title: Mutations in the membrane-proximal region of the influenza A virus M2 protein cytoplasmic tail have modest effects on virus replication.
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.
authors.affiliation: W. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins University, Bloomberg School of Public Health, 615 North Wolfe St., Suite 5132, Baltimore, MD 21205, USA.
authors.forename: Shaun M
authors.initials: SM
authors.lastname: Stewart
authors.forename: Andrew
authors.initials: A
authors.lastname: Pekosz
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002462:Cell Membrane / Q000378:metabolism*; D002478:Cells, Cultured; D003593:Cytoplasm / Q000378:metabolism*; D004285:Dogs; D053122:Influenza A Virus, H3N2 Subtype / Q000235:genetics*; D007668:Kidney / Q000166:cytology / Q000378:metabolism / Q000821:virology; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D009154:Mutation / Q000235:genetics*; D009976:Orthomyxoviridae Infections / Q000235:genetics / Q000378:metabolism / Q000821:virology; D010957:Plasmids; D017386:Sequence Homology, Amino Acid; D014763:Viral Matrix Proteins / Q000235:genetics* / Q000378:metabolism; D019065:Virus Assembly; D014779:Virus Replication; D000086082:Viroporin Proteins
chemical_list: D014763:Viral Matrix Proteins; C488937:M2 protein, Influenza A virus; D000086082:Viroporin Proteins