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J Gen Virol 72 (1991), 1461-1465; DOI 10.1099/0022-1317-72-6-1461
© 1991 Society for General Microbiology
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The M2 protein of influenza A virus is acylated

M. Veit1,2,, H.-D. Klenk1, A. Kendal1,{dagger} and R. Rott2

1 Institut für Virologie, Philipps-Universität Marburg, Robert-Koch-Strasse 17, D-3550 Marburg, Germany
and2 Institut für Virologie, Justus Liebig-Universität Giessen, Frankfurter Strasse 107, D-6300 Giessen, Germany

The M2 protein of influenza A virus, a 97 amino acid integral membrane protein expressed on the surface of infected cells, is covalently modified with long chain fatty acids. The fatty acid bond is sensitive to treatment with neutral hydroxylamine and mercaptoethanol, which indicates a labile thioester type linkage. Thinlayer chromatographic fatty acid analysis of [3H]myristic and [3H]palmitic acid-labelled M2 protein shows that palmitic acid is the predominant fatty acid linked to this polypeptide. Palmitoylation of M2 occurs post-translationally and causes an upward shift in the SDS-PAGE mobility of the protein.

{dagger} Permanent address: Centers for Disease Control, Center of Infectious Diseases, 1600 Clifton Road, N.E., Atlanta, Georgia 30333, U.S.A.

Received 4 December 1990; accepted 14 February 1991.


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Copyright © 1991 by the Society for General Microbiology.