Nature Structural & Molecular Biology
- 13, 996 - 1001 (2006)
Published online: 29 October 2006; | doi:10.1038/nsmb1161
Structure of the Epstein-Barr virus major envelope glycoproteinGerda Szakonyi1, 2, Michael G Klein1, Jonathan P Hannan3, Kendra A Young3, Runlin Z Ma4, Rengasamy Asokan3, V Michael Holers3 & Xiaojiang S Chen11
Department of Molecular and Computational Biology, University of Southern California, 1050 Childs Way, Los Angeles, California 90089, USA. 2
University of Szeged, Institute of Pharmaceutical Analysis, Szeged, 6720, Hungary. 3
Department of Medicine and Immunology, University of Colorado Health Sciences Center, 4200 E 9th Ave., Denver, Colorado 80262, USA. 4
Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
Correspondence should be addressed to Xiaojiang S Chen xiaojiang.chen@usc.edu Epstein-Barr virus (EBV) infection of B cells is associated with lymphoma and other human cancers. EBV infection is initiated by the binding of the viral envelope glycoprotein (gp350) to the cell surface receptor CR2. We determined the X-ray structure of the highly glycosylated gp350 and defined the CR2 binding site on gp350. Polyglycans shield all but one surface of the gp350 polypeptide, and we demonstrate that this glycan-free surface is the receptor-binding site. Deglycosylated gp350 bound CR2 similarly to the glycosylated form, suggesting that glycosylation is not important for receptor binding. Structure-guided mutagenesis of the glycan-free surface disrupted receptor binding as well as binding by a gp350 monoclonal antibody, a known inhibitor of virus-receptor interactions. These results provide structural information for developing drugs and vaccines to prevent infection by EBV and related viruses.
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