2006, Number 1
<< Back
Alerg Asma Inmunol Pediatr 2006; 15 (1)
ENDO-β-1,3-glucanases recognized by IgE antibodies of people with latex-fruit pollen syndrome
Fuentes SD, Rodríguez RA
Language: Spanish
References: 47
Page: 35-42
PDF size: 156.77 Kb.
ABSTRACT
β-1,3-glucanases are widely distributed proteins in plants. They are involved in many metabolic processes such as stress, infection and development. They are able to hydrolyze β-1,3-glucans that are essential components of the cell wall in fungi and bacteria. So, they have been designated as pathogenesis-related proteins (Family 2: PR-2). To date, several β-1,3-glucanases of plants have been described, which are recognized by IgE antibodies of people with latex-fruit pollen syndrome. They have also been recognized as allergens involved in occupational asthma. At primary sequence level and despite they are from different species, there are high similarities among these proteins. Besides, the linear sequences recognized by IgE (sequential epitopes that have been reported recently for the banana β-1,3-glucanase) are conserved. These common epitopes could be the cause of crossed reactivity displayed among many allergens. This is relevant for people sensitized against these β-1,3-glucanases structures. This work compiles reported to date information about β-1,3-glucanases from plants implicated in allergies.
REFERENCES
Peumans WJ, Barre A, Derycke V, Rouge P, Wenling Z, May GD, Delcour JA, Van Leuven F, Van Damme EJM. Purification, characterization and structure analysis of an abundant b-1,3-glucanase from banana fruit. Eur J Biochem 2000; 267: 1188-1195.
Akiyama T, Shibuya N, Hrmova M, Fincher GB. Purification and characterization of a (1-3)-b-D-glucan endohydrolase from rice (Oryza sativa) bran. Carbohydrate Research 1997; 297: 365-374.
Huecas S, Villalba M, Rodríguez R. Ole e 9 a major olive pollen allergen is a 1,3-b-glucanase. J Biol Chem 2001; 276: 27656-27966.
Churngchow N, Suntaro A, Wititsuwannnakul R. b-1,3-glucanase isozymes the latex of Hevea brasiliensis. Phytochemistry 1995; 39: 505-509.
Subroto T, Van Koningsveld GA, Schreuder HA, Soedjanaatmadja UMS, Beintema JJ. Chitinase and b-1,3-glucanase in the lutoid-body fraction of Hevea latex. Phytochemistry 1996; 43: 29-37.
King TP, Norman PS. Isolation of allergens from ragweed pollen. Biochemistry 1962; 1: 709-720.
Marsh DG, Johnson P. The isolation and characterization of allergens from the pollen of rye grass (Lolium perenne). Eur Polymer J 1965; 1: 63-77.
Beezhold DH, Kostyal DA, Tomazic-Jezic VJ. Measurement of latex proteins and assessment of latex protein exposure. Methods 2002; 27: 46-51.
Bredehorst R, David K. What establishes a protein as an allergen? J Chromatography B 2001; 756: 33-40.
Aalberse RC, Akkerdaas JH, Van Ree R. Cross reactivity of IgE antibodies to allergens. Allergy 2001; 56: 478-490.
Rodríguez R, Villalba M, Batanero E, González EM, Monsalves RI, Huecas S, Tejera ML, Ledesma A. Allergenic diversity of the olive pollen. Allergy 2002; 57(Suppl. 71): 6-16.
Bircher AJ, Van Melle G, Haller E, Curty B, Frei PC. IgE to food allergens are highly prevalent in patients allergic to pollens, with and without symptoms of food allergy. Clin Exp Allergy 1994; 24: 367-374.
Wuthrich B, Stager J, Johansson SG. Celery allergy associated with birch and mugwort pollinosis. Allergy 1990; 45: 566-571.
Sussman G, Beezhold DH, Kurup VP. Allergens and natural rubber proteins. J Allergy Clin Immunol 2002; 110: 33-39.
Rihs-Hans P, Raulf-Heimsoth M. Natural Rubber latex allergens: Characterization and evaluation of their allergenic capacity. New Horizons Allergy 2003; 3: 2-8.
Van Loon LC, Pierpoint WS, Boller T, Conejero V. Recommendations of naming plant pathogenesis-related proteins. Plant Mol Biol Rep 1994; 12: 245-264.
Woolhiser MR, Munson AE, Meade BJ. Immunological responses of mice following administration of natural rubber latex proteins by different routes of exposure. Toxicological Science 2000; 55: 343-351.
Thanseem I, Joseph A, Thulaseedharan A. Induction and differential expression of b-1,3-glucanase mRNAs in tolerant and susceptible Hevea clones in response to infection by Phytophthora meadii. Tree Physiology 2005; 25: 1361-1368.
Hoffmann-Sommergruber K. Pathogenesis-related (PR)-proteins identified as allergens. Biochemical Society Transactions 2002; 30: 930-935.
Zhao H, Zhao H, Wang J, Wang B, Wang Y. Stress stimulation induced resistance of plant. Colloids and Surfaces B 2005; 43: 174-178.
Van Loon LC, Van Strien EA. The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 types proteins. Physiol Mol Plant Pathol 1999; 55: 85-97.
Van den Bulcke M, Bauw G, Castresana C, van Montagu M, Vandekerckhove J. Characterization of vacuolar and extracellular b(1,3)-glucanases of tobacco: evidence for a strictly compartmentalized plant defense system. Proc Natl Acad Sci USA 1989; 86: 2673-2677.
