal Vol. 21; no. 1; p. 58 |
---|---|
Main Authors | , , , , , , |
Format | Journal Article |
Language | English |
Published |
London
BioMed Central
06.03.2024
BioMed Central Ltd BMC |
Subjects | |
Online Access | Get full text |
ISSN | 1743-422X 1743-422X |
DOI | 10.1186/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 |
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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 |
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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 |
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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 |
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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 |
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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... |
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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 |
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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 |
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