Open AccessReversible Inhibition of Fusion Activity of a Paramyxovirus Fusion Protein by an Engineered Disulfide Bond in the Membrane-Proximal External Region
Author(s) -
Aarohi Zokarkar,
Sarah A. Connolly,
Theodore S. Jardetzky,
Robert A. Lamb
Publication year - 2012
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.02006-12
Subject(s) - fusion , lipid bilayer fusion , biology , disulfide bond , mutant , fusion protein , biophysics , microbiology and biotechnology , cell fusion , membrane , crystallography , biochemistry , chemistry , cell , recombinant dna , gene , philosophy , linguistics
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 separate for F to be able to refold and cause fusion.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom