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Identification of New Carbohydrate and Membrane Protein Antigens in Cardiac Xenotransplantation

Byrne, Guerard W., Stalboerger, Paul G., Du, Zeji, Davis, Tessa R., McGregor, Christopher G. A.·2011·Transplantation
DOI 10.1097/tp.0b013e318203c27dPMC PMC10022691
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  • Porcine cells display three major glycan antigens on their cell surface - α-Gal, Neu5Gc and Sd(a) - which are the products of GGTA1, CMAH and B4GALNT2/B4GALNT2L.

    “Porcine cells display three major glycan antigens on their cell surface — α-Gal15, Neu5Gc16 and Sd(a)17 (Fig. 1a) — which are the products of the corresponding glycan synthesis genes, glycoprotein α-galactosyltransferase 1 (GGTA1), cytidine monophospho-N-acetylneuraminic acid hydroxylase (CMAH) and β-1,4-N-acetyl-galactosaminyltransferase 2 (B4GALNT2)/B4GALNT2-like (B4GALNT2L).”

    From Design and testing of a humanized porcine donor for xenotransplantation (2023) · cites this paper as [17]

    The Discussion identifies a porcine B4GALNT2-like gene and links its product to a possible Sd(a)-like glycan on porcine vascular cells. It does not establish that those cells display Sd(a) itself: the authors say the glycan’s precise structure is unknown, and the anti-Sd(a) antibody did not bind the porcine aortic endothelial cells tested. The paper also does not identify B4GALNT2L. (LLM, conf=0.87)

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  • In addition to the glycan antigens, a vast array of porcine proteins may also be xenogenic.

    “We recognize that in addition to the glycan antigens, a vast array of porcine proteins may also be xenogenic17 and it may not be possible to identify and eliminate them all.”

    From Design and testing of a humanized porcine donor for xenotransplantation (2023) · cites this paper as [17]

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Research works printed but not linked: 32

