Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus

Don L. Gibbons, Marie Christine Vaney, Alain Roussel, Armelle Vigouroux, Brigid Reilly, Jean Lepault, Margaret Kielian, Félix A. Rey

Research output: Contribution to journalArticle

277 Scopus citations

Abstract

Fusion of biological membranes is mediated by specific lipid-interacting proteins that induce the formation and expansion of an initial fusion pore. Here we report the crystal structure of the ectodomain of the Semliki Forest virus fusion glycoprotein E1 in its low-pH-induced trimeric form. E1 adopts a folded-back conformation that, in the final post-fusion form of the full-length protein, would bring the fusion peptide loop and the transmembrane anchor to the same end of a stable protein rod. The observed conformation of the fusion peptide loop is compatible with interactions only with the outer leaflet of the lipid bilayer. Crystal contacts between fusion peptide loops of adjacent E1 trimers, together with electron microscopy observations, suggest that in an early step of membrane fusion, an intermediate assembly of five trimers creates two opposing nipple-like deformations in the viral and target membranes, leading to formation of the fusion pore.

Original languageEnglish (US)
Pages (from-to)320-325
Number of pages6
JournalNature
Volume427
Issue number6972
DOIs
StatePublished - Jan 22 2004

ASJC Scopus subject areas

  • General

Fingerprint Dive into the research topics of 'Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus'. Together they form a unique fingerprint.

  • Cite this

    Gibbons, D. L., Vaney, M. C., Roussel, A., Vigouroux, A., Reilly, B., Lepault, J., Kielian, M., & Rey, F. A. (2004). Conformational change and protein-protein interactions of the fusion protein of Semliki Forest virus. Nature, 427(6972), 320-325. https://doi.org/10.1038/nature02239