作者: Cynthia L. Rowe , Sarah A. Connolly , Jia Chen , Theodore S. Jardetzky , Richard Longnecker
DOI: 10.1016/J.VIROL.2012.10.039
关键词:
摘要: We investigated whether soluble EBV gH/gL (sgH/gL) functions in fusion and made a series of truncations domains based on the crystal structure. found sgH/gL failed to mediate cell-cell both when co-expressed with other entry glycoproteins added exogenously assays. Interestingly, inhibited dose dependent manner co-expressed. from HSV was unable inhibit fusion, suggesting inhibition specific gH/gL. stably binds gp42, but not gB nor The domain mutants, DI/gL, DI-II/gL DI-II-III/gL were bind gp42. Instead, DI-II/gL, DI/gL decreased expression resulting overall fusion. Overall, our results suggest that IV may be required for proper folding transmembrane cytoplasmic tail are most efficient