Evidence map›Paper›PMID 23824194›Full record

ArticleThe Journal of biological chemistry2013

Hemocytes and plasma of the eastern oyster (Crassostrea virginica) display a diverse repertoire of sulfated and blood group A-modified N-glycans.

Simone Kurz, Chunsheng Jin, Alba Hykollari, Daniel Gregorich, Barbara Giomarelli, Gerardo R Vasta, Iain B H Wilson, Katharina Paschinger

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 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
2.9field-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

30 citing papers in PubMed, 54 citations in OpenAlex.

  1. PNGaseL fromRoyal Society open science · 2025
    Article
  2. Species-SpecificMarine drugs · 2023
    Article
  3. Review
  4. Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  5. Review
  6. Review
  7. Article
  8. Glycosylation at an evolutionary nexus: the brittle starThe Journal of biological chemistry · 2020
    Article
  9. Sulfated and sialylatedThe Journal of biological chemistry · 2020
    Article
  10. Review
  11. Review
  12. Review
  13. Article
  14. Review
  15. The underestimated N-glycomes of lepidopteran species.Biochimica et biophysica acta. General subjects · 2017
    Article
  16. Article
  17. Analysis of Invertebrate and Protist N-Glycans.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  18. Review
  19. Article
  20. 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

8 authors at 3 institutions in 3 countries.

Simone KurzDepartment für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria.
Chunsheng Jin
Alba Hykollari
Daniel Gregorich
Barbara Giomarelli
Gerardo R Vasta
Iain B H Wilson
Katharina Paschinger
BOKU University · ATUniversity of Gothenburg · SEUniversity of Maryland, Baltimore · US

Funding

Biological Roles of GalectinsR01GM070589 · NIGMS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI VASTA, GERARDO RAUL · 2004 to 2013
$2.0M
Austrian Science Fund FWF P 21946Austrian Science Fund FWF W 1224NIGMS NIH HHS R01 GM070589
6 · The paper itself

Abstract

The eastern oyster (Crassostrea virginica) has become a useful model system for glycan-dependent host-parasite interactions due to the hijacking of the oyster galectin CvGal1 for host entry by the protozoan parasite Perkinsus marinus, the causative agent of Dermo disease. In this study, we examined the N-glycans of both the hemocytes, which via CvGal1 are the target of the parasite, and the plasma of the oyster. In combination with HPLC fractionation, exoglycosidase digestion, and fragmentation of the glycans, mass spectrometry revealed that the major N-glycans of plasma are simple hybrid structures, sometimes methylated and core α1,6-fucosylated, with terminal β1,3-linked galactose; a remarkable high degree of sulfation of such glycans was observed. Hemocytes express a larger range of glycans, including core-difucosylated paucimannosidic forms, whereas bi- and triantennary glycans were found in both sources, including structures carrying sulfated and methylated variants of the histo-blood group A epitope. The primary features of the oyster whole hemocyte N-glycome were also found in dominin, the major plasma glycoprotein, which had also been identified as a CvGal1 glycoprotein ligand associated with hemocytes. The occurrence of terminal blood group moieties on oyster dominin and on hemocyte surfaces can account in part for their affinity for the endogenous CvGal1.

Indexed as

ABO Blood-Group SystemAlveolataAnimalsBlood ProteinsCrassostreaEpitopesGalectinsHemocytesHost-Parasite InteractionsPolysaccharidesABO Blood-Group SystemBlood ProteinsEpitopesGalectinsPolysaccharidesGalectinGlycanGlycomicsInvertebratesMass Spectrometry (MS)Oligosaccharide

Identifiers

PMID23824194
PMCPMC3750142
OpenAlexW2010560524

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.