  1. Platt, 1998, Acute vascular rejection., Xenotransplantation, 5, 169, 10.1111/j.1399-3089.1998.tb00024.x · DOI
  2. Cowan, 2007, Coagulation and the xenograft endothelium., Xenotransplantation, 14, 7, 10.1111/j.1399-3089.2006.00368.x · DOI
  3. Byrne, 2002, Evaluation of different alpha-galactosyl glycoconjugates for use in xenotransplantation., Bioconjug Chem, 13, 571, 10.1021/bc015565e · DOI
  4. Lai, 2002, Production of alpha-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning., Science, 295, 1089, 10.1126/science.1068228 · DOI
  5. Lam, 2004, Anti-non-Gal porcine endothelial cell antibodies in acute humoral xenograft rejection of hDAF-transgenic porcine hearts in cynomolgus monkeys., Xenotransplantation, 11, 531, 10.1111/j.1399-3089.2004.00175.x · DOI
  6. Chen, 2005, Acute rejection is associated with antibodies to non-Gal antigens in baboons using Gal-knockout pig kidneys., Nat Med, 11, 1295, 10.1038/nm1330 · DOI
  7. Rood, 2005, Preformed antibodies to alpha1,3-galactosyltransferase gene-knockout (GT-KO) pig cells in humans, baboons, and monkeys: Implications for xenotransplantation., Transplant Proc, 37, 3514, 10.1016/j.transproceed.2005.09.082 · DOI
  8. Buhler, 2003, An investigation of the specificity of induced anti-pig antibodies in baboons., Xenotransplantation, 10, 88, 10.1034/j.1399-3089.2003.01122.x · DOI
  9. Ezzelarab, 2006, Antibodies directed to pig non-Gal antigens in naïve and sensitized baboons., Xenotransplantation, 13, 400, 10.1111/j.1399-3089.2006.00320.x · DOI
  10. Byrne, 2008, Proteomic identification of non-Gal antibody targets after pig-to-primate cardiac xenotransplantation., Xenotransplantation, 15, 268, 10.1111/j.1399-3089.2008.00480.x · DOI
  11. Diswall, 2010, Structural characterization of alpha1,3-galactosyltransferase knockout pig heart and kidney glycolipids and their reactivity with human and baboon antibodies., Xenotransplantation, 17, 48, 10.1111/j.1399-3089.2009.00564.x · DOI
  12. Blixt, 2009, Anticarbohydrate antibody repertoires in patients transplanted with fetal pig islets revealed by glycan arrays., Am J Transplant, 9, 83, 10.1111/j.1600-6143.2008.02471.x · DOI
  13. Davila, 2006, T-cell responses during pig-to-primate xenotransplantation., Xenotransplantation, 13, 31, 10.1111/j.1399-3089.2005.00258.x · DOI
  14. Keusch, 2000, Expression cloning of a new member of the ABO blood group glycosyltransferases, iGb3 synthase, that directs the synthesis of Isoglobo-glycosphingolipids., J Biol Chem, 275, 25308, 10.1074/jbc.M002629200 · DOI
  15. Kitamura, 1995, Efficient screening of retroviral cDNA expression libraries., Proc Natl Acad Sci USA, 92, 9146, 10.1073/pnas.92.20.9146 · DOI
  16. Dorman, 1978, Genetic analysis of the human cell surface: Antigenic marker for the human X chromosome in human-mouse hybrids., Proc Natl Acad Sci USA, 75, 2363, 10.1073/pnas.75.5.2363 · DOI
  17. Liszewski, 1991, Membrane cofactor protein (MCP or CD46): Newest member of the regulators of complement activation gene cluster., Annu Rev Immunol, 9, 431, 10.1146/annurev.iy.09.040191.002243 · DOI
  18. Meri, 1990, Human protectin (CD59), an 18,000–20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 into lipid bilayers., Immunology, 71, 1
  19. Ling, 2004, Annexin II regulates fibrin homeostasis and neoangiogenesis in vivo., J Clin Invest, 113, 38, 10.1172/JCI19684 · DOI
  20. Cesarman-Maus, 2006, Autoantibodies against the fibrinolytic receptor, annexin 2, in antiphospholipid syndrome., Blood, 107, 4375, 10.1182/blood-2005-07-2636 · DOI
  21. Cockrell, 2008, Annexin A2: Biology and relevance to the antiphospholipid syndrome., Lupus, 17, 943, 10.1177/0961203308095329 · DOI
  22. Kawakatsu, 1993, Antithrombotic effect of an anti-glycoprotein IIB/IIIA antibody in primate lethal thrombosis., Thromb Res, 70, 245, 10.1016/0049-3848(93)90131-7 · DOI
  23. Forsyth, 1991, Anti-CD9 antibodies augment neutrophil adherence to endothelium., Immunology, 72, 292
  24. Van de Wouwer, 2004, Thrombomodulin-protein C-EPCR system: Integrated to regulate coagulation and inflammation., Arterioscler Thromb Vasc Biol, 24, 1374, 10.1161/01.ATV.0000134298.25489.92 · DOI
  25. Esmon, 2004, Structure and functions of the endothelial cell protein C receptor., Crit Care Med, 32, S298, 10.1097/01.CCM.0000126128.64614.81 · DOI
  26. Renton, 1967, Anti-Sd(a), a new blood group antibody., Vox Sang, 13, 493
  27. Montiel, 2003, Molecular cloning, gene organization and expression of the human UDP-GalNAc:Neu5Acalpha2-3Galbeta-R beta1,4-N-acetylgalactosaminyltransferase responsible for the biosynthesis of the blood group Sda/Cad antigen: Evidence for an unusual extended cytoplasmic domain., Biochem J, 373, 369, 10.1042/bj20021892 · DOI · Paper page
  28. Malagolini, 1994, Identification and characterization of the Sda beta 1,4, N-acetylgalactosaminyltransferase from pig large intestine., Glycoconj J, 11, 89, 10.1007/BF00731148 · DOI
  29. Wu, 1998, Differential binding of human blood group Sd(a+) and Sd(a−) Tamm-Horsfall glycoproteins with Dolichos biflorus and Vicia villosa-B4 agglutinins., FEBS Lett, 429, 323, 10.1016/S0014-5793(98)00617-6 · DOI
  30. Smith, 2006, Blood groups and transfusions in pigs., Xenotransplantation, 13, 186, 10.1111/j.1399-3089.2006.00299.x · DOI
  31. Johnson, 2002, Cultivation and characterization of coronary microvascular endothelial cells: A novel porcine model using micropigs., Microvasc Res, 64, 278, 10.1006/mvre.2002.2423 · DOI
  32. Solanes, 2005, Histological basis of the porcine femoral artery for vascular research., Anat Histol Embryol, 34, 105, 10.1111/j.1439-0264.2004.00580.x · DOI

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Metadata

Authors
Byrne, G. W., Stalboerger, P. G., Du, Z., Davis, T. R., & McGregor, C. G. A.
Venue
Transplantation
Publisher
Ovid Technologies (Wolters Kluwer Health)
Published
2011-02-15
Volume
91
Issue
3
Pages
287-292
ISSN
0041-1337
DOI
10.1097/tp.0b013e318203c27d
PMC
PMC10022691
Cited by
118
References
0
Language
en

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