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Article

Reversible inhibition of fusion activity of a paramyxovirus fusion protein by an engineered disulfide bond in the membrane-proximal external region.

Journal of virology - 1 Nov 2012

Zokarkar Aarohi, Connolly Sarah A, Jardetzky Theodore S, Lamb Robert A

Abstract excerpt

Cysteines were introduced into the membrane-proximal external region (MPER) of the paramyxovirus F protein. A disulfide bond formed, and the mutant protein was expressed at the cell surface but was fusion inactive. Reduction of the disulfide bond restored fusion activity. The data indicate that in addition to dissociation of the three-helix bundle stalk domain of prefusion F, the MPER region also needs to...

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Identifiers

PMID: 22951841
DOI: 10.1128/JVI.02006-12
PMCID: PMC3486459

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