Reversible Inhibition of Fusion Activity of a Paramyxovirus Fusion Protein by an Engineered Disulfide Bond in the Membrane-Proximal External Region |
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| Authors: | Aarohi Zokarkar Sarah A. Connolly Theodore S. Jardetzky Robert A. Lamb |
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| Affiliation: | aDepartment of Molecular Biosciences;bHoward Hughes Medical Institute, Northwestern University, Evanston, Illinois, USA;cDepartment of Structural Biology, Stanford University School of Medicine, Stanford, California, USA |
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| Abstract: | 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. |
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