Evidence map›Paper›PMID 24033743›Full record

ArticleXenotransplantation

N-linked glycan profiling of GGTA1/CMAH knockout pigs identifies new potential carbohydrate xenoantigens.

Christopher Burlak, Marshall Bern, Alejandro E Brito, Dragan Isailovic, Zheng-Yu Wang, Jose L Estrada, Ping Li, A Joseph Tector

Abstract read
In one paragraph

Article in Xenotransplantation. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

29 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Complement, Coagulation, and Fibrinolysis: The Role of the Endothelium and Its Glycocalyx Layer in Xenotransplantation.Transplant international : official journal of the European Society for Organ Transplantation · 2024
    Review
  6. Regulatory macrophages in solid organ xenotransplantation.Korean journal of transplantation · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Progress towards xenogenic tolerance.Current opinion in organ transplantation · 2020
    Review
  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

8 authors at 4 institutions in 1 country.

Christopher BurlakDepartment of Surgery, Indiana University School of Medicine, Indianapolis, IN, USA.
Marshall Bern
Alejandro E Brito
Dragan Isailovic
Zheng-Yu Wang
Jose L Estrada
Ping Li
A Joseph Tector
Indiana University – Purdue University Indianapolis · USIndiana University School of MedicinePalo Alto Research Center · USUniversity of Toledo · US

Funding

Widely Distributed Software for Using Mass Spectrometry to Identify GlycansR01GM103428 · NIGMS · PALO ALTO RESEARCH CENTER · PI BERN, MARSHALL WAYNE · 2012 to 2013
$799k
NIGMS NIH HHS R01 GM103428
6 · The paper itself

Abstract

backgroundThe temporary or long-term xenotransplantation of pig organs into people would save thousands of lives each year if not for the robust human antibody response to pig carbohydrates. Genetically engineered pigs deficient in galactose α1,3 galactose (gene modified: GGTA1) and N-glycolylneuraminic acid (gene modified: CMAH) have significantly improved cell survival when challenged by human antibody and complement in vitro. There remains, however, a significant portion of human antibody binding.

methodsTo uncover additional xenoantigens, we compared the asparagine-linked (N-linked) glycome from serum proteins of humans, domestic pigs, GGTA1 knockout pigs, and GGTA1/CMAH knockout pigs using mass spectrometry. Carbohydrate structures were determined with assistance from GlycoWorkbench, Cartoonist, and SimGlycan software by comparison to existing database entries and collision-induced dissociation fragmentation data.

resultsMatrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) analysis of reduced and solid-phase permethylated glycans resulted in the detection of high-mannose, hybrid, and complex type N-linked glycans in the 1000-4500 m/z ion range. GGTA1/CMAH knockout pig samples had increased relative amounts of high-mannose, incomplete, and xylosylated N-linked glycans. All pig samples had significantly higher amounts of core and possibly antennae fucosylation.

conclusionsWe provide for the first time a comparison of the serum protein glycomes of the human, domestic pig, and genetically modified pigs important to xenotransplantation.

Indexed as

AnimalsAntigens, HeterophileCarbohydratesCarbohydrate SequenceCytidine Monophosphate N-Acetylneuraminic AcidGalactoseGalactosyltransferasesGene Knockout TechniquesHumansPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSus scrofaSwineTransplantation, Heterologousalpha-1,3-galactosyltransferase 1, porcineAntigens, HeterophileCarbohydratesCytidine Monophosphate N-Acetylneuraminic AcidGalactoseGalactosyltransferasesPolysaccharidesasparagine-linkedglycomeMALDI-TOF/TOFpermethylationserumxenotransplantation

Identifiers

PMID24033743
PMCPMC4593510
OpenAlexW2069934759

What OpenQuestion holds

Textmetadata
LicenceTDM
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.