Authors
Heather M Callaway, Dawid S Zyla, Kathryn M Hastie, Stephanie S Harkins, Shanika Kothalawalage, Nimasha Samarasinghe, Alexander Flynn, Chitra Hariharan, Jieyun Yin, Davide Corti, Herve Bourhy, Scott K Dessain, Erica Ollmann Saphire
Published in
Cell reports. Volume 45. Issue 10. Pages 117993. Sep 17, 2026. Epub Sep 17, 2026.
Abstract
Rabies continues to kill over 60,000 people per year despite life-saving vaccines and post-exposure treatments and costs billions of dollars in prevention and treatment. Preventing rabies deaths and reducing the global economic burden of the virus will require both developing a monoclonal antibody cocktail to replace human serum in treatment and improving rabies vaccines to elicit long-lasting protection. Here, we solve nine cryo-electron microscopy (cryo-EM) structures of neutralizing monoclonal antibodies (mAbs) in complex with the rabies virus glycoprotein (RABV-G). The nine structures span three known antigenic sites plus two additional antigenic sites, not among the five classically identified sites. We find that these antigenic sites, V and VI, are broadly cross-reactive across lyssaviruses, whereas immunodominant sites II/IV and III are rabies specific. Across the mAb panel, fusion inhibition and binding affinity correlate best with neutralization. Together, these results provide a roadmap for structure-guided vaccine and therapeutic antibody design for rabies and related lyssaviruses.
PMID:
42758589
Bibliographic data and abstract were imported from PubMed on 19 Sep 2026.
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