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- Title
Solution structure and functional analysis of the influenza B proton channel.
- Authors
Junfeng Wang; Pielak, Rafal M.; McClintock, Mark A.; Chou, James J.
- Abstract
Influenza B virus contains an integral membrane protein, BM2, that oligomerizes in the viral membrane to form a pH-activated proton channel. Here we report the solution structures of both the membrane-embedded channel domain and the cytoplasmic domain of BM2. The channel domain assumes a left-handed coiled-coil tetramer formation with a helical packing angle of −37° to form a polar pore in the membrane for conducting ions. Mutagenesis and proton flux experiments identified residues involved in proton relay and suggest a mechanism of proton conductance. The cytoplasmic domain of BM2 also forms a coiled-coil tetramer. It has a bipolar charge distribution, in which a negatively charged region interacts specifically with the M1 matrix protein that is involved in packaging the genome in the virion. This interaction suggests BM2 also recruits matrix proteins to the cell surface during virus budding, making BM2 an unusual membrane protein with the dual roles of conducting ions and recruiting proteins to the membrane.
- Subjects
INFLUENZA B virus; PROTONS; MEMBRANE proteins; VIRAL envelopes; MUTAGENESIS; CELL membranes
- Publication
Nature Structural & Molecular Biology, 2009, Vol 16, Issue 12, p1267
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb.1707