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Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein.

Identifieur interne : 002275 ( PubMed/Checkpoint ); précédent : 002274; suivant : 002276

Biochemical and functional characterization of the membrane association and membrane permeabilizing activity of the severe acute respiratory syndrome coronavirus envelope protein.

Auteurs : Y. Liao [Singapour] ; Q. Yuan ; J. Torres ; J P Tam ; D X Liu

Source :

RBID : pubmed:16507314

Descripteurs français

English descriptors

Abstract

A diverse group of cytolytic animal viruses encodes small, hydrophobic proteins to modify host cell membrane permeability to ions and small molecules during their infection cycles. In this study, we show that expression of the SARS-CoV E protein in mammalian cells alters the membrane permeability of these cells. Immunofluorescent staining and cell fractionation studies demonstrate that this protein is an integral membrane protein. It is mainly localized to the ER and the Golgi apparatus. The protein can be translocated to the cell surface and is partially associated with lipid rafts. Further biochemical characterization of the protein reveals that it is posttranslationally modified by palmitoylation on all three cysteine residues. Systematic mutagenesis studies confirm that the membrane permeabilizing activity of the SARS-CoV E protein is associated with its transmembrane domain.

DOI: 10.1016/j.virol.2006.01.028
PubMed: 16507314


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pubmed:16507314

Le document en format XML

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