Evidence map›Paper›PMID 19704115›Full record

ArticleBlood2009

ABO blood group glycans modulate sialic acid recognition on erythrocytes.

Miriam Cohen, Nancy Hurtado-Ziola, Ajit Varki

Open access · bronzeAbstract read
In one paragraph

Article in Blood, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

41 citing papers in PubMed, 80 citations in OpenAlex.

  1. Trial
  2. Article
  3. Ficolin-1 in pediatricInfection and immunity · 2025
    Article
  4. Article
  5. A Computational and Chemical Design Strategy for Manipulating Glycan-Protein Recognition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  6. Article
  7. Article
  8. Review
  9. SialylatedJournal of extracellular biology · 2022
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. Probing the binding specificities of human Siglecs by cell-based glycan arrays.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

3 authors at 1 institution in 1 country.

Miriam CohenGlycobiology Research and Training Center, Departments of Medicine and Cellular and Molecular Medicine, University of California, San Diego, La Jolla, CA, USA.
Nancy Hurtado-Ziola
Ajit Varki
University of California, San Diego · US

Funding

U of Calif, San Diego Neuroscience Microscopy ImagingP30NS047101 · NINDS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GLEESON, JOSEPH G, ZHENG, BINHAI · 2003 to 2022
$9.0M
BIOSYNTHESIS AND REGULATION OF SUBSTITUTED SIALIC ACIDSR01GM032373 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VARKI, AJIT P · 1985 to 2022
$6.9M
SULFATED OLIGOSACCHARIDES OF NORMAL AND MALIGNANT CELLSR01CA038701 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI VARKI, AJIT P · 1985 to 2015
$5.5M
NCI NIH HHS R01 CA038701NCI NIH HHS R01CA38701NIGMS NIH HHS R01 GM032373NIGMS NIH HHS R01GM032373NINDS NIH HHS NS047101NINDS NIH HHS P30 NS047101
6 · The paper itself

Abstract

ABH(O) blood group polymorphisms are based on well-known intraspecies variations in structures of neutral blood cell surface glycans in humans and other primates. Whereas natural antibodies against these glycans can act as barriers to blood transfusion and transplantation, the normal functions of this long-standing evolutionary polymorphism remain largely unknown. Although microbial interactions have been suggested as a selective force, direct binding of lethal pathogens to ABH antigens has not been reported. We show in this study that ABH antigens found on human erythrocytes modulate the specific interactions of 3 sialic acid-recognizing proteins (human Siglec-2, 1918SC influenza hemagglutinin, and Sambucus nigra agglutinin) with sialylated glycans on the same cell surface. Using specific glycosidases that convert A and B glycans to the underlying H(O) structure, we show ABH antigens stabilize sialylated glycan clusters on erythrocyte membranes uniquely for each blood type, generating differential interactions of the 3 sialic acid-binding proteins with erythrocytes from each blood type. We further show that by stabilizing such structures ABH antigens can also modulate sialic acid-mediated interaction of pathogens such as Plasmodium falciparum malarial parasite. Thus, ABH antigens can noncovalently alter the presentation of other cell surface glycans to cognate-binding proteins, without themselves being a direct ligand.

Indexed as

ABO Blood-Group SystemAnimalsBlood Group AntigensChlorocebus aethiopsCOS CellsEnzyme-Linked Immunosorbent AssayErythrocytesFlow CytometryHemagglutininsHumansMalaria, FalciparumN-Acetylneuraminic AcidPlant LectinsPlasmodium falciparumPolysaccharidesRibosome Inactivating ProteinsABO Blood-Group SystemBlood Group AntigensHemagglutininsN-Acetylneuraminic AcidPlant LectinsPolysaccharidesRibosome Inactivating ProteinsSambucus nigra lectinsSialic Acid Binding Ig-like Lectin 2

Identifiers

PMID19704115
PMCPMC2766682
OpenAlexW2012799331

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.