Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel.

Virology ·Vol. 180 ·No. 2 ·1991-02-00 ·Pages 617-24

Sugrue RJ, Hay AJ

Abstract

The evidence presented shows that the M2 protein of influenza A viruses exists in infected cells as a homotetramer composed of two disulfide-linked dimers held together by noncovalent interactions. The amphiphilic nature of the transmembrane alpha-helical domain is consistent with the protein forming a transmembrane channel with which amantadine, the specific anti-influenza A drug, interacts. Together these features provide a structural basis for the hypothesis that M2 has a proton translocation function capable of regulating the pH of vesicles of the trans-Golgi network, a role important in promoting the correct maturation of the hemagglutinin glycoprotein.

MeSH Terms

Animals Cells, Cultured Centrifugation, Density Gradient Chick Embryo Chickens Ducks Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Influenza A virus/physiology Macromolecular Substances Models, Structural Molecular Weight Protein Conformation Viral Matrix Proteins/isolation & purification,metabolism

Chemicals

M-protein, influenza virus M2 protein, Influenza A virus Macromolecular Substances Viral Matrix Proteins

Authors & Affiliations

2 authors, click to expand affiliations / ORCID

Sugrue R J

National Institute for Medical Research, Mill Hill, London, United Kingdom.

Hay A J

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Article Info

Journal

Virology

Abbr.

Virology

ISSN

0042-6822

DOI

10.1016/0042-6822(91)90075-m

Published

1991-02-00

Pages

617-24

Language

English

Region

United States

NLM ID

0110674

PMCID

PMC7131614

Subset

External Links

PubMed source DOI: 10.1016/0042-6822(91)90075-m PMC Full Text View journal details

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Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel.

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