National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
5F32AI147531-03
米国
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
5T32AI07244-36
米国
Swiss National Science Foundation
P2EZP3_195680
スイス
引用
ジャーナル: Sci Adv / 年: 2022 タイトル: Structure of the rabies virus glycoprotein trimer bound to a prefusion-specific neutralizing antibody. 著者: Heather M Callaway / Dawid Zyla / Florence Larrous / Guilherme Dias de Melo / Kathryn M Hastie / Ruben Diaz Avalos / Alyssa Agarwal / Davide Corti / Hervé Bourhy / Erica Ollmann Saphire / 要旨: Rabies infection is nearly 100% lethal if untreated and kills more than 50,000 people annually, many of them children. Existing rabies vaccines target the rabies virus glycoprotein (RABV-G) but ...Rabies infection is nearly 100% lethal if untreated and kills more than 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 Å cryo-electron microscopy structure of trimeric, prefusion 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 from which to develop improved rabies vaccines based on RABV-G stabilized in the prefusion conformation.
#256 - 2021年4月 SARSコロナウイルス2型のスパイクと抗体 (SARS-CoV-2 Spike and Antibodies) 類似性 (2)
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A: Glycoprotein B: Glycoprotein C: Glycoprotein D: RVA122 Fab Light Chain E: RVA122 Fab Light Chain F: RVA122 Fab Light Chain G: RVA122 Fab Heavy Chain H: RVA122 Fab Heavy Chain I: RVA122 Fab Heavy Chain ヘテロ分子