Palmitoylation of the influenza A virus M2 protein.
The M2 proteins of a variety of influenza A viruses of different subtypes were shown to possess associated palmitate. Susceptibility to removal by reduction or treatment with hydroxylamine is consistent with attachment via a thioester linkage to cysteine. The absence of the acyl group from the M2 proteins of several equine viruses of the H3N8 subtype correlates with the replacement of cysteine 50 with phenylalanine and points to this as the site of palmitate attachment.
Sugrue
R J
RJ
Virology Division, National Institute for Medical Research, Mill Hill, London, United Kingdom.
Belshe
R B
RB
Hay
A J
AJ
D000595:Amino Acid Sequence; D000818:Animals; D002642:Chick Embryo; D009980:Influenza A virus / Q000378:metabolism*; D008969:Molecular Sequence Data; D008970:Molecular Weight; D019308:Palmitic Acid; D010169:Palmitic Acids / Q000378:metabolism*; D012689:Sequence Homology, Nucleic Acid; D014763:Viral Matrix Proteins / Q000302:isolation & purification / Q000378:metabolism*; D000086082:Viroporin Proteins
D019308:Palmitic Acid; D010169:Palmitic Acids; D014763:Viral Matrix Proteins; C031540:M-protein, influenza virus; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins