Giuseppe
Emeritus
J Virol. 2009 Jun 24. [Epub ahead of print]
Palmitoylation of the influenza A virus M2 protein is not required for virus replication in vitro but contributes to virus virulence.
Grantham ML, Wu WH, Lalime EN, Lorenzo ME, Klein SL, Pekosz A. W. Harry Feinstone Department of Molecular Microbiology and Immunology, Department of Biochemistry and Molecular Biology, Johns Hopkins University, Bloomberg School of Public Health, 615 North Wolfe St, Suite 5132, Baltimore, MD, USA, 21205; Department of Molecular and Comparative Pathobiology, The Johns Hopkins University School of Medicine, Baltimore, MD, USA, 21204.
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, CaLu3 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 there may be novel functions for M2 palmitoylation during in vivo infection.
PMID: 19553312 [PubMed - as supplied by publisher]
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Palmitoylation of the influenza A virus M2 protein is not required for virus replication in vitro but contributes to virus virulence.
Grantham ML, Wu WH, Lalime EN, Lorenzo ME, Klein SL, Pekosz A. W. Harry Feinstone Department of Molecular Microbiology and Immunology, Department of Biochemistry and Molecular Biology, Johns Hopkins University, Bloomberg School of Public Health, 615 North Wolfe St, Suite 5132, Baltimore, MD, USA, 21205; Department of Molecular and Comparative Pathobiology, The Johns Hopkins University School of Medicine, Baltimore, MD, USA, 21204.
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, CaLu3 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 there may be novel functions for M2 palmitoylation during in vivo infection.
PMID: 19553312 [PubMed - as supplied by publisher]
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