Pedraza EMM, Dra. Adela Rodríguez RA

Idioma: Español
Referencias bibliográficas: 33
Paginas: 5-10
Archivo PDF: 83.88 Kb.

RESUMEN

Las alergias mediadas por anticuerpos IgE son consideradas un grave problema de salud en los países industrializados, debido a la capacidad de algunas proteínas normalmente inocuas (alergenos) para inducir reacciones alérgicas en pacientes sensibilizados. La comunidad científica realiza diversos estudios inmunológicos y moleculares para determinar los fundamentos del potencial alergénico y de la reactividad cruzada de los alergenos, los cuales podrían estar relacionados con las características intrínsecas de estas moléculas. Como objetivos principales se tienen el desarrollar inmunoterapias apropiadas para evitar estas enfermedades, predecir dicho potencial en productos y alimentos nuevos, y establecer las herramientas de diagnóstico adecuadas. En este trabajo se describen algunos estudios realizados primordialmente a las regiones inmunodominantes que interaccionan con los anticuerpos IgE.

REFERENCIAS (EN ESTE ARTÍCULO)

1. Ring J, Kramer U, Schafer T et al. Why are allergies increasing? Curr Opin Immunol 2001; 13: 701-708.

2. Aalberse RC, Stapel SO. Structure of food allergens in relation to allergenicity. Pediatr Allergy Immunol 2001; 12: 10-14.

3. Rob C, Aalberse RC. Structural biology of allergens. J Allergy Clin Immunol 2000; 106: 228-238.

4. Roitt I, Brostoff J, Male D. Immunology. 5th edition. UK Mosby International Ltd, 1998: 107-119.

5. Holgate S, Church M, Lichtenstein L. Alergia. 2a Edición España Editorial Harcout, 2001: 3-16.

6. Sela M, Pecht I. The nature of the antigen. Adv Protein Chem 1996; 49: 289-328.

7. Valenta R. The future of antigen-specific immunotherapy of allergy. Nat Rev Immunol 2002; 2: 446-453.

8. Valenta R, Hayek B, Seiberler S et al. Calcium-binding allergens: from plants to man. Int Arch Allergy Immunol 1998; 117: 160-6.

9. Flicker S, Vrtala S, Steinberger et al. A human monoclonal IgE antibody defines a highly allergenic fragment of the major timothy grass pollen allergen, Phl p 5: Molecular, immunological and structural characterization of the epitope-containing domain. J Immunol 2000; 165: 3849-3859.

10. Pómes A. Intrinsic properties of allergens and environmental exposure as determinants of allergenicity. Allergy 2002; 57: 673-679.

11. Huby R, Dearman R, Kimber I. Why are some protein allergens? Toxicol Sci 2000; 55: 235-246.

12. Fötisch F, Vieths S. N-and O-linked oligosaccharides of allergenic glycoproteins. Glycoconj J 2001; 18: 373-390.

13. Van Ree R. Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases. Int Arch Allergy Immunol 2002; 129: 189-97.

14. Lombardero M, Quirce S, Duffort O et al. Monoclonal antibodies agains Olea europea major allergen: Allergenic activity of affinity-purifies allergen and depleted extract and development of a radioimmunoassay for the quantification of the allergen. J Allergy Clin Immunol 1992; 89: 884-94.

15. González EM, Villalba M, Lombardero M et al. Influence of the 3D-conformation, glycan component and micro-heterogeneity on the epitope structures of Ole e 1 the major olive allergen. Use of the recombinant isoforms and specific monoclonal antibodies as immunological tools. Mol Immunol 2002; 39: 93-101.

16. Taylor SB, Lenher SL. Principles and characteristics of food allergens. Crit Rev Food Sci Nutr 1996; 36: S91-S118.

17. Brederhost R, Kerstin D. What establishes a protein as an allergen? J Chromatogr B Biomed Sci Appl 2001; 756: 33-40.

18. Takai T, Yuuki T, Okumura Y et al. Determination on the N- and C- terminal sequences required to bind human IgE of the major house dust mite allergen Der f 2 and epitope mapping for monoclonal antibodies. Mol Immunol 1997; 34: 255-261.

19. Buchanan BB, Adamidi C, Lozano MR et al. Thioredexin-linked mitigation of allergic response to wheat. Proc Natl Acad Sci 1997; 94: 5372-77.

20. Bufe A. The biological function of allergens relevant for the induction of allergic diseases. Int Arch Allergy Immunol 1998; 117: 215-219.

21. Tinghino R, Twardosz A, Barletta B et al. Molecular, structural, and immunologic relationships between different families of recombinant calcium-binding pollen allergens. J Allergy Clin Immunol 2002; 109: 314-20.

22. Ledesma A, González E, Pascual CY et al. Are Ca2+-binding motifs involved in the immunoglobin E-binding of allergens? Olive pollen allergens as model of study. Clin Exp Allergy 2002; 32: 1476-83.

23. Valenta R. Recombinant allergen molecules: tools to study effector cell activation Immunol Rev 2001; 179: 119-127.

24. Mäntyjärvi R, Rautiainen J, Virtanen T. Lipocalins as allergens. Biochim Biophys Acta 2000; 1482: 308-17.

25. Virtanen T. Lipocalis allergens. Allergy 2001; 56: 48-51.

26. Wal JM. Structure and function of milk allergens. Allergy 2001; 56: 35-38.

27. Breiteneder H, Ebner C. Molecular and biochemical classification of plant-derived food allergens. J Allergy Clin Immunol 2000; 106: 27-36.

28. Rouvinen J, Rautiainen J, Virtanen T et al. Probing the molecular basis of allergy. Three-dimensional structure of the bovine lipocalin allergen Bos d 2. J Biol Chem 1999; 274: 2337-2343.

29. Ichikawa S, Hatakana H, Yuuki T et al. (1998) Solution structure of Der f 2, the major mite allergen for atopic diseases. J Biol Chem 1998; 273: 356-60.

30. Verdino P, Westritschnig K, Valenta R et al. The cross-reactive calcium-binding pollen allergen, Phl p 7, reveals a novel dimer assembly. Embo J 2002; 21: 5007-16.

31. mirza o, Henriksen A, Ipsen H et al. Dominant epitopes and allergic cross-reactivity: complex formation between a Fab fragment of a monoclonal murine IgG antibody and the major allergen from birch pollen Bet v 1. J Immunol 2000; 165: 331–338.

32. Li Y, Li H, Yang F et al. X-ray snapshots of the maturation of an antibody response to a protein antigen. Nat Struct Biol 2003; 10: 482-8.

33. Reyes-Lopez C, Hernandez-Santoyo A, Pedraza-Escalona M et al. Insights into a conformational epitope of Hev b 6.02 (hevein). Biochem Biophys Res Commun 2004; 314: 123-130.