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Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.

Identifieur interne : 003152 ( Main/Exploration ); précédent : 003151; suivant : 003153

Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide.

Auteurs : Berend Jan Bosch [Pays-Bas] ; Willem Bartelink ; Peter J M. Rottier

Source :

RBID : pubmed:18562523

Descripteurs français

English descriptors

Abstract

Unlike other class I viral fusion proteins, spike proteins on severe acute respiratory syndrome coronavirus virions are uncleaved. As we and others have demonstrated, infection by this virus depends on cathepsin proteases present in endosomal compartments of the target cell, suggesting that the spike protein acquires its fusion competence by cleavage during cell entry rather than during virion biogenesis. Here we demonstrate that cathepsin L indeed activates the membrane fusion function of the spike protein. Moreover, cleavage was mapped to the same region where, in coronaviruses carrying furin-activated spikes, the receptor binding subunit of the protein is separated from the membrane-anchored fusion subunit.

DOI: 10.1128/JVI.00415-08
PubMed: 18562523


Affiliations:


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Le document en format XML

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