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TitleA non-neutralizing glycoprotein B monoclonal antibody protects against herpes simplex virus disease in mice.
Journal, issue, pagesJ Clin Invest, Vol. 133, Issue 3, Year 2023
Publish dateFeb 1, 2023
AuthorsMasayuki Kuraoka / Clare Burn Aschner / Ian W Windsor / Aakash Mahant Mahant / Scott J Garforth / Susan Luozheng Kong / Jacqueline M Achkar / Steven C Almo / Garnett Kelsoe / Betsy C Herold /
PubMed AbstractThere is an unmet need for monoclonal antibodies (mAbs) for prevention or as adjunctive treatment of herpes simplex virus (HSV) disease. Most vaccine and mAb efforts focus on neutralizing antibodies, ...There is an unmet need for monoclonal antibodies (mAbs) for prevention or as adjunctive treatment of herpes simplex virus (HSV) disease. Most vaccine and mAb efforts focus on neutralizing antibodies, but for HSV this strategy has proven ineffective. Preclinical studies with a candidate HSV vaccine strain, ΔgD-2, demonstrated that non-neutralizing antibodies that activate Fcγ receptors (FcγRs) to mediate antibody-dependent cellular cytotoxicity (ADCC) provide active and passive protection against HSV-1 and HSV-2. We hypothesized that this vaccine provides a tool to identify and characterize protective mAbs. We isolated HSV-specific mAbs from germinal center and memory B cells and bone marrow plasmacytes of ΔgD-2-vaccinated mice and evaluated these mAbs for binding, neutralizing, and FcγR-activating activity and for protective efficacy in mice. The most potent protective mAb, BMPC-23, was not neutralizing but activated murine FcγRIV, a biomarker of ADCC. The cryo-electron microscopic structure of the Fab-glycoprotein B (gB) assembly identified domain IV of gB as the epitope. A single dose of BMPC-23 administered 24 hours before or after viral challenge provided significant protection when configured as mouse IgG2c and protected mice expressing human FcγRIII when engineered as a human IgG1. These results highlight the importance of FcR-activating antibodies in protecting against HSV.
External linksJ Clin Invest / PubMed:36454639 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.4 Å
Structure data

26520

7uhz

EMDB-26520, PDB-7uhz:
Post-fusion ectodomain of HSV-1 gB in complex with BMPC-23 Fab
Method: EM (single particle) / Resolution: 3.3 Å

26521

7ui0

EMDB-26521, PDB-7ui0:
Post-fusion ectodomain of HSV-1 gB in complex with HSV010-13 Fab
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • mus musculus (house mouse)
  • human alphaherpesvirus 1 strain kos
KeywordsVIRAL PROTEIN / glycoprotein / fusogen / antibody / ADCC / VIRAL PROTEIN/Immune System / VIRAL PROTEIN-Immune System complex

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