2002, Número 3
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Alerg Asma Inmunol Pediatr 2002; 11 (3)
Características bioquímicas y moleculares de alergenos del látex de Hevea brasiliensis
Reyes LCAS, Rodríguez RA
Idioma: Español
Referencias bibliográficas: 65
Paginas: 92-100
Archivo PDF: 331.03 Kb.
RESUMEN
En los últimos años las reacciones de hipersensibilidad de tipo I, ocasionadas por algunas proteínas del látex de Hevea brasiliensis (hule), se han incrementado de forma importante hasta llegar a ser un problema de salud pública ocupacional en muchos países. Esto ha generado un interés especial por entender las bases moleculares e inmunológicas del reconocimiento de estos alergenos por las IgE’s de personas alérgicas a este material. Recientemente se han realizado una gran cantidad de estudios moleculares e inmunológicos sobre los alergenos del látex, lo que ha permitido que once proteínas del hule sean consideradas como las principales que participan en la sensibilización de las personas y se les ha asignado una nomenclatura oficial. Estos estudios sentarán las bases para el desarrollo de mejores métodos de diagnóstico y proveerán de nuevas herramientas para emplearse en procesos de inmunoterapia.
REFERENCIAS (EN ESTE ARTÍCULO)
Janeway AC, Travers P. Immunobiology, 2a ed., London, Curren Biology Ltd. 1996; p. 11: 3-11:9.
van Neerven RJ, Ebner C, Yssel H, Kapsenberg ML, Lamb RJ. T-cell responses to allergens: epitope-specificity and clinical relevance. Immunology Today 1996; 17: 526-532.
Nuter A. Contact urticaria to rubber. Br J Dermatol 1979; 101: 597-598.
Instituto Nacional de Estadística, Geografía e Informática. XII Censo General de Población y Vivienda. 2002.
http://www.anesth.com/lair/latex/contents.html
http://www.latexallergy.net/historymain.htm
Nel A, Gujuluva Ch. Latex antigens: identification and use in clinical and experimental studies including cross reactivity with food and pollen alergens. Ann Allergy Asthma & immunol 1998; 81: 388-398.
Breiteneder H, Scheiner O. Molecular and immunological characteristics of latex allergens. Int Arch Allergy Immunol 1998; 116: 83-92.
Ferreira MB, Carlos AG. Latex: a complex allergy. Allerg Immunol 1999; 31: 18-21.
Terwisscha SA, Hennin M, Dijkstra BW. The 1.8 Å resolution structure of hevamina, a plant chitinase/lysozyme and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18. J Mol Biol 1996; 262: 243-257.
Posch A, Wheeler CH, Chen Z, Flagge A, Dunn MJ, Papentuss F, Raulf-Hemsoth M, Baur X. Class I endochitinase containing a hevein domain the causative allergen in latex-associated avocado allergy. Clin Exp Allergy 1999; 29: 667-672.
Bufe A. The biological function of allergens: Relevant for the induction of allergic diseases? Int Arch Allergy Immunol 1998; 117: 215-219.
Mark SD, David R. Rubber Elongation Factor from Hevea brasiliensis. Identification, characterization, and role in rubber biosynthesis. J Biol Chem 1989; 264: 18608-18617.
Mark SD, William JH, Bell J, William K, David RL. Amino acid sequence of rubber elongation factor protein associated with rubber particles in Hevea latex. J Bio Chem 1989; 264: 18618-18626.
Goyvaerts E, Dennis M, Light D, Chau NH. Cloning and sequencing of the cDNA encoding the rubber elongation factor of Hevea brasiliensis. Plant Physiol 1991; 97: 317-321.
Chen Z, Van Kampen V, Raulf-Heimsoth M, Baur X. Allergenic and antigenic determinants of latex allergen Hev b 1: peptide mapping of epitopes recognized by human, murine and rabbit antibodies. Clin Exp Allergy 1996; 26: 406-415.
