Advanced search
Publication Cover
Expert Opinion on Biological Therapy Volume 9, 2009 - Issue 8
Submit an article Journal homepage
177
Views
19
CrossRef citations to date
0
Altmetric
Reviews

Structural biology of carbohydrate xenoantigens

Elizabeth Yuriev Monash University, Monash Institute of Pharmaceutical Sciences, Medicinal Chemistry and Drug Action, Parkville, Victoria 3052, Australia
,
Mark Agostino Monash University, Monash Institute of Pharmaceutical Sciences, Medicinal Chemistry and Drug Action, Parkville, Victoria 3052, Australia
,
William Farrugia Centre for Immunology, Burnet Institute, Kronheimer Building (Austin Health), Studley Road, Heidelberg, Victoria 3084, Australia +61 3 9282 2111; +61 3 9282 2100; [email protected]
,
Dale Christiansen The University of Melbourne, Department of Surgery (Austin Health/Northern Heath), Heidelberg, Victoria 3084, Australia
,
Mauro S Sandrin The University of Melbourne, Department of Surgery (Austin Health/Northern Heath), Heidelberg, Victoria 3084, Australia
&
Paul A Ramsland Centre for Immunology, Burnet Institute, Kronheimer Building (Austin Health), Studley Road, Heidelberg, Victoria 3084, Australia +61 3 9282 2111; +61 3 9282 2100; [email protected]; The University of Melbourne, Department of Surgery (Austin Health/Northern Heath), Heidelberg, Victoria 3084, Australia; Monash University, Alfred Medical Research and Education Precinct, Department of Immunology, Melbourne, Victoria 3004, Australia
Pages 1017-1029 | Published online: 11 Jul 2009

Bibliography

  • Galili U. Xenotransplantation and ABO incompatible transplantation: the similarities they share. Transfus Apher Sci 2006;35:45-58
  • Holgersson J, Gustafsson A, Breimer ME. Characteristics of protein–carbohydrate interactions as a basis for developing novel carbohydrate-based antirejection therapies. Immunol Cell Biol 2005;83:694-708
  • Ramsland P. Blood brothers: carbohydrates in xenotransplantation and cancer immunotherapy. Immunol Cell Biol 2005;83:315-7
  • Roux FA, Sai P, Deschamps JY. Xenotransfusions, past and present. Xenotransplantation 2007;14:208-16
  • Cooper DK, Ezzelarab M, Hara H, Ayares D. Recent advances in pig-to-human organ and cell transplantation. Expert Opin Biol Ther 2008;8:1-4
  • Cooper DK, Good AH, Koren E, et al. Identification of α-galactosyl and other carbohydrate epitopes that are bound by human anti-pig antibodies: relevance to discordant xenografting in man. Transpl Immunol 1993;1:198-205
  • Sandrin MS, McKenzie IF. Galα(1,3)Gal, the major xenoantigen(s) recognised in pigs by human natural antibodies. Immunol Rev 1994;141:169-90
  • Nydegger U, Mohacsi P, Koestner S, et al. ABO histo-blood group system-incompatible allografting. Int Immunopharmacol 2005;5:147-53
  • Baldwin WM 3rd, Paul LC, Claas FH, Daha MR. Destructive and protective effects of antibody on transplants in humans: practical and theoretical considerations. Prog Clin Biol Res 1986;224:41-67
  • Porter KA. The effects of antibodies on human renal allografts. Transplant Proc 1976;8:189-97
  • Baumann BC, Stussi G, Huggel K, et al. Reactivity of human natural antibodies to endothelial cells from Galα(1,3)Gal-deficient pigs. Transplantation 2007;83:193-201
  • Galili U, Macher BA, Buehler J, Shohet SB. Human natural anti-α-galactosyl IgG. II. The specific recognition of α(1-3)-linked galactose residues. J Exp Med 1985;162:573-82
  • Good AH, Cooper DK, Malcolm AJ, et al. Identification of carbohydrate structures that bind human antiporcine antibodies: implications for discordant xenografting in humans. Transplant Proc 1992;24:559-62
  • Sandrin MS, Vaughan HA, Dabkowski PL, Mckenzie IF. Anti-pig IgM antibodies in human serum react predominantly with Gal(α 1–3)Gal epitopes. Proc Natl Acad Sci USA 1993;90:11391-5
