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Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
The influenza M2 protein not only forms a proton channel but also mediates membrane scission in a cholesterol-dependent manner to cause virus budding and release. The atomic interaction of cholesterol with M2, as with most eukaryotic membrane proteins, has long been elusive. We have now determined the cholesterol-binding site of the M2 protein in phospholipid bilayers using solid-state NMR spectroscopy. Chain-fluorinated cholesterol was used to measure cholesterol proximity to M2 while sterol-deuterated cholesterol was used to measure bound-cholesterol orientation in lipid bilayers. Carbon-fluorine distance measurements show that at a cholesterol concentration of 17 mol%, two cholesterol molecules bind each M2 tetramer. Cholesterol binds the C-terminal transmembrane (TM) residues, near an amphipathic helix, without requiring a cholesterol recognition sequence motif. Deuterium NMR spectra indicate that bound cholesterol is approximately parallel to the bilayer normal, with the rough face of the sterol rings apposed to methyl-rich TM residues. The distance- and orientation-restrained cholesterol-binding site structure shows that cholesterol is stabilized by hydrophobic interactions with the TM helix and polar and aromatic interactions with neighboring amphipathic helices. At the 1:2 binding stoichiometry, lipid P spectra show an isotropic peak indicative of high membrane curvature. This M2-cholesterol complex structure, together with previously observed M2 localization at phase boundaries, suggests that cholesterol mediates M2 clustering to the neck of the budding virus to cause the necessary curvature for membrane scission. The solid-state NMR approach developed here is generally applicable for elucidating the structural basis of cholesterol's effects on membrane protein function.
Authors : Elkins Matthew R , Williams Jonathan K , Gelenter Martin D , Dai Peng , Kwon Byungsu , Sergeyev Ivan V , Pentelute Bradley L , Hong Mei ,
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Pathways :
WP1438: Influenza A virus infection
WP1531: Vitamin D synthesis
WP1616: ABC transporters
WP2011: SREBF and miR33 in cholesterol and lipid homeostasis
WP2084: SREBF and miR33 in cholesterol and lipid homeostasis
WP2292: Chemokine signaling pathway
WP731: Sterol regulatory element binding protein related
WP103: Cholesterol Biosynthesis
WP1049: G Protein Signaling Pathways
WP1070: Cholesterol Biosynthesis
WP1099: Nuclear receptors in lipid metabolism and toxicity
WP114: Core lipid-linked oligosaccharide biosynthesis
WP1165: G Protein Signaling Pathways
WP1186: Cholesterol Biosynthesis
WP132: Cholesterol Biosynthesis
WP1326: Nuclear receptors in lipid metabolism and toxicity
WP1371: G Protein Signaling Pathways
WP1387: Cholesterol Biosynthesis
WP139: Nuclear receptors in lipid metabolism and toxicity
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1624: Bacterial secretion system
WP1625: Base excision repair
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Bibliography :
[29158386] Cholesterol-binding site of the influenza M2 protein in lipid bilayers from solid-state NMR.
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