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.
View Article and Find Full Text PDFThe Paramyxoviridae family of enveloped viruses enters cells through the concerted action of two viral glycoproteins. The receptor-binding protein, hemagglutinin-neuraminidase (HN), H, or G, binds its cellular receptor and activates the fusion protein, F, which, through an extensive refolding event, brings viral and cellular membranes together, mediating virus-cell fusion. However, the underlying mechanism of F activation on receptor engagement remains unclear.
View Article and Find Full Text PDFParamyxoviruses enter host cells by fusing the viral envelope with a host cell membrane. Fusion is mediated by the viral fusion (F) protein, and it undergoes large irreversible conformational changes to cause membrane merger. The C terminus of PIV5 F contains a membrane-proximal 7-residue external region (MPER), followed by the transmembrane (TM) domain and a 20-residue cytoplasmic tail.
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