Evidence map›Paper›PMID 22355715›Full record

ArticleScientific reports2011

Networks link antigenic and receptor-binding sites of influenza hemagglutinin: mechanistic insight into fitter strain propagation.

Venkataramanan Soundararajan, Shu Zheng, Neel Patel, Ken Warnock, Rahul Raman, Ian A Wilson, S Raguram, V Sasisekharan, Ram Sasisekharan

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
3.0field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Learned features of antibody-antigen binding affinity.Frontiers in molecular biosciences · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Insights on the mutational landscape of the SARS-CoV-2 Omicron variant.bioRxiv : the preprint server for biology · 2021
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Allele-specific nonstationarity in evolution of influenza A virus surface proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Glycan-protein interactions in viral pathogenesis.Current opinion in structural biology · 2016
    Review
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 4 institutions in 2 countries.

Venkataramanan SoundararajanHarvard-MIT Division of Health Sciences & Technology, the Koch Institute for Integrative Cancer Research, and the Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Shu Zheng
Neel Patel
Ken Warnock
Rahul Raman
Ian A Wilson
S Raguram
V Sasisekharan
Ram Sasisekharan
Harvard–MIT Division of Health Sciences and Technology · USMassachusetts Institute of Technology · USInstitute of Cognitive and Brain Sciences · USScripps Research Institute · US

Funding

Viral and Host cDNA Libraries from 1918 Influenza CasesP01AI058113 · NIAID · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI GARCIA-SASTRE, ADOLFO · 2004 to 2010
$20.3M
Structure-Function Relationship of GlycosaminoglycansR37GM057073 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SASISEKHARAN, RAM · 2010 to 2019
$3.9M
NIAID NIH HHS P01 AI058113NIGMS NIH HHS GM R37GM057073-13NIGMS NIH HHS R37 GM057073
6 · The paper itself

Abstract

Influenza viral passaging through pre-vaccinated mice shows that emergent antigenic site mutations on the viral hemagglutinin (HA) impact host receptor-binding affinity and, therefore, the evolution of fitter influenza strains. To understand this phenomenon, we computed the Significant Interactions Network (SIN) for each residue and mapped the networks of antigenic site residues on a representative H1N1 HA. Specific antigenic site residues are 'linked' to receptor-binding site (RBS) residues via their SIN and mutations within "RBS-linked" antigenic residues can significantly influence receptor-binding affinity by impacting the SIN of key RBS residues. In contrast, other antigenic site residues do not have such "RBS-links" and do not impact receptor-binding affinity upon mutation. Thus, a potential mechanism emerges for how immunologic pressure on RBS-linked antigenic residues can contribute to evolution of fitter influenza strains by modulating the host receptor-binding affinity.

Indexed as

Influenza A Virus, H1N1 SubtypeProtein Interaction MappingAlgorithmsAntigens, ViralBinding SitesComputational BiologyEpitopesGene Expression RegulationHemagglutinin Glycoproteins, Influenza VirusHumansModels, MolecularMutationPhylogenyProtein BindingProtein FoldingProtein Structure, TertiaryAntigens, ViralEpitopesHemagglutinin Glycoproteins, Influenza VirusReceptors, Virus

Identifiers

PMID22355715
PMCPMC3242012
OpenAlexW1982770245

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.