8SGN
Crystal structure of Epstein-Barr virus glycoprotein 350 (gp350) in complex with Cy651H02, a monoclonal antibody isolated from macaques immunized with a gp350 nanoparticle vaccine
Summary for 8SGN
| Entry DOI | 10.2210/pdb8sgn/pdb |
| Descriptor | Cy651H02 Fab light chain, Cy651H02 Fab heavy chain, Envelope glycoprotein gp350, ... (8 entities in total) |
| Functional Keywords | epstein-barr virus, immune system, monoclonal antibody, macaques, viral protein, viral protein-immune system complex, viral protein/immune system |
| Biological source | Macaca fascicularis More |
| Total number of polymer chains | 3 |
| Total formula weight | 97426.03 |
| Authors | Joyce, M.G.,Jensen, J.L.,Chen, W.H.,Kanekiyo, M. (deposition date: 2023-04-12, release date: 2024-04-17, Last modification date: 2025-02-26) |
| Primary citation | Joyce, M.G.,Bu, W.,Chen, W.H.,Gillespie, R.A.,Andrews, S.F.,Wheatley, A.K.,Tsybovsky, Y.,Jensen, J.L.,Stephens, T.,Prabhakaran, M.,Fisher, B.E.,Narpala, S.R.,Bagchi, M.,McDermott, A.B.,Nabel, G.J.,Kwong, P.D.,Mascola, J.R.,Cohen, J.I.,Kanekiyo, M. Structural basis for complement receptor engagement and virus neutralization through Epstein-Barr virus gp350. Immunity, 58:295-, 2025 Cited by PubMed Abstract: Epstein-Barr virus (EBV) causes infectious mononucleosis and is associated with malignancies in humans. Viral infection of B cells is initiated by the viral glycoprotein 350 (gp350) binding to complement receptor 2 (CR2). Despite decades of effort, no vaccines or curative agents have been developed, partly due to lack of atomic-level understanding of the virus-host interface. Here, we determined the 1.7 Å structure of gp350 in complex with CR2. CR2 binding of gp350 utilized the same set of Arg residues required for recognition of its natural ligand, complement C3d. We further determined the structures of gp350 in complex with three potently neutralizing antibodies (nAbs) obtained from vaccinated macaques and EBV-infected individuals. Like the CR2 interaction, these nAbs targeted the acidic pocket within the CR2-binding site on gp350 using Arg residues. Our results illustrate two axes of molecular mimicry-gp350 versus C3d and CR2 versus EBV nAbs-offering insights for EBV vaccines and therapeutics development. PubMed: 39909035DOI: 10.1016/j.immuni.2025.01.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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