Department of Molecular Biosciences, Northwestern University, Evanston, Illinois, USA.
J Virol. 2012 Nov;86(22):12397-401. doi: 10.1128/JVI.02006-12. Epub 2012 Sep 5.
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.
半胱氨酸被引入副粘病毒 F 蛋白的膜近端外部区域(MPER)。形成二硫键,突变蛋白在细胞表面表达但融合失活。二硫键的还原恢复了融合活性。数据表明,除了预融合 F 的三螺旋束茎域的解离之外,MPER 区域也需要分离,以便 F 能够重新折叠并引起融合。