5t1d
From Proteopedia
Crystal structure of EBV gHgL/gp42/E1D1 complex
Structural highlights
FunctionGL_EBVB9 The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Membrane fusion is mediated by the fusion machinery composed at least of gB and the heterodimer gH/gL. Fusion of EBV with B-lymphocytes requires the additional receptor-binding protein gp42, which forms a complex with gH/gL. May also be required for virus attachment to epithelial cells (By similarity). Publication Abstract from PubMedHerpesvirus entry into host cells is mediated by multiple virally encoded receptor binding and membrane fusion glycoproteins. Despite their importance in host cell tropism and associated disease pathology, the underlying and essential interactions between these viral glycoproteins remain poorly understood. For Epstein-Barr virus (EBV), gHgL/gp42 complexes bind HLA class II to activate membrane fusion with B cells, but gp42 inhibits fusion and entry into epithelial cells. To clarify the mechanism by which gp42 controls the cell specificity of EBV infection, here we determined the structure of gHgL/gp42 complex bound to an anti-gHgL antibody (E1D1). The critical regulator of EBV tropism is the gp42 N-terminal domain, which tethers the HLA-binding domain to gHgL by wrapping around the exterior of three gH domains. Both the gp42 N-terminal domain and E1D1 selectively inhibit epithelial-cell fusion; however, they engage distinct surfaces of gHgL. These observations clarify key determinants of EBV host cell tropism. Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.,Sathiyamoorthy K, Hu YX, Mohl BS, Chen J, Longnecker R, Jardetzky TS Nat Commun. 2016 Dec 8;7:13557. doi: 10.1038/ncomms13557. PMID:27929061[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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