Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1
Structure of the Epstein-Barr virus gp42 protein bound to the MHC class II receptor HLA-DR1
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DOI：
10.1016/s1097-2765(02)00465-3
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发表时间：
2002-02-01
期刊：
影响因子：
16
通讯作者：
Jardetzky, TS
中科院分区：
文献类型：
--
作者：
Mullen, MM;Haan, KM;Jardetzky, TS
EB病毒（EBV）引起传染性单核细胞增多症，建立长期潜伏感染，并与多种人类肿瘤有关。EBV gp 42糖蛋白结合MHC 11类分子，在B淋巴细胞的感染中起关键作用。EBV gp 42属于C型凝集素超家族，与免疫系统的NK受体具有同源性。我们报告的晶体结构的gp 42结合到人类MHC 11类分子HLA-DR 1。gp 42使用不同于典型凝集素和NK受体配体结合位点的表面位点结合HLA-DR 1。在典型的配体结合位点，gp 42形成了一个大的疏水沟，它可以与EBV进入所需的其他配体相互作用，提供了一种耦合MHC识别和膜融合的机制。
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 11 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 11 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.