Evidence map›Paper›PMID 21410647›Full record

ArticleThe FEBS journal2011

Glycomics-based analysis of chicken red blood cells provides insight into the selectivity of the viral agglutination assay.

Udayanath Aich, Nia Beckley, Zachary Shriver, Rahul Raman, Karthik Viswanathan, Sven Hobbie, Ram Sasisekharan

Open access · bronzeAbstract read
In one paragraph

Article in The FEBS journal, 2011. 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
–field-weighted citation impact, top 95% 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, 1 citations in OpenAlex.

  1. Journal of virology · 2022
    Article
  2. Article
  3. Article
  4. Article
  5. N-Glycomics of Human Erythrocytes.International journal of molecular sciences · 2021
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Influenza virus-glycan interactions.Current opinion in virology · 2014
    Review
  15. Review
  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

7 authors at 3 institutions in 2 countries.

Udayanath AichHarvard-MIT Division of Health Sciences & Technology, Department of Biological Engineering, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.
Nia Beckley
Zachary Shriver
Rahul Raman
Karthik Viswanathan
Sven Hobbie
Ram Sasisekharan
Harvard–MIT Division of Health Sciences and Technology · USMassachusetts Institute of Technology · USSingapore-MIT Alliance for Research and Technology · SG

Funding

Structure-Function Relationship of GlycosaminoglycansR37GM057073 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SASISEKHARAN, RAM · 2010 to 2019
$3.9M
Sequence Analysis of GlycosaminoglycansR01GM057073 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SASISEKHARAN, RAM · 1998 to 2010
$3.1M
NIGMS NIH HHS R01 GM057073NIGMS NIH HHS R37 GM057073
6 · The paper itself

Abstract

Agglutination of red blood cells (RBCs), including chicken RBCs (cRBCs), has been used extensively to estimate viral titer, to screen glycan-receptor binding preference, and to assess the protective response of vaccines. Although this assay enjoys widespread use, some virus strains do not agglutinate RBCs. To address these underlying issues and to increase the usefulness of cRBCs as tools for studying viruses, such as influenza, we analyzed the cell surface N-glycans of cRBCs. On the basis of the results obtained from complementary analytical strategies, including MS, 1D and 2D-NMR spectroscopy, exoglycosidase digestions, and HPLC profiling, we report the major glycan structures present on cRBCs. By comparing the glycan structures of cBRCs with those of representative human upper respiratory cells, we offer a possible explanation for the fact that certain influenza strains do not agglutinate cRBCs, using specific human-adapted influenza hemagglutinins as examples. Finally, recent understanding of the role of various glycan structures in high affinity binding to influenza hemagglutinins provides context to our findings. These results illustrate that the field of glycomics can provide important information with respect to the experimental systems used to characterize, detect and study viruses.

Indexed as

Agglutination TestsAnimalsChickensErythrocytesGlycomicsHemagglutinin Glycoproteins, Influenza VirusInfluenza A virusNuclear Magnetic Resonance, Biomolecularortho-AminobenzoatesPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationanthranilamideHemagglutinin Glycoproteins, Influenza Virusortho-AminobenzoatesPeptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine AmidasePolysaccharides

Identifiers

PMID21410647
PMCPMC3740515
OpenAlexW1533993983

What OpenQuestion holds

Textmetadata
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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.