Evidence map›Paper›PMID 26755806›Full record

ArticleGlycobiology2016

Diverse molecular recognition properties of blood group A binding monoclonal antibodies.

Jeffrey C Gildersleeve, Whitney Shea Wright

Open access · hybridAbstract read
In one paragraph

Article in Glycobiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-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

18 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Review
  3. Serum antibody screening using glycan arrays.Chemical Society reviews · 2024
    Review
  4. Article
  5. Article
  6. Characterization of ABH-subtype donor-specific antibodies in ABO-A-incompatible kidney transplantation.American journal of transplantation : official journal of the American Society of Transplantation and the American Society of Transplant Surgeons · 2021
    Article
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  9. Article
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Article
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  18. 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

2 authors at 2 institutions in 1 country.

Jeffrey C GildersleeveChemical Biology Laboratory, National Cancer Institute, NIH, 376 Boyles St., Frederick, MD 21702, USA gildersj@mail.nih.gov.
Whitney Shea WrightChemical Biology Laboratory, National Cancer Institute, NIH, 376 Boyles St., Frederick, MD 21702, USA.
Frederick National Laboratory for Cancer Research · USNational Cancer Institute · US

Funding

Structural Basis of Immune Recognition of Glycosylated AntigensU54GM062116 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI SASISEKHARAN, RAM · 2001 to 2010
$80.3M
Carbohydrate Microarray Profiling of Glycan-Binding Antibodies and LectinsZIABC010740 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI GILDERSLEEVE, JEFFREY · 2009 to 2025
$10.7M
Intramural NIH HHSNIGMS NIH HHS U54 GM062116
6 · The paper itself

Abstract

Information about specificity and affinity is critical for use of carbohydrate-binding antibodies. Herein, we evaluated eight monoclonal antibodies to the blood group A (BG-A) antigen. Antibodies 87-G, 9A, HE-10, HE-24, HE-193, HE-195, T36 and Z2A were profiled on a glycan microarray to assess specificity, relative affinity and the influence of glycan density on recognition. Our studies highlight several noteworthy recognition properties. First, most antibodies bound GalNAcα1-3Gal and the BG-A trisaccharide nearly as well as larger BG-A oligosaccharides. Second, several antibodies only bound the BG-A trisaccharide when displayed on certain glycan chains. These first two points indicate that the carrier glycan chains primarily influence selectivity, rather than binding strength. Third, binding of some antibodies was highly dependent on glycan density, illustrating the importance of glycan presentation for recognition. Fourth, some antibodies recognized the tumor-associated Tn antigen, and one antibody only bound the variant composed of a GalNAc-alpha-linked to a serine residue. Collectively, these results provide new insights into the recognition properties of anti-BG-A antibodies.

Indexed as

ABO Blood-Group SystemAntibodies, Monoclonal, Murine-DerivedHumansTrisaccharidesABO Blood-Group SystemAntibodies, Monoclonal, Murine-DerivedTrisaccharidesAnti-glycan antibodiesblood group antigenglycan microarray

Identifiers

PMID26755806
PMCPMC4813731
OpenAlexW2253687527

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.