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Callaway, H. M.

Publications and source records attributed to Callaway, H. M..

2 recordsLinked to original sources

Antigenic landscape of rabies and related lyssaviruses revealed by cryo-EM

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-EM structures of neutralizing monoclonal antibodies in complex with the rabies virus surface glycoprotein (RABV-G). The nine structures span three known antigenic sites plus two new antigenic sites, not previously mapped. We further find that these two new sites are the targets of antibodies with the desired broad neutralization of rabies as well as other emerging lyssaviruses. 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.

microbiology↗

Structure of the rabies virus glycoprotein trimer bound to a pre-fusion specific neutralizing antibody

Rabies infection is nearly 100% lethal if untreated and kills over 50,000 people annually, many of them children. Existing rabies vaccines target the rabies virus glycoprotein (RABV-G) but generate short-lived immune responses, likely because the protein is heterogeneous under physiological conditions. Here, we report the 3.39[A] cryo-EM structure of trimeric, pre-fusion RABV-G complexed with RVA122, a potently neutralizing human antibody. RVA122 binds to a quaternary epitope at the top of RABV-G, bridging domains and stabilizing RABV-G protomers in a prefusion state. RABV-G trimerization involves side-to-side interactions between the central -helix and adjacent loops, rather than contacts between central helices, and interactions among the fusion loops at the glycoprotein base. These results provide a basis to develop improved rabies vaccines based on RABV-G stabilized in the prefusion conformation. One sentence summaryWe report the structure and trimeric interface of pre-fusion rabies virus glycoprotein bound to the neutralizing antibody RVA122.

microbiology↗