Czuppon AB, Chen Z, Rennert S, Engelke T, Meyer HE, Heber M, Baur X. The rubber elongation factor of rubber trees (Hevea brasiliensis) is the major allergen in latex. J Allergy Clin Immunol 1993; 92: 690-697.
Rhis AP, Chen Z, Schumacher S, Rozynek P, Cremer R, Lundberg M, Raulf-Heimsoth M, Petersen A, Baur X. Recombinant Hev b 1: large-scale production and immunological characterization. Clin Exp Allergy 2000; 30: 1285-1292.
Sunderasan E, Hamzah S, Hamid S, 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.
Midoro-Horiuti T, Brooks EG, Goldblum RM. Pathogenesis-related proteins of plants as allergens. Ann Allergy Asthma Immunol 2001; 87: 261-71.
Subroto T, van Koningsveld GA, Schreuder HA, Soedjanaatmadja UM, Beintema JJ. Chitinase and beta-1,3-glucanase in the lutoid-body fraction of Hevea latex. Phytochemistry 1996; 43: 29-37.
Meade JB, Weissman NA, Beezhold HD. Latex allergy: past and present. Int Immunopharmacology 2002; 2: 225-238.
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 allergen. Clin Exp Allergy 2000; 30: 359-369.
Yeang YH, Cheong FK, Sunderasan E, Hamzah S, Chew PN, Hamid S, Hamilton GR, Cardosa JM. The 14.6 kD rubber elongation factor (Hev b 1) and 24 kD (Hev b 3) rubber particle proteins are recognized by IgE from patients with spina bifida and latex allergy. J Allergy Clin Immunol 1996; 98: 628-39.
Alenius H, Palosuo T, Kelly K, Kurup V, Reunala T, Mäkinen-Kiljunen S, Turjanmaa K, Fink J. IgE reactivity to 14-kD and 27-kD natural rubber proteins in latex-allergic children with spina bifida and other congenital anomalies. Int Arch Allergy Immunol 1993; 102: 61-66.
Wagner B, Krebitz M, Buck D, Niggemann B, Yang HY, Han KH, Scheiner O, Breinteneder H. Cloning, expression, and characterization of recombinant Hev b 3, a Hevea brasiliensis. J Allergy Clin Immunol 1999; 104: 1084-1092.
Bohle B, Wagner B, Vollmann D, Buck D, Niggemann B, Szépfalusi Z, Scheiner O, Breiteneder H, Ebner C. Characterization of T Cell Responses to Hev b 3, an allergen associated with latex allergy in spina bifida patients. J Immunol 2000; 164: 4393-4398.
Banerjee B, Kanitpong K, Fink JN, Zussman M, Sussman GL, Kelly KJ, Kurup VP. Unique and shared IgE epitopes of Hev b 1 and Hev b 3 in latex allergy. Mol Immunol 2000; 37: 789-798.
Slater JE, Vedvick T, Arthur-Smith A, Trybul DE, Kekwick RGO. Identification, Cloning, and sequence of a major allergen (Hev b 5) from natural rubber latex (Hevea brasiliensis). J Biol Chem 1996; 271: 25394-25399.
Akasawa A, Hsieh LS, Martín BM, Liu T, Lin Y. A Novel Acidic Allergen, Hev b 5, in latex. Purification, cloning and characterization. J Biol Chem 1996; 271: 25389-25393.
Beeezhold DH, Hickey VL, Slater JE, Sussman GL. Human IgE-binding epitopes of the latex allergen Hev b 5. J Allergy Clin Immunol 1999; 103: 1166-1172.
Beezhold DH, Hickey VL, Sussman GL. Mutational analysis of the IgE epitopes in the latex allergen Hev b 5. J Allergy Clin Immunol 2001; 107: 1069-1076.
Lee HI, Broekcaert WF, Raikhel NV. Co-and post-traslational processing of the hevein preprotein of latex of the rubber tree (Hevea brasiliensis). J Biol Chem 1991; 266: 15944-15948.
