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TitleA broadly neutralizing antibody confers cross-genus protection against alphaherpesviruses by inhibiting gB-mediated membrane fusion.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 11144, Year 2025
Publish dateDec 16, 2025
AuthorsGuosong Wang / Yu Li / Chongxin Wu / Tian Chen / Mengxuan Gui / Yue Zeng / Hui Sun / Kaiyun Chen / Xiangfeng Xi / Yanbo Yang / Yuchen Jiang / Yanan Jiang / Liqin Liu / Chengyu Yang / Jiarui Xin / Caihong Liu / Yiyi Li / Ningning Huo / Yang Huang / Lina Lin / Hai Yu / Chenghao Huang / Quan Yuan / Shaowei Li / Kegong Tian / Qingbing Zheng / Ningshao Xia / Yixin Chen /
PubMed AbstractThe global prevalence and disease burden of alphaherpesviruses infections, including human-infecting viruses such as HSV-1, HSV-2, and VZV, as well as animal-infecting viruses like PRV, BHV, CHV, and ...The global prevalence and disease burden of alphaherpesviruses infections, including human-infecting viruses such as HSV-1, HSV-2, and VZV, as well as animal-infecting viruses like PRV, BHV, CHV, and FHV, highlight the unmet need for more effective and universal antiviral strategies. However, there has been no significant progress in developing broad-spectrum interventions against herpesvirus. Here we report the identification of a broadly neutralizing antibody against alphaherpesviruses, 16F9, which targets the glycoprotein B (gB) of alphaherpesviruses and offers cross-protection against multiple viruses such as HSV-1, HSV-2, and PRV in mice. 16F9 demonstrated robust therapeutic efficacy in various female mouse models of herpesvirus diseases including PRV-induced viral encephalitis, HSV-1-induced viral encephalitis, viral keratitis, cutaneous herpes, and neonatal herpesvirus infections. High-resolution cryo-electron microscopy structures revealed that 16F9 binds a conserved site of vulnerability on Domain I of gB. The binding of 16F9 disrupts the interaction between pre-gB and gHgL complex, thereby preventing viral membrane fusion and blocking viral infection. This study provides a foundation for advancing antiviral strategies and underscores the potential of gB-targeted interventions for combating herpesvirus infections.
External linksNat Commun / PubMed:41402251 / PubMed Central
MethodsEM (single particle)
Resolution2.18 - 3.12 Å
Structure data

61596

9jmb

EMDB-61596, PDB-9jmb:
Cryo-EM structure of HSV-2 gB and FAB 16F9 complex
Method: EM (single particle) / Resolution: 2.18 Å

61599

9jme

EMDB-61599, PDB-9jme:
Cryo-EM structure of BV gB and FAB 16F9 complex
Method: EM (single particle) / Resolution: 2.18 Å

61611

9jmr

EMDB-61611, PDB-9jmr:
Cryo-EM structure of PRV gB and FAB 16f9 complex
Method: EM (single particle) / Resolution: 2.78 Å

61612

9jms

EMDB-61612, PDB-9jms:
Cryo-EM structure of VZV gB and FAB 16F9 complex
Method: EM (single particle) / Resolution: 3.12 Å

Source
  • Human alphaherpesvirus 2
  • human herpesvirus 2
  • mus musculus (house mouse)
  • Macacine alphaherpesvirus 1 (monkey B virus)
  • cercopithecine herpesvirus 1 (monkey B virus)
  • suid alphaherpesvirus 1
  • Bacillus sp. DSM 5850 (bacteria)
  • human herpesvirus 3 (Varicella-zoster virus)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Cryo-EM / HSV-2 gB / FAB 16F9 / Herpes virus / VIRAL PROTEIN-IMMUNE SYSTEM complex / MBV gB protein / Hepes virus / PRV gB / Herpe svirus / VZV gB

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