Evidence map›Paper›PMID 18853253›Full record

ArticleGlycoconjugate journal2009

Analysis of N-glycans in embryonated chicken egg chorioallantoic and amniotic cells responsible for binding and adaptation of human and avian influenza viruses.

Nongluk Sriwilaijaroen, Sachiko Kondo, Hirokazu Yagi, Prapon Wilairat, Hiroaki Hiramatsu, Morihiro Ito, Yasuhiko Ito, Koichi Kato, Yasuo Suzuki

Open access · hybridAbstract read
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In one paragraph

Article in Glycoconjugate journal, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

25 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Influenza Hemagglutinin Structures and Antibody Recognition.Cold Spring Harbor perspectives in medicine · 2020
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Cellular scent of influenza virus infection.Chembiochem : a European journal of chemical biology · 2014
    Article
  16. Molecular basis of a pandemic of avian-type influenza virus.Methods in molecular biology (Clifton, N.J.) · 2014
    Review
  17. Review
  18. Article
  19. Molecular basis of the structure and function of H1 hemagglutinin of influenza virus.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2012
    Review
  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

9 authors at 6 institutions in 2 countries.

Nongluk SriwilaijaroenDepartment of Biomedical Sciences, College of Life and Health Sciences, Chubu University, 1200 Matsumoto-cho, Kasugai, Aichi, 487-8501, Japan.
Sachiko Kondo
Hirokazu Yagi
Prapon Wilairat
Hiroaki Hiramatsu
Morihiro Ito
Yasuhiko Ito
Koichi Kato
Yasuo Suzuki
Chubu University · JPJapan Science and Technology Agency · JPMahidol University · THNagoya City University · JPNagoya University · JPUniversity of Shizuoka · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The initial step essential in influenza virus infection is specific binding of viral hemagglutinin to host cell-surface glycan receptors. Influenza A virus specificity for the host is mediated by viral envelope hemagglutinin, that binds to receptors containing glycans with terminal sialic acids. Human viruses preferentially bind to alpha2-->6 linked sialic acids on receptors of host cells, whereas avian viruses are specific for the alpha2-->3 linkage on the target cells. Human influenza virus isolates more efficiently infect amniotic membrane (AM) cells than chorioallantoic membrane (CAM) cells. N-glycans were isolated from AM and CAM cells of 10-day-old chicken embryonated eggs and their structures were analyzed by multi-dimensional HPLC mapping and MALDI-TOF-MS techniques. Terminal N-acetylneuraminic acid contents in the two cell types were similar. However, molar percents of alpha2-->3 linkage preferentially bound by avian influenza virus were 27.2 in CAM cells and 15.4 in AM cells, whereas those of alpha2-->6 linkage favored by human influenza virus were 8.3 (CAM) and 14.2 (AM). Molar percents of sulfated glycans, recognized by human influenza virus, in CAM and AM cells were 3.8 and 12.7, respectively. These results have revealed structures and molar percents of N-glycans in CAM and AM cells important in determining human and avian influenza virus infection and viral adaptation.

Indexed as

Adaptation, BiologicalAmnionAnimalsBirdsCarbohydrate ConformationCarbohydrate SequenceChick EmbryoChorioallantoic MembraneChromatography, High Pressure LiquidHumansInfluenza A virusMolecular Sequence DataOvumPolysaccharidesPolysaccharides

Identifiers

PMID18853253
OpenAlexW2165796516

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.