Abstract：
:Alphaviruses infect cells via a low-pH-triggered membrane fusion reaction mediated by the class II virus fusion protein E1, an elongated molecule with three extramembrane domains (DI-III). E1 drives fusion by inserting its fusion peptide loop into the target membrane and refolding to a hairpin-like trimer in which DIII moves toward the target membrane and packs against the central trimer. Three-dimensional structures provide static pictures of prefusion and postfusion E1 but do not explain this transition. Using truncated forms of E1, we reconstituted a low-pH-dependent intermediate composed of trimers of DI/II. Unexpectedly, DI/II trimers were stable in the absence of DIII. Once formed at a low pH, DI/II trimers efficiently and specifically bound recombinant DIII through a pH-independent reaction. Even in the absence of DIII, DI/II trimers interacted to form hexagonal lattices and to cause membrane deformation and tubulation. These studies identify a prefusion intermediate in class II membrane fusion.
journal_name
Cell Host Microbejournal_title
Cell host & microbeauthors
Sánchez-San Martín C,Sosa H,Kielian Mdoi
10.1016/j.chom.2008.10.012subject
Has Abstractpub_date
2008-12-11 00:00:00pages
600-8issue
6eissn
1931-3128issn
1934-6069pii
S1931-3128(08)00360-0journal_volume
4pub_type
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