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-Structure paper
| タイトル | Structural basis of Epstein-Barr virus gp350 receptor recognition and neutralization. |
|---|---|
| ジャーナル・号・ページ | Cell Rep, Vol. 44, Issue 1, Page 115168, Year 2025 |
| 掲載日 | 2025年1月8日 |
著者 | Cong Sun / Xin-Yan Fang / Guo-Long Bu / Lan-Yi Zhong / Chu Xie / Ge-Xin Zhao / Sen-Fang Sui / Zheng Liu / Mu-Sheng Zeng / ![]() |
| PubMed 要旨 | Epstein-Barr virus (EBV) is an oncogenic virus associated with multiple lymphoid malignancies and autoimmune diseases. During infection in B cells, EBV uses its major glycoprotein gp350 to recognize ...Epstein-Barr virus (EBV) is an oncogenic virus associated with multiple lymphoid malignancies and autoimmune diseases. During infection in B cells, EBV uses its major glycoprotein gp350 to recognize the host receptor CR2, initiating viral attachment, a process that has lacked direct structural evidence for decades. In this study, we resolved the structure of the gp350-CR2 complex, elucidated their key interactions, and determined the site-specific N-glycosylation map of gp350. Our findings reveal that CR2 primarily binds to gp350 through an electrostatically complementary and glycan-free interface and that the diversity of key residues in CR2 across different species influences EBV host selectivity mediated by gp350. With the confirmed binding, we constructed a CR2-Fc antibody analog that targets the vulnerable site of gp350, demonstrating a potent neutralization effect against EBV infection in B cells. Our work provides essential structural insights into the mechanism of EBV infection and host tropism, suggesting a potential antiviral agent. |
リンク | Cell Rep / PubMed:39792550 |
| 手法 | EM (単粒子) |
| 解像度 | 3.29 Å |
| 構造データ | EMDB-60272, PDB-8zni: |
| 化合物 | ![]() ChemComp-NAG: |
| 由来 |
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キーワード | VIRAL PROTEIN |
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human gammaherpesvirus 4 (ヘルペスウイルス)
homo sapiens (ヒト)
キーワード