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

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.

journal_name

Nature

journal_title

Nature

authors

Gibbons DL,Vaney MC,Roussel A,Vigouroux A,Reilly B,Lepault J,Kielian M,Rey FA

doi

10.1038/nature02239

keywords:

subject

Has Abstract

pub_date

2004-01-22 00:00:00

pages

320-5

issue

6972

eissn

0028-0836

issn

1476-4687

pii

nature02239

journal_volume

427

pub_type

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