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• W2783137619 endingPage "709" @default.
• W2783137619 startingPage "695" @default.
• W2783137619 abstract "Enveloped viruses enter cells by using their fusion proteins to merge the virus lipid envelope and the cell membrane. While crystal structures of the water-soluble ectodomains of many viral fusion proteins have been determined, the structure and assembly of the C-terminal transmembrane domain (TMD) remains poorly understood. Here we use solid-state NMR to determine the backbone conformation and oligomeric structure of the TMD of the parainfluenza virus 5 fusion protein. 13C chemical shifts indicate that the central leucine-rich segment of the TMD is α-helical in POPC/cholesterol membranes and POPE membranes, while the Ile- and Val-rich termini shift to the β-strand conformation in the POPE membrane. Importantly, lipid mixing assays indicate that the TMD is more fusogenic in the POPE membrane than in the POPC/cholesterol membrane, indicating that the β-strand conformation is important for fusion by inducing membrane curvature. Incorporation of para-fluorinated Phe at three positions of the α-helical core allowed us to measure interhelical distances using 19F spin diffusion NMR. The data indicate that, at peptide:lipid molar ratios of ~ 1:15, the TMD forms a trimeric helical bundle with inter-helical distances of 8.2–8.4 Å for L493F and L504F and 10.5 Å for L500F. These data provide high-resolution evidence of trimer formation of a viral fusion protein TMD in phospholipid bilayers, and indicate that the parainfluenza virus 5 fusion protein TMD harbors two functions: the central α-helical core is the trimerization unit of the protein, while the two termini are responsible for inducing membrane curvature by transitioning to a β-sheet conformation." @default.
• W2783137619 created "2018-01-26" @default.
• W2783137619 creator A5007765901 @default.
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• W2783137619 date "2018-03-01" @default.
• W2783137619 modified "2023-10-14" @default.
• W2783137619 title "Conformation and Trimer Association of the Transmembrane Domain of the Parainfluenza Virus Fusion Protein in Lipid Bilayers from Solid-State NMR: Insights into the Sequence Determinants of Trimer Structure and Fusion Activity" @default.
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• W2783137619 doi "https://doi.org/10.1016/j.jmb.2018.01.002" @default.
• W2783137619 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5831503" @default.
• W2783137619 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/29330069" @default.
• W2783137619 hasPublicationYear "2018" @default.
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