SrasV1, PubMed, Corpus, bibRecord, 000B09

Different residues in the SARS-CoV spike protein determine cleavage and activation by the host cell protease TMPRSS2.

Identifieur interne : 000B09 ( PubMed/Corpus ); précédent : 000B08; suivant : 000B10

Different residues in the SARS-CoV spike protein determine cleavage and activation by the host cell protease TMPRSS2.

Auteurs : Lennart Michel Reinke ; Martin Spiegel ; Teresa Plegge ; Anika Hartleib ; Inga Nehlmeier ; Stefanie Gierer ; Markus Hoffmann ; Heike Hofmann-Winkler ; Michael Winkler ; Stefan Pöhlmann

Source :

PloS one [ 1932-6203 ] ; 2017.

RBID : pubmed:28636671

English descriptors

KwdEn :
- HEK293 Cells, Host-Pathogen Interactions, Humans, Mutation (genetics), Protein Transport, Serine Endopeptidases (genetics), Serine Endopeptidases (metabolism), Spike Glycoprotein, Coronavirus (genetics), Spike Glycoprotein, Coronavirus (metabolism), Virus Internalization.
MESH :
- chemical , genetics : Serine Endopeptidases, Spike Glycoprotein, Coronavirus.
- genetics : Mutation.
- chemical , metabolism : Serine Endopeptidases, Spike Glycoprotein, Coronavirus.
- HEK293 Cells, Host-Pathogen Interactions, Humans, Protein Transport, Virus Internalization.

Abstract

The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) mediates viral entry into target cells. Cleavage and activation of SARS S by a host cell protease is essential for infectious viral entry and the responsible enzymes are potential targets for antiviral intervention. The type II transmembrane serine protease TMPRSS2 cleaves and activates SARS S in cell culture and potentially also in the infected host. Here, we investigated which determinants in SARS S control cleavage and activation by TMPRSS2. We found that SARS S residue R667, a previously identified trypsin cleavage site, is also required for S protein cleavage by TMPRSS2. The cleavage fragments produced by trypsin and TMPRSS2 differed in their decoration with N-glycans, suggesting that these proteases cleave different SARS S glycoforms. Although R667 was required for SARS S cleavage by TMPRSS2, this residue was dispensable for TMPRSS2-mediated S protein activation. Conversely, residue R797, previously reported to be required for SARS S activation by trypsin, was dispensable for S protein cleavage but required for S protein activation by TMPRSS2. Collectively, these results show that different residues in SARS S control cleavage and activation by TMPRSS2, suggesting that these processes are more complex than initially appreciated.

DOI: 10.1371/journal.pone.0179177
PubMed: 28636671

Links to Exploration step

pubmed:28636671

Le document en format XML

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<front><div type="abstract" xml:lang="en">The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) mediates viral entry into target cells. Cleavage and activation of SARS S by a host cell protease is essential for infectious viral entry and the responsible enzymes are potential targets for antiviral intervention. The type II transmembrane serine protease TMPRSS2 cleaves and activates SARS S in cell culture and potentially also in the infected host. Here, we investigated which determinants in SARS S control cleavage and activation by TMPRSS2. We found that SARS S residue R667, a previously identified trypsin cleavage site, is also required for S protein cleavage by TMPRSS2. The cleavage fragments produced by trypsin and TMPRSS2 differed in their decoration with N-glycans, suggesting that these proteases cleave different SARS S glycoforms. Although R667 was required for SARS S cleavage by TMPRSS2, this residue was dispensable for TMPRSS2-mediated S protein activation. Conversely, residue R797, previously reported to be required for SARS S activation by trypsin, was dispensable for S protein cleavage but required for S protein activation by TMPRSS2. Collectively, these results show that different residues in SARS S control cleavage and activation by TMPRSS2, suggesting that these processes are more complex than initially appreciated.</div>
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<Abstract><AbstractText>The spike (S) protein of severe acute respiratory syndrome coronavirus (SARS-CoV) mediates viral entry into target cells. Cleavage and activation of SARS S by a host cell protease is essential for infectious viral entry and the responsible enzymes are potential targets for antiviral intervention. The type II transmembrane serine protease TMPRSS2 cleaves and activates SARS S in cell culture and potentially also in the infected host. Here, we investigated which determinants in SARS S control cleavage and activation by TMPRSS2. We found that SARS S residue R667, a previously identified trypsin cleavage site, is also required for S protein cleavage by TMPRSS2. The cleavage fragments produced by trypsin and TMPRSS2 differed in their decoration with N-glycans, suggesting that these proteases cleave different SARS S glycoforms. Although R667 was required for SARS S cleavage by TMPRSS2, this residue was dispensable for TMPRSS2-mediated S protein activation. Conversely, residue R797, previously reported to be required for SARS S activation by trypsin, was dispensable for S protein cleavage but required for S protein activation by TMPRSS2. Collectively, these results show that different residues in SARS S control cleavage and activation by TMPRSS2, suggesting that these processes are more complex than initially appreciated.</AbstractText>
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Different residues in the SARS-CoV spike protein determine cleavage and activation by the host cell protease TMPRSS2.

Different residues in the SARS-CoV spike protein determine cleavage and activation by the host cell protease TMPRSS2.

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