Molecular characterization of Api g 2, a novel allergenic member of the lipid-transfer protein 1 family from celery stalks

Molecular Nutrition and Food Research

Volumn 55, Issue 4, 2011, Pages 568-577

  Gadermaier, Gabriele ^a   Egger, Matthias ^a   Girbl, Tamara ^a   Erler, Anja ^a   Harrer, Andrea ^a   Vejvar, Eva ^a   Liso, Marina ^b   Richter, Klaus ^a   Zuidmeer, Laurian ^c   Mari, Adriano ^b   Ferreira, Fatima ^a  

^a UNIVERSITY OF SALZBURG   (Austria)

^b LABORATORIO DI PATOLOGIA VASCOLARE   (Italy)

^c ACADEMIC MEDICAL CENTER   (Netherlands)

Author keywords

Api g 2; Celery allergy; Gastrointestinal digestion; Non specific lipid transfer protein; Thermal stability

Indexed keywords

API G 2 ALLERGEN, CELERY; CARRIER PROTEIN; IMMUNOGLOBULIN E; ISOPROTEIN; LIPID TRANSFER PROTEINS, PLANT; PLANT ANTIGEN; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ANIMAL; ANTIGEN ANTIBODY REACTION; ARTICLE; CELERY; CELL LINE; CHEMISTRY; CROSS REACTION; DIGESTION; FOOD ALLERGY; GENETICS; HUMAN; IMMUNOLOGY; METABOLISM; MOLECULAR GENETICS; PLANT STEM; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; RAT; SEQUENCE ALIGNMENT;

AMINO ACID SEQUENCE; ANIMALS; ANTIGEN-ANTIBODY REACTIONS; ANTIGENS, PLANT; APIUM GRAVEOLENS; CARRIER PROTEINS; CELL LINE; CROSS REACTIONS; DIGESTION; FOOD HYPERSENSITIVITY; HUMANS; IMMUNOGLOBULIN E; MOLECULAR SEQUENCE DATA; PLANT PROTEINS; PLANT STEMS; PROTEIN ISOFORMS; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; RATS; RECOMBINANT PROTEINS; SEQUENCE ALIGNMENT;

APIUM GRAVEOLENS VAR. DULCE; ARTEMISIA VULGARIS; ESCHERICHIA COLI; PRUNUS PERSICA;

EID: 79953309467     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.201000443     Document Type: Article

References (38)

