Evidence map›Paper›PMID 30987023›Full record

ArticleViruses2019

Subclade 2.2.1-Specific Human Monoclonal Antibodies That Recognize an Epitope in Antigenic Site A of Influenza A(H5) Virus HA Detected between 2015 and 2018.

Moe Okuda, Seiya Yamayoshi, Ryuta Uraki, Mutsumi Ito, Taiki Hamabata, Yoshihiro Kawaoka

Abstract read
In one paragraph

Article in Viruses, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

  1. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Moe OkudaDivision of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan. 1923890575@edu.k.u-tokyo.ac.jp.
Seiya YamayoshiDivision of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan. yamayo@ims.u-tokyo.ac.jp.ORCID 0000-0001-7768-5157
Ryuta UrakiDivision of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan. r-uraki@med.nagoya-cu.ac.jp.ORCID 0000-0003-0890-1922
Mutsumi ItoDivision of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan. ito-mu@ims.u-tokyo.ac.jp.
Taiki HamabataDivision of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan. hamabata@ims.u-tokyo.ac.jp.
Yoshihiro KawaokaDivision of Virology, Department of Microbiology and Immunology, Institute of Medical Science, University of Tokyo, Minato-ku, Tokyo 108-8639, Japan. yoshihiro.kawaoka@wisc.edu.

Funding

NIAID NIH HHS HHSN272201400008C
6 · The paper itself

Abstract

Highly pathogenic avian H5 influenza viruses persist among poultry and wild birds throughout the world. They sometimes cause interspecies transmission between avian and mammalian hosts. H5 viruses possessing the HA of subclade 2.3.4.4, 2.3.2.1, 2.2.1, or 7.2 were detected between 2015 and 2018. To understand the neutralizing epitopes of H5-HA, we characterized 15 human monoclonal antibodies (mAbs) against the HA of H5 viruses, which were obtained from volunteers who received the H5N1 vaccine that contains a subclade 2.2.1 or 2.1.3.2 virus as an antigen. Twelve mAbs were specific for the HA of subclade 2.2.1, two mAbs were specific for the HA of subclade 2.1.3.2, and one mAb was specific for the HA of both. Of the 15 mAbs analyzed, nine, which were specific for the HA of subclade 2.2.1, and shared the VH and VL genes, possessed hemagglutination inhibition and neutralizing activities, whereas the others did not. A single amino acid substitution or insertion at positions 144-147 in antigenic site A conferred resistance against these nine mAbs to the subclade 2.2.1 viruses. The amino acids at positions 144-147 are highly conserved among subclade 2.2.1, but differ from those of other subclades. These results show that the neutralizing epitope including amino acids at positions 144-147 is targeted by human antibodies, and plays a role in the antigenic difference between subclade 2.2.1 and other subclades.

Indexed as

Amino AcidsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitope MappingEpitopesHemagglutination Inhibition TestsHemagglutinin Glycoproteins, Influenza VirusHumansImmune EvasionInfluenza A virusInfluenza A Virus, H5N1 SubtypeInfluenza VaccinesMutationNeutralization TestsAmino AcidsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralEpitopeshemagglutinin, avian influenza A virusHemagglutinin Glycoproteins, Influenza VirusInfluenza Vaccinesescape mutant virusH5-HAhuman monoclonal antibodyInfluenza A virus

Identifiers

PMID30987023
PMCPMC6521261

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Registered trials

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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.