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Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity.

Identifieur interne : 006583 ( Main/Exploration ); précédent : 006582; suivant : 006584

Proteolytic cleavage of the murine coronavirus surface glycoprotein is not required for fusion activity.

Auteurs : R. Stauber [Allemagne] ; M. Pfleiderera ; S. Siddell

Source :

RBID : pubmed:8381459

Descripteurs français

English descriptors

Abstract

A cDNA copy of the murine coronavirus [otherwise known as murine hepatitis virus (MHV)] surface (S) glycoprotein gene was isolated and expressed in DBT cells by using a recombinant vaccinia virus system. The expressed S protein induced extensive syncytium formation at neutral pH. Oligonucleotide mutagenesis was used to engineer an S protein gene in which codons for the proteolytic cleavage site, Arg-Arg-Ala-Arg-Arg, were replaced with an equal number of codons for amino acids with aliphatic or aliphatic hydroxyl side-chains. The mutated S protein was stably expressed in DBT cells and, in contrast to the wild-type protein, was not proteolytically cleaved. Nevertheless, the non-cleaved protein induced extensive syncytium formation. These results clearly indicate that the non-cleaved form of the MHV S protein is able to mediate cell membrane fusion. Thus proteolytic cleavage is not an absolute requirement for fusion activity.

DOI: 10.1099/0022-1317-74-2-183
PubMed: 8381459


Affiliations:


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