ArticleAntimicrobial agents and chemotherapy2016
Trivalency of a Nanobody Specific for the Human Respiratory Syncytial Virus Fusion Glycoprotein Drastically Enhances Virus Neutralization and Impacts Escape Mutant Selection.
Article in Antimicrobial agents and chemotherapy, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.
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.
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
22 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.
- Research Progress and Applications of Multivalent, Multispecific and Modified Nanobodies for Disease Treatment.Frontiers in immunology · 2021Pooled it
- Time-Multiplexed Organic Electrochemical Transistor for Saliva-Based Rapid Detection of Viral Proteins.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Preclinical characterisation of the protective capacity of an anti-nucleoprotein hRSV monoclonal antibody.EBioMedicine · 2026Article
- Review
- Review
- Nanobody engineering for SARS-CoV-2 neutralization and detection.Microbiology spectrum · 2024Article
- New Developments and Challenges in Antibody-Based Therapies for the Respiratory Syncytial Virus.Infection and drug resistance · 2023Review
- Correlation between the binding affinity and the conformational entropy of nanobody SARS-CoV-2 spike protein complexes.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Multivalent designed proteins neutralize SARS-CoV-2 variants of concern and confer protection against infection in mice.Science translational medicine · 2022Article
- The role of single-domain antibodies (or nanobodies) in SARS-CoV-2 neutralization.Molecular biology reports · 2022Review
- A comprehensive comparison between camelid nanobodies and single chain variable fragments.Biomarker research · 2021Review
- Review
- The use of nanobodies in a sensitive ELISA test for SARS-CoV-2 Spike 1 protein.Royal Society open science · 2021Article
- Potent neutralization of clinical isolates of SARS-CoV-2 D614 and G614 variants by a monomeric, sub-nanomolar affinity nanobody.Scientific reports · 2021Article
- Bi-paratopic and multivalent VH domains block ACE2 binding and neutralize SARS-CoV-2.Nature chemical biology · 2021Article
- Bi-paratopic and multivalent human VH domains neutralize SARS-CoV-2 by targeting distinct epitopes within the ACE2 binding interface of Spike.bioRxiv : the preprint server for biology · 2020Article
- Recombinant expression of nanobodies and nanobody-derived immunoreagents.Protein expression and purification · 2020Review
- The Therapeutic Potential of Nanobodies.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2020Review
- Single-Domain Antibodies and Their Formatting to Combat Viral Infections.Antibodies (Basel, Switzerland) · 2018Review
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
ALX-0171 is a trivalent Nanobody derived from monovalent Nb017 that binds to antigenic site II of the human respiratory syncytial virus (hRSV) fusion (F) glycoprotein. ALX-0171 is about 6,000 to 10,000 times more potent than Nb017 in neutralization tests with strains of hRSV antigenic groups A and B. To explore the effect of this enhanced neutralization on escape mutant selection, viruses resistant to either ALX-0171 or Nb017 were isolated after serial passage of the hRSV Long strain in the presence of suboptimal concentrations of the respective Nanobodies. Resistant viruses emerged notably faster with Nb017 than with ALX-0171 and in both cases contained amino acid changes in antigenic site II of hRSV F. Detailed binding and neutralization analyses of these escape mutants as well as previously described mutants resistant to certain monoclonal antibodies (MAbs) offered a comprehensive description of site II mutations which are relevant for neutralization by MAbs and Nanobodies. Notably, ALX-0171 showed a sizeable neutralization potency with most escape mutants, even with some of those selected with the Nanobody, and these findings make ALX-0171 an attractive antiviral for treatment of hRSV infections.
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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.