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- W3214116169 abstract "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 3.39Å 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 α-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." @default.
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- W3214116169 date "2021-11-16" @default.
- W3214116169 modified "2023-10-18" @default.
- W3214116169 title "Structure of the rabies virus glycoprotein trimer bound to a pre-fusion specific neutralizing antibody" @default.
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- W3214116169 doi "https://doi.org/10.1101/2021.11.16.468852" @default.
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