Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel
- PMID: 1989386
- PMCID: PMC7131614
- DOI: 10.1016/0042-6822(91)90075-m
Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel
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.
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