7CZE

Crystal structure of Epstein-Barr virus (EBV) gHgL and in complex with the ligand binding domian (LBD) of EphA2

7CZE の概要

• エントリーDOI: 10.2210/pdb7cze/pdb
• 分子名称: Envelope glycoprotein H, Envelope glycoprotein L, Ephrin type-A receptor 2, ... (4 entities in total)
• 機能のキーワード: glycoprotein, receptor, complex, virus entry, viral protein
• 由来する生物種: Epstein-Barr virus (strain B95-8) (HHV-4); 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 431836.34

構造登録者

Su, C.,Wu, L.L.,Song, H.,Chai, Y.,Qi, J.X.,Yan, J.H.,Gao, G.F. (登録日: 2020-09-08, 公開日: 2020-10-21, 最終更新日: 2024-10-30)

主引用文献

Su, C.,Wu, L.,Chai, Y.,Qi, J.,Tan, S.,Gao, G.F.,Song, H.,Yan, J.
Molecular basis of EphA2 recognition by gHgL from gammaherpesviruses.
Nat Commun, 11:5964-5964, 2020

PubMed Abstract: The human γ-herpesviruses Kaposi sarcoma associated herpesvirus (KSHV) and Epstein-Barr virus (EBV) are associated with many human malignancies. Viral glycoprotein H (gH) and glycoprotein L (gL) are crucial for the cell tropism by binding to specific receptors. Recently, EphA2 was identified as the specific entry receptor for both KSHV and EBV. Here, we characterized the crystal structures of KSHV gHgL or EBV gHgL in complex with the ligand binding domain (LBD) of EphA2. Both KSHV and EBV gHgL bind to the channel and peripheral regions of LBD primarily using gL. Extensive interactions with more contacts contribute to the higher affinity of KSHV gHgL to LBD than that of EBV gHgL. These binding characteristics were verified using cell-based fusion assays with mutations in key EphA2 residues. Our experiments suggest that multiple animal γ-herpesviruses could use EphA2 as an entry receptor, implying a potential threat to human health.

PubMed: 33235207
DOI: 10.1038/s41467-020-19617-9

実験手法

X-RAY DIFFRACTION (3 Å)