Evidence map›Paper›PMID 23645684›Full record

ArticleThe Journal of biological chemistry2013

The universal epitope of influenza A viral neuraminidase fundamentally contributes to enzyme activity and viral replication.

Tracey M Doyle, Bozena Jaentschke, Gary Van Domselaar, Anwar M Hashem, Aaron Farnsworth, Nicole E Forbes, Changgui Li, Junzhi Wang, Runtao He, Earl G Brown and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Antivirals Targeting the Neuraminidase.Cold Spring Harbor perspectives in medicine · 2022
    Review
  6. Article
  7. Impact of Protein Glycosylation on the Design of Viral Vaccines.Advances in biochemical engineering/biotechnology · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Why Do Exceptionally Dangerous Gain-of-Function Experiments in Influenza?Methods in molecular biology (Clifton, N.J.) · 2018
    Review
  16. Influenza A surface glycosylation and vaccine design.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Article
  19. Article
  20. 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

11 authors at 4 institutions in 3 countries.

Tracey M DoyleCentre for Vaccine Evaluation, Biologics and Genetic Therapies Directorate, Health Products and Food Branch, Health Canada, Ottawa, Ontario K1A 0K9, Canada.
Bozena Jaentschke
Gary Van Domselaar
Anwar M Hashem
Aaron Farnsworth
Nicole E Forbes
Changgui Li
Junzhi Wang
Runtao He
Earl G Brown
Xuguang Li
University of Ottawa · CAHealth Canada · CANational Institutes for Food and Drug Control · CNPublic Health Agency of Canada · CA

Funding

Canadian Institutes of Health Research TPA-90188
6 · The paper itself

Abstract

The only universally conserved sequence among all influenza A viral neuraminidases is located between amino acids 222 and 230. However, the potential roles of these amino acids remain largely unknown. Through an array of experimental approaches including mutagenesis, reverse genetics, and growth kinetics, we found that this sequence could markedly affect viral replication. Additional experiments revealed that enzymes with mutations in this region demonstrated substantially decreased catalytic activity, substrate binding, and thermostability. Consistent with viral replication analyses and enzymatic studies, protein modeling suggests that these amino acids could either directly bind to the substrate or contribute to the formation of the active site in the enzyme. Collectively, these findings reveal the essential role of this unique region in enzyme function and viral growth, which provides the basis for evaluating the validity of this sequence as a potential target for antiviral intervention and vaccine development.

Indexed as

Virus ReplicationAmino Acid SubstitutionAnimalsBinding SitesBiocatalysisCatalytic DomainCell LineChick EmbryoEnzyme StabilityEpitopesHEK293 CellsHumansInfluenza A virusKineticsModels, MolecularMutationEpitopesNeuraminidaseViral ProteinsEnzyme MutationEpitope MappingInfluenza VirusInfluenza Virus ReplicationNeuraminidaseStructural StabilitySubstrate BindingThermodynamicsUniversal EpitopeViral Replication

Identifiers

PMID23645684
PMCPMC3689970
OpenAlexW2020171297

What OpenQuestion holds

Textmetadata
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.