Abstract:
:Epstein-Barr virus (EBV) causes infectious mononucleosis, establishes long-term latent infections, and is associated with a variety of human tumors. The EBV gp42 glycoprotein binds MHC class II molecules, playing a critical role in infection of B lymphocytes. EBV gp42 belongs to the C-type lectin superfamily, with homology to NK receptors of the immune system. We report the crystal structure of gp42 bound to the human MHC class II molecule HLA-DR1. The gp42 binds HLA-DR1 using a surface site that is distinct from the canonical lectin and NK receptor ligand binding sites. At the canonical ligand binding site, gp42 forms a large hydrophobic groove, which could interact with other ligands necessary for EBV entry, providing a mechanism for coupling MHC recognition and membrane fusion.
journal_name
Mol Celljournal_title
Molecular cellauthors
Mullen MM,Haan KM,Longnecker R,Jardetzky TSdoi
10.1016/s1097-2765(02)00465-3subject
Has Abstractpub_date
2002-02-01 00:00:00pages
375-85issue
2eissn
1097-2765issn
1097-4164pii
S1097-2765(02)00465-3journal_volume
9pub_type
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