Conformational states of the severe acute respiratory syndrome coronavirus spike protein ectodomain

Fang Li, Marcelo Berardi, Wenhui Li, Michael Farzan, Philip R. Dormitzer, Stephen C. Harrison

Research output: Contribution to journalArticlepeer-review

69 Scopus citations

Abstract

The severe acute respiratory syndrome coronavirus enters cells through the activities of a spike protein (S) which has receptor-binding (S1) and membrane fusion (S2) regions. We have characterized four sequential states of a purified recombinant S ectodomain (S-e) comprising S1 and the ectodomain of S2. They are S-e monomers, uncleaved S-e trimers, cleaved S-e trimers, and dissociated S1 monomers and S2 trimer rosettes. Lowered pH induces an irreversible transition from flexible, L-shaped S-e monomers to clove-shaped trimers. Protease cleavage of the trimer occurs at the S1-S2 boundary; an ensuing S1 dissociation leads to a major rearrangement of the trimeric S2 and to formation of rosettes likely to represent clusters of elongated, postfusion trimers of S2 associated through their fusion peptides. The states and transitions of S suggest conformational changes that mediate viral entry into cells.

Original languageEnglish (US)
Pages (from-to)6794-6800
Number of pages7
JournalJournal of virology
Volume80
Issue number14
DOIs
StatePublished - Jul 2006

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