tetano
Editor, Senior Moderator
First published September 2011, doi: 10.1128/JVI.05970-11 J. Virol. December 2011 vol. 85 no. 23 12179-12187
Mutations in the Membrane-Proximal Region of the Influenza A Virus M2 Protein Cytoplasmic Tail Have Modest Effects on Virus Replication
Shaun M. Stewart1,2 and
Andrew Pekosz1,*
+ Author Affiliations
1W. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins University, Bloomberg School of Public Health, 615 North Wolfe St., Suite 5132, Baltimore, Maryland 21205
2Division of Biology and Biomedical Sciences, Washington University in St. Louis, Campus Box 8226, 660 South Euclid St., St. Louis, Missouri 63110
ABSTRACT
Influenza A virus encodes M2, a proton channel that has been shown to be important during virus entry and assembly. In order to systematically investigate the role of the membrane-proximal residues in the M2 cytoplasmic tail in virus replication, we utilized scanning and directed alanine mutagenesis in combination with transcomplementation assays and recombinant viruses. The membrane-proximal residues 46 to 69 tolerated numerous mutations, with little, if any, effect on virus replication, suggesting that protein structure rather than individual amino acid identity in this region may be critical for M2 protein function.
http://jvi.asm.org/content/85/23/12179.short?rss=1
Mutations in the Membrane-Proximal Region of the Influenza A Virus M2 Protein Cytoplasmic Tail Have Modest Effects on Virus Replication
Shaun M. Stewart1,2 and
Andrew Pekosz1,*
+ Author Affiliations
1W. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins University, Bloomberg School of Public Health, 615 North Wolfe St., Suite 5132, Baltimore, Maryland 21205
2Division of Biology and Biomedical Sciences, Washington University in St. Louis, Campus Box 8226, 660 South Euclid St., St. Louis, Missouri 63110
ABSTRACT
Influenza A virus encodes M2, a proton channel that has been shown to be important during virus entry and assembly. In order to systematically investigate the role of the membrane-proximal residues in the M2 cytoplasmic tail in virus replication, we utilized scanning and directed alanine mutagenesis in combination with transcomplementation assays and recombinant viruses. The membrane-proximal residues 46 to 69 tolerated numerous mutations, with little, if any, effect on virus replication, suggesting that protein structure rather than individual amino acid identity in this region may be critical for M2 protein function.
http://jvi.asm.org/content/85/23/12179.short?rss=1