Structure of a flavivirus envelope glycoprotein in its low-pH-induced membrane fusion conformation.

ABSTRACT: Enveloped viruses enter cells via a membrane fusion reaction driven by conformational changes of specific viral envelope proteins. We report here the structure of the ectodomain of the tick-borne encephalitis virus envelope glycoprotein, E, a prototypical class II fusion protein, in its trimeric low-pH-induced conformation. We show that, in the conformational transition, the three domains of the neutral-pH form are maintained but their relative orientation is altered. Similar to the postfusion class I proteins, the subunits rearrange such that the fusion peptide loops cluster at one end of an elongated molecule and the C-terminal segments, connecting to the viral transmembrane region, run along the sides of the trimer pointing toward the fusion peptide loops. Comparison with the low-pH-ind

SUBMITTER: Bressanelli S 

PROVIDER: S-EPMC380989 | biostudies-literature | 2004 Feb

REPOSITORIES: biostudies-literature