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Structural basis for Epstein–Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins
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Structural basis for Epstein–Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins
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Journal Article
Structural basis for Epstein–Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins
2016
Overview
Herpesvirus 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.
The entry of herpesviruses (such as Epstein-Barr virus) into host cells is mediated by a multitude of glycoproteins. Here, the authors show the structure of a viral glycoprotein complex, gHgL/gp42, bound to an anti-gHgL antibody, clarifying determinants of EBV host cell tropism.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