  • Dai Y, Vaught TD, Boone J, et al. Targeted disruption of the α1,3-galactosyltransferase gene in cloned pigs. Nat Biotechnol 2002;20:251-5
  • Lai L, Kolber-Simonds D, Park KW, et al. Production of α-1,3-galactosyltransferase knockout pigs by nuclear transfer cloning. Science 2002;295:1089-92
  • Phelps CJ, Koike C, Vaught TD, et al. Production of α1,3-galactosyltransferase-deficient pigs. Science 2003;299:411-4
  • Nottle MB, Beebe LF, Harrison SJ, et al. Production of homozygous α-1,3-galactosyltransferase knockout pigs by breeding and somatic cell nuclear transfer. Xenotransplantation 2007;14:339-44
  • Milland J, Christiansen D, Lazarus BD, et al. The molecular basis for Galα(1,3)Gal expression in animals with a deletion of the α1,3galactosyltransferase gene. J Immunol 2006;176:2448-54
  • Sharma A, Naziruddin B, Cui C, et al. Pig cells that lack the gene for α1-3 galactosyltransferase express low levels of the gal antigen. Transplantation 2003;75:430-6
  • Milland J, Christiansen D, Sandrin MS. α1,3-galactosyltransferase knockout pigs are available for xenotransplantation: are glycosyltransferases still relevant? Immunol Cell Biol 2005;83:687-93
  • Larsen RD, Rajan VP, Ruff MM, et al. Isolation of a cDNA encoding a murine UDPgalactose:β-D-galactosyl-1, 4-N-acetyl-D-glucosaminide α-1, 3-galactosyltransferase: expression cloning by gene transfer. Proc Natl Acad Sci USA 1989;86:8227-31
  • Lazarus BD, Milland J, Ramsland PA, et al. Histidine 271 has a functional role in pig α-1,3galactosyltransferase enzyme activity. Glycobiology 2002;12:793-802
  • Galili U, Shohet SB, Kobrin E, et al. Man, apes, and Old World monkeys differ from other mammals in the expression of α-galactosyl epitopes on nucleated cells. J Biol Chem 1988;263:17755-62
  • Larsen RD, Rivera-Marrero CA, Ernst LK, et al. Frameshift and nonsense mutations in a human genomic sequence homologous to a murine UDP-Gal:β-D-Gal(1,4)-D-GlcNAc α(1,3)-galactosyltransferase cDNA. J Biol Chem 1990;265:7055-61
  • Keusch JJ, Manzella SM, Nyame KA, et al. Expression cloning of a new member of the ABO blood group glycosyltransferases, iGb3 synthase, that directs the synthesis of isoglobo-glycosphingolipids. J Biol Chem 2000;275:25308-14
  • Taylor SG, Mckenzie IF, Sandrin MS. Characterization of the rat α(1,3)galactosyltransferase: evidence for two independent genes encoding glycosyltransferases that synthesize Galα(1,3)Gal by two separate glycosylation pathways. Glycobiology 2003;13:327-37
  • Kiernan K, Harnden I, Gunthart M, et al. The anti-non-gal xenoantibody response to xenoantigens on gal knockout pig cells is encoded by a restricted number of germline progenitors. Am J Transplant 2008;8:1829-39
  • Diswall M, Angstrom J, Schuurman HJ, et al. Studies on glycolipid antigens in small intestine and pancreas from α1,3-galactosyltransferase knockout miniature swine. Transplantation 2007;84:1348-56
  • Puga Yung G, Schneider MK, Seebach JD. Immune responses to α1,3 galactosyltransferase knockout pigs. Curr Opin Organ Transplant 2009;14:154-60
  • Christiansen D, Milland J, Mouhtouris E, et al. Humans lack iGb3 due to the absence of functional iGb3-synthase: implications for NKT cell development and transplantation. PLoS Biol 2008;6:e172. Published online 15 July 2008, doi:10.1371/journal.pbio.0060172
  • Speak AO, Cerundolo V, Platt FM. CD1d presentation of glycolipids. Immunol Cell Biol 2008;86:588-97
  • Grahn E, Askarieh G, Holmner A, et al. Crystal structure of the Marasmius oreades mushroom lectin in complex with a xenotransplantation epitope. J Mol Biol 2007;369:710-21
  • Greco A, Ho JG, Lin SJ, et al. Carbohydrate recognition by Clostridium difficile toxin A. Nat Struct Mol Biol 2006;13:460-1
