5T1D

Crystal structure of EBV gHgL/gp42/E1D1 complex

Summary for 5T1D

• Entry DOI: 10.2210/pdb5t1d/pdb
• Related: 1KG0 3FD4 3PHF
• Descriptor: Envelope glycoprotein H, Envelope glycoprotein L, Glycoprotein 42, ... (6 entities in total)
• Functional Keywords: receptor binding, herpesvirus entry, epstein-barr virus, membrane fusion, viral protein
• Biological source: Epstein-Barr virus (strain B95-8) (HHV-4); More
• Total number of polymer chains: 5
• Total formula weight: 154376.85

Authors

Sathiyamoorthy, K.,Jardetzky, T.S. (deposition date: 2016-08-18, release date: 2016-12-28, Last modification date: 2024-10-16)

Primary citation

Sathiyamoorthy, K.,Hu, Y.X.,Mohl, B.S.,Chen, J.,Longnecker, R.,Jardetzky, T.S.
Structural basis for Epstein-Barr virus host cell tropism mediated by gp42 and gHgL entry glycoproteins.
Nat Commun, 7:13557-13557, 2016

PubMed Abstract: 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.

PubMed: 27929061
DOI: 10.1038/ncomms13557

Experimental method

X-RAY DIFFRACTION (3.1 Å)