Structural characteristics of the M2 protein of influenza A viruses: evidence that it forms a tetrameric channel.
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.
Sugrue
R J
RJ
National Institute for Medical Research, Mill Hill, London, United Kingdom.
Hay
A J
AJ
D000818:Animals; D002478:Cells, Cultured; D002499:Centrifugation, Density Gradient; D002642:Chick Embryo; D002645:Chickens; D004372:Ducks; D015180:Electrophoresis, Gel, Two-Dimensional; D004591:Electrophoresis, Polyacrylamide Gel; D009980:Influenza A virus / Q000502:physiology*; D046911:Macromolecular Substances; D008961:Models, Structural; D008970:Molecular Weight; D011487:Protein Conformation; D014763:Viral Matrix Proteins / Q000302:isolation & purification* / Q000378:metabolism; D000086082:Viroporin Proteins
D046911:Macromolecular Substances; D014763:Viral Matrix Proteins; C031540:M-protein, influenza virus; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins