title: Reversible inhibition of fusion activity of a paramyxovirus fusion protein by an engineered disulfide bond in the membrane-proximal external region.
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.
authors.affiliation: Department of Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.
authors.forename: Aarohi
authors.initials: A
authors.lastname: Zokarkar
authors.forename: Sarah A
authors.initials: SA
authors.lastname: Connolly
authors.forename: Theodore S
authors.initials: TS
authors.lastname: Jardetzky
authors.forename: Robert A
authors.initials: RA
authors.lastname: Lamb
mesh_terms: D002462:Cell Membrane / Q000378:metabolism; D003545:Cysteine / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry; D006367:HeLa Cells; D006801:Humans; D008561:Membrane Fusion; D008958:Models, Molecular; D009154:Mutation; D011485:Protein Binding; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D023822:Tissue Engineering / Q000379:methods; D014760:Viral Fusion Proteins / Q000737:chemistry* / Q000378:metabolism; D014764:Viral Proteins / Q000737:chemistry
chemical_list: D004220:Disulfides; D014760:Viral Fusion Proteins; D014764:Viral Proteins; D003545:Cysteine