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J Virol. 2009 Sep;83(17):8655-61. doi: 10.1128/JVI.01129-09. Epub 2009 Jun 24.

Palmitoylation of the influenza A virus M2 protein is not required for virus replication in vitro but contributes to virus virulence.

Author information

1
W. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins University, Bloomberg School of Public Health, 615 North Wolfe St., Baltimore, MD 21205, USA.

Abstract

The influenza A virus M2 protein has important roles during virus entry and in the assembly of infectious virus particles. The cytoplasmic tail of the protein can be palmitoylated at a cysteine residue, but this residue is not conserved in a number of human influenza A virus isolates. Recombinant viruses encoding M2 proteins with a serine substituted for the cysteine at position 50 were generated in the A/WSN/33 (H1N1) and A/Udorn/72 (H3N2) genetic backgrounds. The recombinant viruses were not attenuated for replication in MDCK cells, Calu-3 cells, or in primary differentiated murine trachea epithelial cell cultures, indicating there was no significant contribution of M2 palmitoylation to virus replication in vitro. The A/WSN/33 M2C50S virus displayed a slightly reduced virulence after infection of mice, suggesting that there may be novel functions for M2 palmitoylation during in vivo infection.

PMID:
19553312
PMCID:
PMC2738213
DOI:
10.1128/JVI.01129-09
[Indexed for MEDLINE]
Free PMC Article

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