ArticleNature communications2020
Structure of the prefusion-locking broadly neutralizing antibody RVC20 bound to the rabies virus glycoprotein.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
34 citing papers in PubMed, 50 citations in OpenAlex.
- Peripheral human mAb therapy yields modulation of neuroinflammation and long-term functional recovery from lyssavirus infection.Emerging microbes & infections · 2026Article
- Dog bite-associated pathogens: advances in pathogenic mechanisms and systemic clinical consequences in humans.One health (Amsterdam, Netherlands) · 2026Review
- Breaking the Silent Barrier: Engineering Antibodies for Brain-Targeted Rabies Immunotherapy.Pharmaceutics · 2026Review
- Structural overview of lyssavirus glycoproteins, antibodies, and receptors.Journal of virology · 2026Review
- Conserved use of tetraspanin CD9 as an entry receptor by rhabdoviruses spanning multiple genera.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A Fully Human Derived Monoclonal Antibody Provides Potent Pre- and Postexposure Protection Against Rabies Virus.Transboundary and emerging diseases · 2026Article
- A SynB1-conjugated antibody cocktail crosses the blood-brain barrier to produce a therapeutic effect on rabies.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural basis for broad neutralization of rabies virus by an antibody cocktail SYN023.Emerging microbes & infections · 2025Article
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- Deep mutational scanning of rabies glycoprotein defines mutational constraint and antibody-escape mutations.Cell host & microbe · 2025Article
- Molecular convergence of neutralizing antibodies in human revealed by repeated rabies vaccination.NPJ vaccines · 2025Article
- Structures of two lyssavirus glycoproteins trapped in pre- and post-fusion states and the implications on the spatial-temporal conformational transition along with pH-decrease.PLoS pathogens · 2025Article
- Article
- Self-assembling nanoparticle engineered from the ferritinophagy complex as a rabies virus vaccine candidate.Nature communications · 2024Article
- Development of novel canine phage display-derived neutralizing monoclonal antibody fragments against rabies virus from immunized dogs.Scientific reports · 2024Article
- Toward the Development of a Pan-Lyssavirus Vaccine.Viruses · 2024Article
- Establishment of serological neutralizing tests using pseudotyped viruses for comprehensive detection of antibodies against all 18 lyssaviruses.The Journal of veterinary medical science · 2024Article
- Emerging Rhabdoviruses and Human Infection.Biology · 2023Review
- Antiviral mechanisms of two broad-spectrum monoclonal antibodies for rabies prophylaxis and therapy.Frontiers in immunology · 2023Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rabies virus (RABV) causes fatal encephalitis in more than 59,000 people yearly. Upon the bite of an infected animal, the development of clinical disease can be prevented with post-exposure prophylaxis (PEP), which includes the administration of Rabies immunoglobulin (RIG). However, the high cost and limited availability of serum-derived RIG severely hamper its wide use in resource-limited countries. A safe low-cost alternative is provided by using broadly neutralizing monoclonal antibodies (bnAbs). Here we report the X-ray structure of one of the most potent and most broadly reactive human bnAbs, RVC20, in complex with its target domain III of the RABV glycoprotein (G). The structure reveals that the RVC20 binding determinants reside in a highly conserved surface of G, rationalizing its broad reactivity. We further show that RVC20 blocks the acid-induced conformational change required for membrane fusion. Our results may guide the future development of direct antiviral small molecules for Rabies treatment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.