  • Walser PJ, Haebel PW, Kunzler M, et al. Structure and functional analysis of the fungal galectin CGL2. Structure 2004;12:689-702
  • Teneberg S, Lonnroth I, Torres Lopez JF, et al. Molecular mimicry in the recognition of glycosphingolipids by Galα3Galβ4GlcNAcβ-binding Clostridium difficile toxin A, human natural anti α-galactosyl IgG and the monoclonal antibody Gal-13: characterization of a binding-active human glycosphingolipid, non-identical with the animal receptor. Glycobiology 1996;6:599-609
  • Kirkeby S, Winter HC, Goldstein IJ. Comparison of the binding properties of the mushroom Marasmius oreades lectin and Griffonia simplicifolia I-B4 isolectin to αgalactosyl carbohydrate antigens in the surface phase. Xenotransplantation 2004;11:254-61
  • Blanchard B, Nurisso A, Hollville E, et al. Structural basis of the preferential binding for globo-series glycosphingolipids displayed by Pseudomonas aeruginosa lectin I. J Mol Biol 2008;383:837-53
  • Natchiar SK, Srinivas O, Mitra N, et al. Structural studies on peanut lectin complexed with disaccharides involving different linkages: further insights into the structure and interactions of the lectin. Acta Crystallogr D Biol Crystallogr 2006;62:1413-21
  • Tempel W, Tschampel S, Woods RJ. The xenograft antigen bound to Griffonia simplicifolia lectin 1-B4. X-ray crystal structure of the complex and molecular dynamics characterization of the binding site. J Biol Chem 2002;277:6615-21
  • Lescar J, Loris R, Mitchell E, et al. Isolectins I-A and I-B of Griffonia (Bandeiraea) simplicifolia. Crystal structure of metal-free GS I-B4 and molecular basis for metal binding and monosaccharide specificity. J Biol Chem 2002;277:6608-14
  • Milland J, Yuriev E, Xing PX, et al. Carbohydrate residues downstream of the terminal Galα(1,3)Gal epitope modulate the specificity of xenoreactive antibodies. Immunol Cell Biol 2007;85:623-32
  • Kirkeby S, Moe D. Lectin interactions with α-galactosylated xenoantigens. Xenotransplantation 2002;9:260-7
  • Imberty A, Mikros E, Koca J, et al. Computer simulation of histo-blood group oligosaccharides: energy maps of all constituting disaccharides and potential energy surfaces of 14 ABH and Lewis carbohydrate antigens. Glycoconj J 1995;12:331-49
  • Strotz CA, Cerezo AS. Use of a general purpose force-field (MM2) for the conformational analysis of the disaccharide α-D-galactopyranosyl-(1-3)-β-D-galactopyranose. J Carb Chem 1994;13:235-47
  • Corzana F, Bettler E, Herve DU, et al. Solution structure of two xenoantigens: αGal-LacNAc and αGal-Lewis X. Glycobiology 2002;12:241-50
  • Li J, Ksebati MB, Zhang W, et al. Conformational analysis of an α-galactosyl trisaccharide epitope involved in hyperacute rejection upon xenotransplantation. Carbohydr Res 1999;315:76-88
  • Otter A, Lemieux RU, Ball RG, et al. Crystal state and solution conformation of the B blood group trisaccharide α-L-Fucp-(1→2)- [α-D-Galp]-(1→3)]-β-D-Galp-OCH3. Eur J Biochem 1999;259:295-303
  • Lamba D, Segre AL, Glover S, et al. Molecular structure of 3-O-(3,6-anhydro-α-D-galactopyranosyl)-β-D-galactopyranose (neocarrabiose) in the solid state and in solution: an investigation by X-ray crystallography, n.m.r. spectroscopy, and molecular mechanics calculations. Carbohydr Res 1990;208:215-30
  • Yuriev E, Farrugia W, Scott AM, Ramsland PA. Three-dimensional structures of carbohydrate determinants of Lewis system antigens: implications for effective antibody targeting of cancer. Immunol Cell Biol 2005;83:709-17
  • Ramsland PA, Farrugia W, Yuriev E, et al. Evidence for structurally conserved recognition of the major carbohydrate xenoantigen by natural antibodies. Cell Mol Biol (Noisy-le-grand) 2003;49:307-17
  • Lee M, Lloyd P, Zhang X, et al. Shapes of antibody binding sites: qualitative and quantitative analyses based on a geomorphic classification scheme. J Org Chem 2006;71:5082-92
