9ZWE
Soluble ectodomain of Herpes simplex virus 2 (HSV-2) glycoprotein B (gB) in the prefusion conformation in complex with 2c and D48 Fabs
Summary for 9ZWE
| Entry DOI | 10.2210/pdb9zwe/pdb |
| EMDB information | 74907 |
| Descriptor | Envelope glycoprotein B, Antibody D48 Heavy Chain, Antibody D48 Light Chain, ... (5 entities in total) |
| Functional Keywords | prefusion, ectodomain, viral fusion protein, viral protein-immune system complex, viral protein/immune system |
| Biological source | Human herpesvirus 2 strain HG52 More |
| Total number of polymer chains | 15 |
| Total formula weight | 539113.88 |
| Authors | Sponholtz, M.R.,Johnson, N.V.,McLellan, J.S. (deposition date: 2026-01-01, release date: 2026-02-04, Last modification date: 2026-09-30) |
| Primary citation | Sponholtz, M.R.,Ma, D.Y.,Ndashimye, E.,Byrne, P.O.,Shu, Y.,Warren, C.,Thambi, N.,McCool, R.S.,Slein, M.D.,Johnson, N.V.,Rose 2nd, W.A.,Zhang, L.,Durr, E.,Wang, D.,McLellan, J.S. Structure-based design of soluble prefusion-stabilized herpes simplex virus type 2 glycoprotein B antigens. Cell Rep, 45:117936-117936, 2026 Cited by PubMed Abstract: Herpes simplex virus type 2 (HSV-2) infection causes recurrent genital herpes throughout life, yet no vaccines have been approved. Glycoprotein B (gB) is a class III fusion protein that mediates HSV-2 entry by transitioning from a metastable prefusion conformation to a stable postfusion conformation. Here, using structure-based design, we stabilize HSV-2 gB in its prefusion conformation. A 2.8 Å resolution cryo-EM structure reveals a closed state of prefusion gB, which differs from recently published open states. Vaccination of mice with protein subunit and mRNA-based vaccines of pre- and postfusion gB variants elicits robust humoral and cellular responses. Although prefusion stabilization of gB does not improve neutralizing antibody titers relative to the postfusion construct, prefusion gB elicits antibodies exhibiting higher FcγR-mediated effector activities. Collectively, these findings reveal insights into prefusion gB conformational dynamics, provide stabilized reagents for studying gB-directed immune responses, and inform HSV-2 vaccine design. PubMed: 42709545DOI: 10.1016/j.celrep.2026.117936 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.75 Å) |
Structure validation
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