2H6O

Epstein Barr Virus Major Envelope Glycoprotein

Summary for 2H6O

• Entry DOI: 10.2210/pdb2h6o/pdb
• Descriptor: Major outer envelope glycoprotein gp350, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-[beta-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-3)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (15 entities in total)
• Functional Keywords: glycoprotein, viral protein
• Biological source: Human herpesvirus 4 (Epstein-Barr virus)
• Total number of polymer chains: 1
• Total formula weight: 68299.15

Authors

Chen, X.S. (deposition date: 2006-05-31, release date: 2006-10-31, Last modification date: 2021-02-03)

Primary citation

Szakonyi, G.,Klein, M.G.,Hannan, J.P.,Young, K.A.,Ma, R.Z.,Asokan, R.,Holers, V.M.,Chen, X.S.
Structure of the Epstein-Barr virus major envelope glycoprotein
Nat.Struct.Mol.Biol., 13:996-1001, 2006

PubMed Abstract: 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.

PubMed: 17072314
DOI: 10.1038/nsmb1161

Experimental method

X-RAY DIFFRACTION (3.5 Å)