Evidence map›Paper›PMID 24945805›Full record

ArticlePloS one2014

Broad cross-reactive epitopes of the H5N1 influenza virus identified by murine antibodies against the A/Vietnam/1194/2004 hemagglutinin.

Mie Kobayashi-Ishihara, Hitoshi Takahashi, Kazuo Ohnishi, Kengo Nishimura, Kazutaka Terahara, Manabu Ato, Shigeyuki Itamura, Tsutomu Kageyama, Yasuko Tsunetsugu-Yokota

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.4field-weighted citation impact, top 34% of its field
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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Article
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

9 authors at 3 institutions in 1 country.

Mie Kobayashi-IshiharaDepartment of Immunology, National Institute of Infectious Diseases, Shinjuku, Tokyo, Japan.
Hitoshi TakahashiInfluenza Virus Research Center, National Institute of Infectious Diseases, Musashimurayama, Tokyo, Japan.
Kazuo OhnishiDepartment of Immunology, National Institute of Infectious Diseases, Shinjuku, Tokyo, Japan.
Kengo NishimuraTsuruga Institute of Biotechnology, Toyobo, Co., Ltd., Tsuruga, Fukui, Japan.
Kazutaka TeraharaDepartment of Immunology, National Institute of Infectious Diseases, Shinjuku, Tokyo, Japan.
Manabu AtoDepartment of Immunology, National Institute of Infectious Diseases, Shinjuku, Tokyo, Japan.
Shigeyuki ItamuraInfluenza Virus Research Center, National Institute of Infectious Diseases, Musashimurayama, Tokyo, Japan.
Tsutomu KageyamaInfluenza Virus Research Center, National Institute of Infectious Diseases, Musashimurayama, Tokyo, Japan.
Yasuko Tsunetsugu-YokotaDepartment of Immunology, National Institute of Infectious Diseases, Shinjuku, Tokyo, Japan; Department of Medical Technology, School of Human Sciences, Tokyo University of Technology, Ohta-ku, Tokyo, Japan.
National Institute of Infectious Diseases · JPTokyo University of Technology · JPToyobo (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is an urgent need for a rapid diagnostic system to detect the H5 subtype of the influenza A virus. We previously developed monoclonal antibodies (mAbs) against the H5 hemagglutinin (HA) for use in a rapid diagnostic kit. In this study, we determined the epitopes of the anti-H5 HA murine mAbs OM-b, AY-2C2, and YH-1A1. Binding assays of the mAbs to different strains of H5 HAs indicated that OM-b and AY-2C2 cross-reacted with HAs from clades 1, 2.1.3.2, 2.2, and 2.3.4, whereas YH-1A1 failed to bind to those of clades 2.1.3.2 and 2.3.4. HA chimeras revealed that the epitopes for each of the mAbs were in the HA1 region. Analysis of escape mutants revealed that OM-b and AY-2C2 mAbs interacted mainly with amino acid residues D43 and G46, and the YH-1A1 mAb interacted with G139 and K or R140 of H5 HA. Multiple alignments of H5 HA protein sequences showed that D43 and G46 were very conserved among H5N1 HAs, except those in clade 2.2.1 and clade 7 (88.7%). The epitope for YH-1A1 mAb was highly variable in the HAs of H5N1, although it was well conserved in those of H5N2-N9. The OM-b and AY-2C2 mAbs could bind to the HAs of clades 1.1 and 2.3.2.1 that are currently epidemic in Asia, and we conclude that these would be effective for the detection of H5N1 infections in this region.

Indexed as

AnimalsAntibodies, MonoclonalCross ReactionsEnzyme-Linked Immunosorbent AssayEpitope MappingEpitopesHemagglutinin Glycoproteins, Influenza VirusHumansInfluenza A Virus, H5N1 SubtypeInfluenza, HumanMiceAntibodies, MonoclonalEpitopeshemagglutinin, avian influenza A virusHemagglutinin Glycoproteins, Influenza Virus

Identifiers

PMID24945805
PMCPMC4063728
OpenAlexW2019295084

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.