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• W2022271413 abstract "To enter cells, enveloped viruses use fusion-mediating glycoproteins to facilitate the merger of the viral and host cell membranes. These glycoproteins undergo large-scale irreversible refolding during membrane fusion. The paramyxovirus parainfluenza virus 5 mediates membrane merger through its fusion protein (F). The transmembrane (TM) domains of viral fusion proteins are typically required for fusion. The TM domain of F is particularly interesting in that it is potentially unusually long; multiple calculations suggest a TM helix length between 25 and 48 residues. Oxidative cross-linking of single-cysteine substitutions indicates the F TM trimer forms a helical bundle within the membrane. To assess the functional role of the paramyxovirus parainfluenza virus 5 F protein TM domain, alanine scanning mutagenesis was performed. Two residues located in the outer leaflet of the bilayer are critical for fusion. Multiple amino acid substitutions at these positions indicate the physical properties of the side chain play a critical role in supporting or blocking fusion. Analysis of intermediate steps in F protein refolding indicated that the mutants were not trapped at the open stalk intermediate or the prehairpin intermediate. Incorporation of a known F protein destabilizing mutation that causes a hyperfusogenic phenotype restored fusion activity to the mutants. Further, altering the curvature of the lipid bilayer by addition of oleic acid promoted fusion of the F protein mutants. In aggregate, these data indicate that the TM domain plays a functional role in fusion beyond merely anchoring the protein in the viral envelope and that it can affect the structures and steady-state concentrations of the various conformational intermediates en route to the final postfusion state. We suggest that the unusual length of this TM helix might allow it to serve as a template for formation of or specifically stabilize the lipid stalk intermediate in fusion." @default.
• W2022271413 created "2016-06-24" @default.
• W2022271413 creator A5021623971 @default.
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• W2022271413 creator A5077136795 @default.
• W2022271413 creator A5081695483 @default.
• W2022271413 date "2009-02-01" @default.
• W2022271413 modified "2023-10-10" @default.
• W2022271413 title "Functional Analysis of the Transmembrane Domain in Paramyxovirus F Protein-Mediated Membrane Fusion" @default.
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• W2022271413 doi "https://doi.org/10.1016/j.jmb.2008.12.029" @default.
• W2022271413 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2750892" @default.
• W2022271413 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/19121325" @default.
• W2022271413 hasPublicationYear "2009" @default.
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