Van Kan JAL, Joosten MHAJ, Wagemakers CAM, Van den Berg-Velthuis GCM, de Wit PJGM. Differential accumulation of mRNAs encoding extracellular and intracellular PR-proteins in tomato induced by virulent and avirulent races of Cladosporium fulvum. Plant Mol Biol 1992; 20: 513-527.
Vögeli-Lange R, Fründt C, Hart CM, Beffa R, Nagy F, Meins F Jr. Evidence for a role of b-1,3-glucanase in dicot seed germination. Plant J 1994; 5: 273-278.
Leubner-Metzger O, Fründt C, Vögeli-Lange R, Meins F Jr. Class I b-1,3-glucanase in the endosperm of tobacco during germination. Plant Physiol 1995; 109: 751-759.
Sunderasan E, Samsidar H, Sharifah H, Ward MA, Yeang HY, Cardosa MJ. Latex B serum b-1,3-glucanase (Hev b 2) and a component of the microhelix (Hev b 4) are major latex allergens. J Nat Rubb Res 1995; 10: 82-99.
Alenius H, Kalkkinen N, Lukka M, Reúnala T, Turjanmaa K, Maakinen-Kiljunen S, Yip E, Palosuo T. Prohevein from the rubber tree (Hevea brasiliensis) is a major latex allergen. Clin Exp Allergy 1995; 25: 659-665.
Hřj PB, Fincher GB. Molecular evolution of plant b-glucan endohydrolases. Plan J 1995; 7: 367-379.
Kurup VP, Yeang HY, Sussman GL, Bansal NK, Beezhold DH, Kelly KJ, Hoffman DR, Williams B, Fink JN. Detection of immunoglobulin antibodies in the sera of patients using purified latex allergens. Clin Exp Allergy 2000; 30: 359-369.
Asero R, Mistrello G, Roncarolo D, Amato S, Falagiani P. Detection of novel latex allergen associated with clinically relevant allergy to plant-derived foods. J Allergy Clin Immunol 2005; 115: 1312-1314.
Koh D, Ng V, Leow Y-H, Goh CL. A study of natural rubber latex allergens in gloves used by health care workers in Singapure. British Journal of Dermatology 2005; 153: 954-959.
O’connor TM, Bourke JF, Jones M, Brennan N. Report of occupational asthma due to phytase and b-glucanase. Occup Enviro Med 2001; 58: 417-419.
Moreno HL, Avila E, Angulo Y, Portillo J, Moreno L, Reza G, Hernández V, Levario M. Frequency in allergy to proteins of latex in health care workers. Allergol et Immunopathol 2005; 33: 210-213.
Palomares O, Villalba M, Rodríguez R. The C-terminal segment of the 1,3-b- glucanase Ole e 9 from olive (Olea europaea) pollen is an independent domain with allergenic activity: expression in Pichia pastoris and characterization. Biochem J 2003; 369: 593-601.
Palomares O, Villalba M, Quiralte J, Polo F, Rodríguez R. 1,3-b-glucanase as candidates in latex-pollen-vegetable food cross-reactivity. Clin Exp Allergy 2005; 35: 345-351.
Akiyama T, Shibuya N, Hrmova M, Fincher GB. Purification and characterization of a (1-3)-b-D-glucan endohydrolase from rice (Oryza sativa) bran. Carbohydrate Research 1997; 297: 365-374.
Receveur V, Czjzek M, Barre A, Roussel A, Peumans WJ. Crystal structure at 1.45-Ĺ Resolution of Major Allergen Endo-b-1,3-glucanase of Banana as a Molecular basis for the Latex-Fruit Syndrome. Proteins: Structure, Function and Bioinformatics 2006; 63: 235-242.
Yagami T, Sato M, Nakamura A, Komiyama T, Kitagawa K, Akasawa A, Ikezawa Z. Plant defense-related enzymes as latex antigens. J Allergy Clin Immunol 1998; 101: 379-385.
Nieto GA, Mazón RA, Pamies ER, Caballero GL, Oliver JF, Colomer HN. Implicación clínica de la reactividad cruzada entre alergenos. Allergol et Immunopathol 2004; 32: 124-129.
Kurup VP, Sussman GL, Yeang HY, Elms N, Breiteneder H, Arif SAM, Kelly KJ, Bansal NK, Fink JN. Specific IgE response to purified and recombinant allergens in latex allergy. Clin Mol Allergy 2005; 3: 1-9.
Yagami T, Osuna H, Kouno M, Haishima Y, Nakamura A, Ikezawa Z. Significance of carbohydrate epitopes in a latex allergen with b-1,3-glucanase activity. Int Arch Allergy Immunol 2002; 129: 27-37.
Thomas WR. How good are carbohydrates as allergens? Clin Exp Allergy 2002; 32: 658-661.
Calabozo B, Barber D, Plo F. Studies on the carbohydrate moiety of Pla l 1 allergen. Identification of a major N-glycan and significance for immunoglobulin E-binding activity. Clin Exp Allergy 2002; 32: 1628-1634.
Aalaberse RC. Structural biology of allergens. J Allergy Clin Immunol 2000; 106: 228-238.
Aalaberse RC. Structural features of allergenic molecules. Chem Immunol Allergy 2006; 91: 134-146.
Varghese JN, Garrett TPJ, Colma PM, Chen L, Hřj PB, Fincher GB. Three- dimensional structure of two plant b-glucan endohydrolases with distinct substrate specificities. Proc Natl Acad Sci 1994; 91: 2785-2789.
Banner DW, Bloomer Ac, Petsko GA, Phillips DC, Pogson CI, Wilson IA, Corran PH, Furth AJ, Milman JD, Offord RE, Priddle JD, Waley SG. Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using aminoacid sequence data. Nature 1975; 255: 609-614.