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- W3094879454 abstract "The interferon-inducible transmembrane (IFITM) proteins belong to the Dispanin/CD225 family and inhibit diverse virus infections. IFITM3 reduces membrane fusion between cells and virions through a poorly characterized mechanism. Mutation of proline-rich transmembrane protein 2 (PRRT2), a regulator of neurotransmitter release, at glycine-305 was previously linked to paroxysmal neurological disorders in humans. Here, we show that glycine-305 and the homologous site in IFITM3, glycine-95, drive protein oligomerization from within a GxxxG motif. Mutation of glycine-95 (and to a lesser extent, glycine-91) disrupted IFITM3 oligomerization and reduced its antiviral activity against Influenza A virus. An oligomerization-defective variant was used to reveal that IFITM3 promotes membrane rigidity in a glycine-95-dependent and amphipathic helix-dependent manner. Furthermore, a compound which counteracts virus inhibition by IFITM3, Amphotericin B, prevented the IFITM3-mediated rigidification of membranes. Overall, these data suggest that IFITM3 oligomers inhibit virus-cell fusion by promoting membrane rigidity." @default.
- W3094879454 created "2020-11-09" @default.
- W3094879454 creator A5003933887 @default.
- W3094879454 creator A5020346922 @default.
- W3094879454 creator A5024498144 @default.
- W3094879454 creator A5030393489 @default.
- W3094879454 creator A5078852696 @default.
- W3094879454 creator A5090656792 @default.
- W3094879454 date "2020-10-28" @default.
- W3094879454 modified "2023-10-03" @default.
- W3094879454 title "Homology-guided identification of a conserved motif linking the antiviral functions of IFITM3 to its oligomeric state" @default.
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- W3094879454 doi "https://doi.org/10.7554/elife.58537" @default.
- W3094879454 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7665892" @default.
- W3094879454 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/33112230" @default.
- W3094879454 hasPublicationYear "2020" @default.
- W3094879454 type Work @default.