Garcia-Hernandez E, Zubillaga RA, Rojo-Dominguez A, Rodriguez-Romero A, Hernandez-Arana A. New insights into the molecular basis of lectincarbohydrate interactions: a calorimetric and structural study of the association of hevein to oligomers of N-acetylglucosamine. Proteins 1997; 29: 467-77.
Parijs JV, Broekaert WF, Goldstein IJ, Peumans WJ. Hevein: an antifungal protein from rubber-tree (Hevea brasiliensis) latex. Planta 1991; 183: 258-264.
Gidrol X, Chrestin H, Tan HL, Kush A. Hevein, a lectin-like protein from Hevea brasiliensis (Rubber Tree) is involved in the coagulation of latex. J Biol Chem 1994; 269: 9278-9283.
Alenius H, Kalkkinen N, Reunala T, Turjanmaa K, Palosuo T. The Main IgE Binding epitope of a major latex allergen, prohevein, is present in its N-terminal 43-amino acid fragment, hevein. J Immunol 1996; 156: 1618-1625.
Chen Z, Posch A, Lohaus C, Raulf-Heimsoth M, Meyer HE, Baur X. Isolation and identification of hevein as a major IgE-binding polypeptide in Hevea latex. J Allergy Clin Immunol 1997; 99: 402-409.
Ylitalo L, Alenius H, Turjanmaa K, Palosuo T, Reúnala T. Environmental and occupational disorders. J Allergy Clin Immunol 1998; 102: 659-664.
Banerjee B, Wang X, Kelly KJ, Fink JN, Sussman GL, Kurup VP. IgE from latex-allergic patients binds to cloned and expressed B cell epitopes of prohevein. J Immunol 1997; 159: 5724-5732.
Rozynek P, Posch A, Baur X. Cloning, expression and characterization of the major latex allergen prohevein. Clin Exp Allergy 1998; 28: 1418-1426.
Collinge DB, Kragh KM, Mikkelsen JD, Nielsen KK, Rasmussen U, Vad K. Plant chitinases. Plant J 1993; 3: 31-40.
Blanco C, Diaz-Perales A, Collado C, Sánchez-Monge R, Aragoncillo C, Castillo R, Ortega N, Alvarez M, Carrillo T, Salcedo G. Class I chitinases as potential panallergens involved in the latex-fruit syndrome. J Allergy Clin Immunol 1999; 103: 507-513.
Lavaud F, Prevost A, Cossart C, Guerin L, Bernard J, Kochman S. Allergy to latex, avocado pear, and banana: Evidece for 30 kD antigen in immunoblotting. J Allergy Clin Immunol 1995; 95: 557-564.
Ahlroth M, Alenius H, Turjanmaa K, Mäkinen-Kiljunen S, Reúnala T, Palosuo T. Cross-reacting allergens in natural rubber latex avocado. J Allergy Clin Immunol 1995; 96: 167-173.
Mikkola JH, Alenius H, Kalkkinen N, Turjanmma K, Palosuo T, Reúnala T. Hevein-like protein domains as a possible cause for allergen cross-reactivity between latex and banana. J Allergy Clin Immunol 1998; 102: 1005-1012.
Diaz-Perales A, Collada C, Blanco C, Sanchez-Monge R, Carrillo T, Aragoncillo C, Salcedo G. Cross-reactions in the latex-fruit syndrome: A relevant role of chitinases but not of complex asparagine-liked glycans. J Allergy Clin Immunol 1999; 104: 681-687.
Rodríguez-Romero A, Ravichandran KG, Soriano-García M. Crystal structure of hevein at 2.8 Å resolution. FEBS 1991; 291: 307-309.
Andersen NH, Cao B, Rodríguez-Romero A, Arreguín B. Hevein: NMR Assignment and assessment of solution-state folding for the agglutinin-toxin motif. Biochemistry 1993; 32: 1407-1422.
Asensio JL, Cañada FJ, Bruix M, Rodríguez-Romero A, Jiménez-Barbero J. The interaction of hevein with N-acetylglucosamine-containing oligosaccharides. Solution structure of hevein complex to chitobiose. Eur J Biochem 1995; 230: 621-633.
