8ZNI

Structure of Epstein-Barr virus major glycoprotein gp350 in complex with the receptor CR2

Summary for 8ZNI

• Entry DOI: 10.2210/pdb8zni/pdb
• EMDB information: 60272
• Descriptor: Complement receptor type 2, BLLF1, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: viral protein
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 199250.26

Authors

Fang, X.Y.,Sun, C.,Liu, Z.,Zeng, M.S. (deposition date: 2024-05-27, release date: 2025-01-15, Last modification date: 2025-01-22)

Primary citation

Sun, C.,Fang, X.Y.,Bu, G.L.,Zhong, L.Y.,Xie, C.,Zhao, G.X.,Sui, S.F.,Liu, Z.,Zeng, M.S.
Structural basis of Epstein-Barr virus gp350 receptor recognition and neutralization.
Cell Rep, 44:115168-115168, 2025

PubMed Abstract: 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.

PubMed: 39792550
DOI: 10.1016/j.celrep.2024.115168

Experimental method

ELECTRON MICROSCOPY (3.29 Å)