1. Andre, F., Andre, C., Colin, L., Cacaraci, F., Cavagna, S., Role of new allergens and of allergens consumption in the increased incidence of food sensitizations in France. Toxicology 1994, 93, 77-83.
2. Asero, R., Relevance of pollen-specific IgE levels to the development of Apiaceae hypersensitivity in patients with birch pollen allergy. Allergy 1997, 52, 560-564.
3. Pauli, G., Bessot, J. C., Braun, P. A., Dietemann-Molard, A. et al., Celery allergy: clinical and biological study of 20 cases. Ann. Allergy 1988, 60, 243-246.
4. Wuthrich, B., Stager, J., Johansson, S. G., Celery allergy associated with birch and mugwort pollinosis. Allergy 1990, 45, 566-571.
5. Ballmer-Weber, B. K., Vieths, S., Luttkopf, D., Heuschmann, P., Wuthrich, B., Celery allergy confirmed by double-blind, placebo-controlled food challenge: a clinical study in 32 subjects with a history of adverse reactions to celery root. J. Allergy Clin. Immunol. 2000, 106, 373-378.
6. Vieths, S., Luttkopf, D., Reindl, J., Anliker, M. D. et al., Allergens in celery and zucchini. Allergy 2002, 57, 100-105.
7. Breiteneder, H., Hoffmann-Sommergruber, K., O'Riordain, G., Susani, M. et al., Molecular characterization of Api g 1, the major allergen of celery (Apium graveolens), and its immunological and structural relationships to a group of 17-kDa tree pollen allergens. Eur. J. Biochem. 1995, 233, 484-489.
8. Scheurer, S., Wangorsch, A., Haustein, D., Vieths, S., Cloning of the minor allergen Api g 4 profilin from celery (Apium graveolens) and its cross-reactivity with birch pollen profilin Bet v 2. Clin. Exp. Allergy 2000, 30, 962-971.
9. Bublin, M., Radauer, C., Wilson, I. B., Kraft, D. et al., 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. 2003, 17, 1697-1699.
10. Ganglberger, E., Radauer, C., Grimm, R., Hoffmann-Sommergruber, K. et al., N-terminal sequences of high molecular weight allergens from celery tuber. Clin. Exp. Allergy 2000, 30, 566-570.
11. Luttkopf, D., Ballmer-Weber, B. K., Wuthrich, B., Vieths, S., Celery allergens in patients with positive double-blind placebo-controlled food challenge. J. Allergy Clin. Immunol. 2000, 106, 390-399.
12. Bauermeister, K., Ballmer-Weber, B. K., Bublin, M., Fritsche, P. et al., Assessment of component-resolved in vitro diagnosis of celeriac allergy. J. Allergy Clin. Immunol. 2009, 124, 1273-1281, e1272.
13. Egger, M., Mutschlechner, S., Wopfner, N., Gadermaier, G. et al., Pollen-food syndromes associated with weed pollinosis: an update from the molecular point of view. Allergy 2006, 61, 461-476.
14. Hoffmann-Sommergruber, K., Demoly, P., Crameri, R., Breiteneder, H. et al., IgE reactivity to Api g 1, a major celery allergen, in a Central European population is based on primary sensitization by Bet v 1. J. Allergy Clin. Immunol. 1999, 104, 478-484.
15. Bohle, B., Zwolfer, B., Heratizadeh, A., Jahn-Schmid, B. et al., Cooking birch pollen-related food: divergent consequences for IgE- and T cell-mediated reactivity in vitro and in vivo. J. Allergy Clin. Immunol. 2006, 118, 242-249.
16. Jankiewicz, A., Aulepp, H., Baltes, W., Bogl, K. W. et al., Allergic sensitization to native and heated celery root in pollen-sensitive patients investigated by skin test and IgE binding. Int. Arch. Allergy Immunol. 1996, 111, 268-278.
17. Harwanegg, C., Hiller, R., Protein microarrays for the diagnosis of allergic diseases: state-of-the-art and future development. Clin. Chem. Lab. Med. 2005, 43, 1321-1326.
18. Sheffield, P., Garrard, S., Derewenda, Z., Overcoming expression and purification problems of RhoGDI using a family of "parallel" expression vectors. Protein Expr. Purif. 1999, 15, 34-39.
19. Dougan, D. A., Truscott, K. N., Zeth, K., The bacterial N-end rule pathway: expect the unexpected. Mol. Microbiol. 2010, 3, 545-558.
20. Gadermaier, G., Harrer, A., Girbl, T., Palazzo, P. et al., Isoform identification and characterization of Art v 3, the lipid-transfer protein of mugwort pollen. Mol. Immunol. 2009, 46, 1919-1924.
21. Ma, Y., Griesmeier, U., Susani, M., Radauer, C. et al., Comparison of natural and recombinant forms of the major fish allergen parvalbumin from cod and carp. Mol. Nutr. Food Res. 2008, 52, S196-S207.
22. Pasquato, N., Berni, R., Folli, C., Folloni, S. et al., Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens. J. Mol. Biol. 2006, 356, 684-694.
23. Moreno, F. J., Mellon, F. A., Wickham, M. S., Bottrill, A. R., Mills, E. N., Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion. FEBS J. 2005, 272, 341-352.
24. Zuidmeer, L., van Leeuwen, W. A., Budde, I. K., Cornelissen, J. et al., Lipid transfer proteins from fruit: cloning, expression and quantification. Int. Arch. Allergy Immunol. 2005, 137, 273-281.
25. Vogel, L., Luttkopf, D., Hatahet, L., Haustein, D., Vieths, S., Development of a functional in vitro assay as a novel tool for the standardization of allergen extracts in the human system. Allergy 2005, 60, 1021-1028.
26. Ballmer-Weber, B. K., Hoffmann, A., Wuthrich, B., Luttkopf, D. et al., Influence of food processing on the allergenicity of celery: DBPCFC with celery spice and cooked celery in patients with celery allergy. Allergy 2002, 57, 228-235.
27. Bublin, M., Lauer, I., Oberhuber, C., Alessandri, S. et al., Production and characterization of an allergen panel for component-resolved diagnosis of celery allergy. Mol. Nutr. Food Res. 2008, 52, S241-S250.
28. Pokoj, S., Lauer, I., Fotisch, K., Himly, M. et al., Pichia pastoris is superior to E. coli for the production of recombinant allergenic non-specific lipid-transfer proteins. Protein Expr. Purif. 2010, 69, 68-75.
29. Asero, R., Antonicelli, L., Arena, A., Bommarito, L. et al., EpidemAAITO: features of food allergy in Italian adults attending allergy clinics: a multi-centre study. Clin. Exp. Allergy 2009, 39, 547-555.
30. Egger, M., Hauser, M., Mari, A., Ferreira, F., Gadermaier, G., The role of lipid transfer proteins in allergic diseases. Curr. Allergy Asthma Rep. 2010, 10, 326-335.
31. Garcia-Casado, G., Pacios, L. F., Diaz-Perales, A., Sanchez-Monge, R. et al., Identification of IgE-binding epitopes of the major peach allergen Pru p 3. J. Allergy Clin. Immunol. 2003, 112, 599-605.
32. Borges, J. P., Barre, A., Culerrier, R., Granier, C. et al., Lipid transfer proteins from Rosaceae fruits share consensus epitopes responsible for their IgE-binding cross-reactivity. Biochem. Biophys. Res. Commun. 2008, 365, 685-690.
33. Zuidmeer, L., van Ree, R., Lipid transfer protein allergy: primary food allergy or pollen/food syndrome in some cases. Curr. Opin. Allergy Clin. Immunol. 2007, 7, 269-273.
34. Barber, D., de la Torre, F., Lombardero, M., Antepara, I. et al., Component-resolved diagnosis of pollen allergy based on skin testing with profilin, polcalcin and lipid transfer protein pan-allergens. Clin. Exp. Allergy 2009, 39, 1764-1773.
35. Cavatorta, V., Sforza, S., Aquino, G., Galaverna, G. et al., In vitro gastrointestinal digestion of the major peach allergen Pru p 3, a lipid transfer protein: molecular characterization of the products and assessment of their IgE binding abilities. Mol. Nutr. Food Res. 2010, 54, 1452-1457.
36. Wijesinha-Bettoni, R., Alexeev, Y., Johnson, P., Marsh, J. et al., The structural characteristics of nonspecific lipid transfer proteins explain their resistance to gastroduodenal proteolysis. Biochemistry 2010, 49, 2130-2139.
37. Gaier, S., Marsh, J., Oberhuber, C., Rigby, N. M. et al., Purification and structural stability of the peach allergens Pru p 1 and Pru p 3. Mol. Nutr. Food Res. 2008, 52, S220-S229.
38. Mills, E. N., Mackie, A. R., The impact of processing on allergenicity of food. Curr. Opin. Allergy Clin. Immunol. 2008, 8, 249-253.