Asensio JL, Cañada FJ, Bruix M, Rodríguez-Romero A, Jiménez-Barbero J. NMR investigations of protein-carbohydrate interactions: refined three dimensional structure of the complex between hevein and methyl betachitobioside. Glycobiology 1998; 8: 569-577.
Beezhold DH, Sussman GL, Kostayl DA, Chang N. Latex allergy can induce clinical reactions to specific foods. Clin Exp Allergy 1996; 26: 416-422.
Kostyal DA, Hickel VL, Noti JD, Sussman GL, Beezhod DH. Cloning and characterization of a latex allergen (Hev b 7): Homology to patatin, a plant PLA2. Clin Exp Immunol 1998; 112: 355-262.
Sowka S, Wagner S, Krebitz M, Arij-Mad-Arif S, Yusof F, Kinaciyan T, Brehler R, Scheiner O, Breiteneder H. cDNA cloning of the 43-kDa latex allergen Hev b 7 with sequences similarity to patatins and its expression in the yeast Pichia pastoris. Eur J Biochem 1998; 255: 213-219.
Sowka S, Hafner C, Radauer C, Focke M, Brehler R, Astwood JD, Arij-Mad-Arif S, Kanani A, Sussman GL, Scheiner O, Beezhold DH, Breiteneder H. Molecular and immunologic characterization of new isoforms of the Hevea brasiliensis latex allergen Hev b 7: Evidence of no cross-reactivity between Hev b 7 isoforms and patato patatin and proteins from avocado and banana. J Allergy Clin Immunol 1999; 104: 1302-1310.
Wagner B, Buck D, Hafner C, Sowka S, Niggemann B, Scheiner O, Breiteneder H. Hev b 7 Hevea brasiliensis protein associated with latex allergy in children with spina bifida. J Allergy Clin Immunol 2001; 108: 621-627.
Vallier P, Balland S, Herf R, Valenta R, Deviller P. Identification of profilin as an IgE-binding component in latex from Hevea brasiliensis. Clinical implications. Clin Exp Allergy 1995; 25: 332-339.
Rihs HP, Chen Z, Rozynek P, Baur X, Lundberg M, Cremer R. PCR-based cloning, isolation, and IgE-binding properties of recombinant latex profilin. Allergy 2000; 55: 712-717.
Wagner S, Breinteneder H, Simon-Nobbe B, Susani M, Krebitz M, Niggemann B, Brehler R, Scheiner O, Hoffmann-Sommergruber K. Hev b 9, an enolase and a new cross-reactive allergen from Hevea latex and molds. Eur J Biochem 2000; 267: 7006-7014.
Posch A, Chen Z, Wheeler C, Dunn MJ, Raulf-Heimsoth M, Baur X. Characterization and identification of latex allergens by two-dimensional electroforesis and protein microsequencing. J Allergy Clin Immunol 1997; 99: 385-395.
Rihs HP, Chen Z, Rozynek P, Cremer R. Allergenicity of rHev b 10 (manganese-superoxide dismutase). Allergy 2001; 56: 85-86.
O’Riordain GO, Radauer C, Wagner S, Blanco C, Hoffmann-Sommergruber K, Scheiner O, Ebner C, Breiteneder H. Hev b 11, a class I chitinase from Hevea brasiliensis and its cross-reactivity with Hev b 6.02, hevein. J Allergy Clin Immunol 2001; 107: S57.
Rozeboom HJ, Budiani A, Beintema JJ, Dijkstra BW. Crystallization of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex. J Mol Biol 1990; 212: 441-443.
Jekel PA, Hartmann JBH, Beintema JJ. The primary structure of hevamine, an enzyme with lysozyme/chitinase activity from Hevea brasiliensis latex. Eur J Biochem 1991; 200: 123-130.
Yagami T, Sato M, Nakamura A, Shono M. One of the rubber latex allergens is a lysozyme. J Allergy Clin Immunol 1995; 96: 677-686.