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Influenza Virus M2 Ion Channel Protein is Necessary for Filamentous Virion Formation. (J Virol., abstract, edited)
[Source: US National Library of Medicine: LINK. EDITED.]
J Virol. 2010 Mar 10. [Epub ahead of print]
Influenza Virus M2 Ion Channel Protein is Necessary for Filamentous Virion Formation.
Rossman JS, Jing X, Leser GP, Balannik V, Pinto LH, Lamb RA. - Department of Biochemistry, Molecular Biology, and Cell Biology and Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500; Department of Neurobiology and Physiology, Northwestern University, Evanston, IL 60208-3500.
Influenza A virus buds from cells as spherical ( approximately 100 nm diameter) and filamentous ( approximately 100 nm x 2-20 mum) virions. Previous work has determined that the matrix protein (M1) confers the ability of the virus to form filaments; however, additional work has suggested that the influenza virus M2 integral membrane protein also plays a role in viral filament formation. In examining the role of the M2 protein in filament formation, we observed that the cytoplasmic tail of M2 contains several sites that are essential for filament formation. Additionally, whereas M2 is a non-raft protein, expression of other viral proteins, in the context of influenza virus infection, leads to the colocalization of M2 with sites of virus budding and lipid raft domains. We find that an amphipathic helix, located within the M2 cytoplasmic tail, is able to bind cholesterol and we speculate that M2 cholesterol-binding is essential for both filament formation as well as the stability of existing viral filaments.
PMID: 20219914 [PubMed - as supplied by publisher]
J Virol. 2010 Mar 10. [Epub ahead of print]
Influenza Virus M2 Ion Channel Protein is Necessary for Filamentous Virion Formation.
Rossman JS, Jing X, Leser GP, Balannik V, Pinto LH, Lamb RA. - Department of Biochemistry, Molecular Biology, and Cell Biology and Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208-3500; Department of Neurobiology and Physiology, Northwestern University, Evanston, IL 60208-3500.
Influenza A virus buds from cells as spherical ( approximately 100 nm diameter) and filamentous ( approximately 100 nm x 2-20 mum) virions. Previous work has determined that the matrix protein (M1) confers the ability of the virus to form filaments; however, additional work has suggested that the influenza virus M2 integral membrane protein also plays a role in viral filament formation. In examining the role of the M2 protein in filament formation, we observed that the cytoplasmic tail of M2 contains several sites that are essential for filament formation. Additionally, whereas M2 is a non-raft protein, expression of other viral proteins, in the context of influenza virus infection, leads to the colocalization of M2 with sites of virus budding and lipid raft domains. We find that an amphipathic helix, located within the M2 cytoplasmic tail, is able to bind cholesterol and we speculate that M2 cholesterol-binding is essential for both filament formation as well as the stability of existing viral filaments.
PMID: 20219914 [PubMed - as supplied by publisher]