  • Ramsland PA, Farrugia W, Bradford TM, et al. Structural convergence of antibody binding of carbohydrate determinants in Lewis Y tumor antigens. J Mol Biol 2004;340:809-18
  • Calarese DA, Scanlan CN, Zwick MB, et al. Antibody domain exchange is an immunological solution to carbohydrate cluster recognition. Science 2003;300:2065-71
  • Cygler M, Rose DR, Bundle DR. Recognition of a cell-surface oligosaccharide of pathogenic Salmonella by an antibody Fab fragment. Science 1991;253:442-5
  • Vulliez-Le Normand B, Saul FA, Phalipon A, et al. Structures of synthetic O-antigen fragments from serotype 2a Shigella flexneri in complex with a protective monoclonal antibody. Proc Natl Acad Sci USA 2008;105:9976-81
  • McKenzie IF, Li YQ, Patton K, et al. A murine model of antibody-mediated hyperacute rejection by galactose-α(1,3)galactose antibodies in Gal o/o mice. Transplantation 1998;66:754-63
  • Nozawa S, Xing PX, Wu GD, et al. Characteristics of immunoglobulin gene usage of the xenoantibody binding to gal-α(1,3)gal target antigens in the gal knockout mouse. Transplantation 2001;72:147-55
  • Yuriev E, Sandrin MS, Ramsland PA. Antibody-ligand docking: insights into peptide–carbohydrate mimicry. Mol Simulation 2008;34:461-8
  • Ekser B, Rigotti P, Gridelli B, Cooper DK. Xenotransplantation of solid organs in the pig-to-primate model. Transpl Immunol 2009;21:87-92
  • Cowan PJ, d'Apice AJ. Complement activation and coagulation in xenotransplantation. Immunol Cell Biol 2009;87:203-8
  • Sandrin MS. Gal knockout pigs: any more carbohydrates? Transplantation 2007;84:8-9
  • Tangvoranuntakul P, Gagneux P, Diaz S, et al. Human uptake and incorporation of an immunogenic nonhuman dietary sialic acid. Proc Natl Acad Sci USA 2003;100:12045-50
  • Cairns T, Lee J, Goldberg LC, et al. Thomsen-Friedenreich and PK antigens in pig-to-human xenotransplantation. Transplant Proc 1996;28:795-6
  • Bouhours D, Liaigre J, Naulet J, et al. A novel pentaglycosylceramide in ostrich liver, IV4-β-Gal-nLc4Cer, with terminal Gal(β1-4)Gal, a xenoepitope recognized by human natural antibodies. Glycobiology 2000;10:857-64
  • Lucq J, Tixier D, Guinault AM, et al. The target antigens of naturally occurring human anti-β-galactose IgG are cryptic on porcine aortic endothelial cells. Xenotransplantation 2000;7:3-13
  • Christiansen D, Mouhtouris E, Milland J, et al. Recognition of a carbohydrate xenoepitope by human NKRP1A (CD161). Xenotransplantation 2006;13:440-6
  • Varki A. Glycan-based interactions involving vertebrate sialic-acid-recognizing proteins. Nature 2007;446:1023-9
  • Zhu A, Hurst R. Anti-N-glycolylneuraminic acid antibodies identified in healthy human serum. Xenotransplantation 2002;9:376-81
  • Miwa Y, Kobayashi T, Nagasaka T, et al. Are N-glycolylneuraminic acid (Hanganutziu-Deicher) antigens important in pig-to-human xenotransplantation? Xenotransplantation 2004;11:247-53
  • Padler-Karavani V, Yu H, Cao H, et al. Diversity in specificity, abundance, and composition of anti-Neu5Gc antibodies in normal humans: potential implications for disease. Glycobiology 2008;18:818-30
  • Higashi H, Naiki M, Matuo S, Okouchi K. Antigen of “serum sickness” type of heterophile antibodies in human sera: indentification as gangliosides with N-glycolylneuraminic acid. Biochem Biophys Res Commun 1977;79:388-95
  • Chou HH, Takematsu H, Diaz S, et al. A mutation in human CMP-sialic acid hydroxylase occurred after the Homo-Pan divergence. Proc Natl Acad Sci USA 1998;95:11751-6
  • Byres E, Paton AW, Paton JC, et al. Incorporation of a non-human glycan mediates human susceptibility to a bacterial toxin. Nature 2008;456:648-52

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.