Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation

Hsien Sheng Yin*, Xiaolin Wen, Reay G. Paterson, Robert A. Lamb, Theodore S. Jardetzky

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

325 Scopus citations

Abstract

Enveloped viruses have evolved complex glycoprotein machinery that drives the fusion of viral and cellular membranes, permitting entry of the viral genome into the cell. For the paramyxoviruses, the fusion (F) protein catalyses this membrane merger and entry step, and it has been postulated that the F protein undergoes complex refolding during this process. Here we report the crystal structure of the parainfluenza virus 5 F protein in its prefusion conformation, stabilized by the addition of a carboxy-terminal trimerization domain. The structure of the F protein shows that there are profound conformational differences between the pre- and postfusion states, involving transformations in secondary and tertiary structure. The positions and structural transitions of key parts of the fusion machinery, including the hydrophobic fusion peptide and two helical heptad repeat regions, clarify the mechanism of membrane fusion mediated by the F protein.

Original languageEnglish (US)
Pages (from-to)38-44
Number of pages7
JournalNature
Volume439
Issue number7072
DOIs
StatePublished - Jan 5 2006

ASJC Scopus subject areas

  • General

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