Evidence map›Paper›PMID 30282714›Full record

ArticleJournal of virology2019

Amino Acid Residue 217 in the Hemagglutinin Glycoprotein Is a Key Mediator of Avian Influenza H7N9 Virus Antigenicity.

Pengxiang Chang, Joshua E Sealy, Jean-Remy Sadeyen, Munir Iqbal

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Antigenic characterization of influenza and SARS-CoV-2 viruses.Analytical and bioanalytical chemistry · 2022
    Review
  11. Article
  12. Article
  13. H7N9 Influenza Virus in China.Cold Spring Harbor perspectives in medicine · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. 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

4 authors at 1 institution in 1 country.

Pengxiang ChangThe Pirbright Institute, Pirbright, United Kingdom.
Joshua E SealyThe Pirbright Institute, Pirbright, United Kingdom.
Jean-Remy SadeyenThe Pirbright Institute, Pirbright, United Kingdom.
Munir IqbalThe Pirbright Institute, Pirbright, United Kingdom munir.iqbal@pirbright.ac.uk.ORCID 0000-0001-5165-5339
The Pirbright Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/I/00001422Biotechnology and Biological Sciences Research Council BBS/E/I/00001708Biotechnology and Biological Sciences Research Council BBS/E/I/00007031Biotechnology and Biological Sciences Research Council BBS/E/I/00007036Biotechnology and Biological Sciences Research Council BBS/E/I/00007038Biotechnology and Biological Sciences Research Council BBS/E/I/00007039
6 · The paper itself

Abstract

Avian influenza viruses continue to evolve and acquire mutations that facilitate antigenic drift and virulence change. In 2017, low-pathogenicity H7N9 avian influenza viruses evolved to a high-pathogenicity phenotype in China. Comparative antigenic analysis of the low- and high-pathogenicity virus strains showed marked variability. In order to identify residues that may be linked to the antigenic change among the H7N9 viruses, we serially passaged the viruses in the presence of homologous ferret antiserum. Progeny viruses able to overcome the neutralizing capacity of the antiserum were sequenced. The analysis showed that the emergent immune escape viruses contained mutations A125T, A151T, and L217Q in the hemagglutinin (HA) glycoprotein as early as passage 5 and that these mutations persisted until passage 10. The results revealed that a single mutation, L217Q, in the HA of H7N9 virus led to 23- and 8-fold reductions in hemagglutination inhibition (HI) titer with ferret and chicken antisera, respectively. Further analysis showed that this change also contributed to antigenic differences between the low- and high-pathogenicity H7N9 viruses, thus playing a major role in their antigenic diversification. Therefore, evolutionary changes at amino acid position 217 in the H7N9 viruses can serve as a genetic marker for virus antigenic diversity during vaccine seed matching and selection. The

Indexed as

MutationAmino AcidsAnimalsAntigenic VariationChinaEvolution, MolecularFerretsHemagglutinin Glycoproteins, Influenza VirusImmune EvasionImmune SeraInfluenza A Virus, H7N9 SubtypeSerial PassageAmino AcidsHemagglutinin Glycoproteins, Influenza VirusImmune Seraantigenic diversificationavian influenza virusevolutionH7N9 virushemagglutinin glycoproteinimmune escape

Identifiers

PMID30282714
PMCPMC6288333
OpenAlexW2895252518

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.