Definition of immunogenic carbohydrate epitopes

• Autorzy: Paschinger K. , Fabini G. , Schuster D. , Rendic D. , Wilson I.B.H.
• Języki publikacji: EN

Abstrakty

EN

Carbohydrates are known as sources of immunological cross-reactivity of allergenic significance. In celery and in cypress pollen, the major allergens Api g 5 and Cup a 1 are recognised by antisera raised against anti-horseradish peroxidase and by patients' IgE which apparently bind carbohydrate epitopes; mass spectrometric analysis of the tryptic peptides and of their N-glycans showed the presence of oligosaccharides carrying both xylose and core α1,3-fucose residues. Core α1,3-fucose residues are also a feature of invertebrates: genetic and biochemical studies on the fruitfly Drosophila melanogaster, the parasitic trematode Schistosoma mansoni and the nematode worm Caenorhabditis elegans indicate that these organisms possess core α1,3-fucosyltransferases. Various experiments have shown that fucosyltransferases from both fly and worm are responsible in vivo and in vitro for the synthesis of N-glycans which cross-react with anti-horseradish peroxidase; thus, we can consider these enzymes as useful tools in generating standard compounds for testing cross-reactive carbohydrate epitopes of allergenic interest.

Słowa kluczowe

EN

cypress; pollen; Drosophila; allergy; plant glycoprotein; carbohydrate; Caenorhabditis; celery; plant

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2005
• Tom: 52
• Numer: 3
• Opis fizyczny: p.629-632,fig.,ref.

Twórcy

autor

Paschinger K.

• Universitat fur Bodenkultur, Wien, Austria

autor

Fabini G.

autor

Schuster D.

autor

Rendic D.

autor

Wilson I.B.H.

Bibliografia

• Afferni C, Iacovacci P, Barletta B, Di Felice G, Tinghino R, Mari A, Pini C (1999) Role of carbohydrate moieties in IgE binding to allergenic components of Cupressus arizonica pollen extract. Clin Exp Allergy 29: 1087–1094.
• Alisi C, Afferni A, Iacovacci P, Barletta B, Tinghino R, Butteroni C, Puggioni EMR, Wilson IBH, Federico R, Schininà ME, Ariano R, Di Felice G, Pini C (2001) Rapid isolation characterization and glycan analysis of Cup a 1 the major allergen of Arizona cypress (Cupressus arizonica) pollen. Allergy 56: 978–984.
• Bencúrová M, Hemmer W, Focke-Tejkl M, Wilson IBH, Altmann F (2004) Specificity of IgG and IgE antibodies against plant and insect glycoprotein glycans determined with artificial glycoforms of human transferrin. Glycobiology 14: 457–466.
• Bublin M, Radauer C, Wilson IBH, Kraft D, Scheiner O, Breiteneder H, Hoffmann-Sommergruber K (2003) Cross-reactive N-glycans of Api g 5 a high molecular weight glycoprotein allergen from celery are required for immunoglobulin E binding and activation of effector cells from allergic patients. FASEB J 17: 1697–1699.
• Fabini G, Freilinger A, Altmann F, Wilson IBH (2001) Identification of core α13-fucosylated glycans and the requisite fucosyltransferase in Drosophila melanogaster. Potential basis of the neural anti-horseradish peroxidase epitope. J Biol Chem 276: 28058–28067.
• Faveeuw C, Mallevaey T, Paschinger K, Wilson IBH, Fontaine J, Mollicone R, Oriol R, Altmann F, Lerouge P, Capron M, Trottein F (2003) Schistosome N-glycans containing core α3-fucose and core β2-xylose epitopes are strong inducers of Th2 responses in mice. Eur J Immunol 33: 1271–1281.
• Fötisch K, Vieths S (2001) N- and O-linked oligosaccharides of allergenic glycoproteins. Glycoconj J 18: 373–390.
• Haase A, Stern M, Wachtler K, Bicker G (2001) A tissuespecific marker of Ecdysozoa. Dev Genes Evol 211: 428–433.
• Harnett W, Harnett MM (2001) Modulation of the host immune system by phosphorylcholine-containing glycoproteins secreted by parasitic filarial nematodes. Biochim Biophys Acta 1539: 7–15.
• Haslam SM, Dell A (2003) Hallmarks of Caenorhabditis elegans N-glycosylation: complexity and controversy. Biochimie 85: 25–32.
• Jan LY, Jan YN (1982) Antibodies to horseradish peroxidase as specific neuronal markers in Drosophila and in grasshopper embryos. Proc Natl Acad Sci USA 79: 2700–2704.
• Khoo KH, Chatterjee D, Caulfield JP, Morris HR, Dell A (1997) Structural mapping of the glycans from the egg glycoproteins of Schistosoma mansoni and Schistosoma japonicum: Identification of novel core structures and terminal sequences. Glycobiology 7: 663–677.
• Paschinger K, Rendic D, Lochnit G, Jantsch V, Wilson IBH (2004) Molecular basis of anti-horseradish peroxidase staining in Caenorhabditis elegans. J Biol Chem 279: 49588–49598.
• Prenner C, Mach L, Glössl J, März L (1992) The antigenicity of the carbohydrate moiety of an insect glycoprotein honey-bee (Apis mellifera) venom phospholipase A2. The role of α1,3-fucosylation of the asparagine-bound N-acetylglucosamine. Biochem J 284: 377–380.
• Seppo A, Moreland M, Schweingruber H, Tiemeyer M (2000) Zwitterionic and acidic glycosphingolipids of the Drosophila melanogaster embryo. Eur J Biochem 267: 3549–3558.
• Siddiqui SS, Culotti JG (1991) Examination of neurons in wild type and mutants of Caenorhabditis elegans using antibodies to horseradish peroxidase. J Neurogenet 7: 193–211.
• Snow PM, Patel NH, Harrelson AL, Goodman CS (1987) Neural-specific carbohydrate moiety shared by many surface glycoproteins in Drosophila and grasshopper embyros. J Neurosci 7: 4137–4144.
• Tawill S, Le Goff L, Ali F, Blaxter M, Allen JE (2004) Both free-living and parasitic nematodes induce a characteristic Th2 response that is dependent on the presence of intact glycans. Infect Immun 72: 398–407.
• van Die I, Gomord V, Kooyman FNJ, van der Berg TK, Cummings RD, Vervelde L (1999) Core α13-fucose is a common modifcation of N-glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonchus contortus infected sheep. FEBS Lett 463: 189–193.
• van Ree R (2002) Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases. Int Arch Allergy Immunol 129: 189–197.
• Wilson IBH (2002) Glycosylation of proteins in plants and invertebrates. Curr Opin Struct Biol 12: 569–577.
• Wilson IBH, Harthill JE, Mullin NP, Ashford DΑ, Αltmann F (1998) Core α1,3-fucose is a key part of the epitope recognized by antibodies reacting against plant Nlinked oligosaccharides and is present in a wide variety of plant extracts. Glycobiology 8: 651–661.