ArticleJournal of virology2002
Mutations conferring resistance to neutralization by a soluble form of the neurotrophin receptor (p75NTR) map outside of the known antigenic sites of the rabies virus glycoprotein.
Article in Journal of virology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 34 citations in OpenAlex.
- 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
- Construction of Vero cell-adapted rabies vaccine strain by five amino acid substitutions in HEP-Flury strain.Scientific reports · 2024Article
- Evaluation of Taxonomic Characteristics of Matlo and Phala Bat Rabies-Related Lyssaviruses Identified in South Africa.Viruses · 2023Article
- Research progress on neutralizing epitopes and antibodies for the Rabies virus.Infectious medicine · 2022Review
- Review
- Animal and human RNA viruses: genetic variability and ability to overcome vaccines.Archives of microbiology · 2021Review
- Lyssavirus Vaccine with a Chimeric Glycoprotein Protects across Phylogroups.Cell reports · 2020Article
- Article
- Identification of Two Classes of Somatosensory Neurons That Display Resistance to Retrograde Infection by Rabies Virus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017Article
- Diversity and epidemiology of Mokola virus.PLoS neglected tropical diseases · 2013Article
- Molecular and cellular aspects of rhabdovirus entry.Viruses · 2012Article
- Lyssaviruses: current trends.Advances in virus research · 2008Review
- The rabies virus glycoprotein receptor p75NTR is not essential for rabies virus infection.Journal of virology · 2007Article
- Rabies virus receptors.Journal of neurovirology · 2005Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The neurotrophin receptor (p75NTR) serves as a receptor for rabies virus (RV). We expressed and purified a soluble chimera consisting of the p75NTR ectodomain fused to the human immunoglobulin G1 (IgG1) Fc fragment (p75-Fc). Although p75-Fc interacts with RV, the infectivity of RV did not decrease significantly when it was incubated in the presence of the soluble receptor alone. However, when it was subsequently incubated with an antihuman IgG directed against the Fc fragment of p75-Fc, the infectivity of RV was significantly lowered (>90%), whereas incubation with antihuman IgG alone had no effect. We then selected eight independent RV mutants that were not neutralized by p75-Fc and antihuman IgG (srr [soluble receptor resistant] mutants). Each mutant carried a single mutation in the glycoprotein gene leading to one amino acid substitution in the protein. A total of four different substitutions were found. Two of the mutations were located at position 318 (phenylalanine replaced by a serine or a valine residue), and two were located at position 352 (histidine replaced by a tyrosine or an arginine residue). All of the mutations prevented the interaction with p75NTR as either a soluble or a membrane-anchored form. Two mutants (F318S) and (H352R) resulted in the formation of small plaques on BSR cells, probably due to the slower maturation of the glycoprotein. Immunoprecipitation, immunofluorescence, and neutralization assays showed that the four mutated glycoproteins still interacted with representative anti-RV glycoprotein monoclonal antibodies (MAbs), indicating that p75NTR binds outside of the known RV glycoprotein antigenic sites.
Indexed as
Identifiers
What OpenQuestion holds
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.