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Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.

Nat Commun. 2016; 
Sathiyamoorthy K, Hu YX, Möhl BS, Chen J, Longnecker R, Jardetzky TS.
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Proteins, Expression, Isolation and Analysis E1D1 mAb was then purified from the clarified supernatant by protein G resin (L00209, Genscript), followed by gel filtration with Superdex 200 (GE Life Sciences). Get A Quote

摘要

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 dom... More

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