ArticleFrontiers in microbiology2018
Isolation and Characterization of Human Monoclonal Antibodies That Recognize the Influenza A(H1N1)pdm09 Virus Hemagglutinin Receptor-Binding Site and Rarely Yield Escape Mutant Viruses.
Article in Frontiers in microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Article
- Preparation and characterization of mouse-derived monoclonal antibodies against the hemagglutinin of the H1N1 influenza virus.Virus research · 2024Article
- Epitopes in the HA and NA of H5 and H7 avian influenza viruses that are important for antigenic drift.FEMS microbiology reviews · 2024Review
- A broadly protective human monoclonal antibody targeting the sialidase activity of influenza A and B virus neuraminidases.Nature communications · 2022Article
- Filovirus Neutralising Antibodies: Mechanisms of Action and Therapeutic Application.Pathogens (Basel, Switzerland) · 2021Review
- Potent sialic acid inhibitors that target influenza A virus hemagglutinin.Scientific reports · 2021Article
- Advances in the development of entry inhibitors for sialic-acid-targeting viruses.Drug discovery today · 2021Review
- Human Monoclonal Antibody Derived from Transchromosomic Cattle Neutralizes Multiple H1 Clades of Influenza A Virus by Recognizing a Novel Conformational Epitope in the Hemagglutinin Head Domain.Journal of virology · 2020Article
- Triple combination therapy of favipiravir plus two monoclonal antibodies eradicates influenza virus from nude mice.Communications biology · 2020Article
- Improving immunological insights into the ferret model of human viral infectious disease.Influenza and other respiratory viruses · 2019Review
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Authors and funding
6 authors.
Funding
Abstract
The influenza A virus rapidly mutates to escape from antibodies. Here, we isolated and characterized three human monoclonal antibodies (mAbs) that neutralize A(H1N1)pdm09 viruses. Generation of escape mutant viruses suggested that these antibodies recognized conserved residues of the receptor-binding site (RBS) of hemagglutinin (HA) and that mutant viruses that escaped from these mAbs rarely appeared. Moreover, the escape mutant viruses grew significantly slower than wild-type virus, indicating their reduced fitness. These results indicate that these three human mAbs against the RBS of HA have the potential to be anti-influenza agents with a low propensity for the development of resistant viruses.
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