Table of Contents Author Guidelines Submit a Manuscript
The Scientific World Journal
Volume 2014, Article ID 543195, 19 pages
http://dx.doi.org/10.1155/2014/543195
Review Article

Current Overview of Allergens of Plant Pathogenesis Related Protein Families

Department of Biophysics, All India Institute of Medical Sciences, Ansari Nagar, New Delhi 110029, India

Received 22 October 2013; Accepted 17 December 2013; Published 16 February 2014

Academic Editors: B. Cardaba and A. J. Chauhan

Copyright © 2014 Mau Sinha et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. S. G. Johansson, “IgE in allergic diseases,” Proceedings of the Royal Society of Medicine, vol. 62, no. 9, pp. 975–976, 1969. View at Google Scholar · View at Scopus
  2. D. G. Marsh, L. M. Lichtenstein, and P. S. Norman, “Induction of IgE-mediated immediate hypersensitivity to group I rye grass pollen allergen and allergoids in non-allergic man,” Immunology, vol. 22, no. 6, pp. 1013–1028, 1972. View at Google Scholar · View at Scopus
  3. E. A. Taketomi, M. C. Sopelete, P. F. D. S. Moreira, and F. D. A. M. Vieira, “Pollen allergic disease: pollens and its major allergens,” Brazilian Journal of Otorhinolaryngology, vol. 72, no. 4, pp. 562–567, 2006. View at Google Scholar · View at Scopus
  4. P. Kennedy, “Acute reaction to apple-eating,” British Medical Journal, vol. 2, no. 6150, pp. 1501–1502, 1978. View at Google Scholar · View at Scopus
  5. B. A. Burrall, “Plant-related allergic contact dermatitis,” Clinical Reviews in Allergy, vol. 7, no. 4, pp. 417–439, 1989. View at Google Scholar · View at Scopus
  6. P. D. Buisseret, “Seasonal allergic symptoms due to fungal spores,” British Medical Journal, vol. 2, no. 6034, pp. 507–508, 1976. View at Google Scholar · View at Scopus
  7. H. L. Spiegelberg and R. A. Simon, “Increase of lymphocytes with Fc receptors for IgE in patients with allergic rhinitis during the grass pollen season,” Journal of Clinical Investigation, vol. 68, no. 4, pp. 845–852, 1981. View at Google Scholar · View at Scopus
  8. M. Mayoral, H. Calderón, R. Cano, and M. Lombardero, “Allergic rhinoconjunctivitis caused by Cannabis sativa pollen,” Journal of Investigational Allergology and Clinical Immunology, vol. 18, no. 1, pp. 73–74, 2008. View at Google Scholar · View at Scopus
  9. J. A. Martin, J. A. Compaired, B. de la Hoz et al., “Bronchial asthma induced by chick pea and lentil,” Allergy, vol. 47, no. 2, part 2, pp. 185–187, 1992. View at Google Scholar · View at Scopus
  10. R. Valdivieso, J. Subiza, S. Varela-Losada et al., “Bronchial asthma, rhinoconjunctivitis, and contact dermatitis caused by onion,” Journal of Allergy and Clinical Immunology, vol. 94, no. 5, pp. 928–930, 1994. View at Publisher · View at Google Scholar · View at Scopus
  11. R. K. Chandra, “Food hypersensitivity and allergic diseases,” European Journal of Clinical Nutrition, vol. 56, no. 3, pp. S54–S56, 2002. View at Google Scholar · View at Scopus
  12. P. Rougé, R. Culerrier, F. Thibau, A. Didier, and A. Barre, “A case of severe anaphylaxis to kidney bean: Phaseolin (vicilin) and PHA (lectin) identified as putative allergens,” Allergy, vol. 66, no. 2, pp. 301–302, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. M. T. Gette and J. E. Marks Jr., “Tulip fingers,” Archives of Dermatology, vol. 126, no. 2, pp. 203–205, 1990. View at Publisher · View at Google Scholar · View at Scopus
  14. S. Goncalo, J. D. Freitas, and I. Sousa, “Contact dermatitis and respiratory symptoms from Narcissus pseudonarcissus,” Contact Dermatitis, vol. 16, no. 2, pp. 115–116, 1987. View at Google Scholar · View at Scopus
  15. E. N. C. Mills, J. Jenkins, N. Marigheto, P. S. Belton, A. P. Gunning, and V. J. Morris, “Allergens of the cupin superfamily,” Biochemical Society Transactions, vol. 30, part 6, pp. 925–929, 2002. View at Publisher · View at Google Scholar · View at Scopus
  16. S. Vrtala, S. Fischer, M. Grote et al., “Molecular, immunological, and structural characterization of Phl p 6, a major allergen and P-particle-associated protein from timothy grass (Phleum pratense) pollen,” Journal of Immunology, vol. 163, no. 10, pp. 5489–5496, 1999. View at Google Scholar · View at Scopus
  17. O. A. Duffort, F. Polo, M. Lombardero et al., “Immunoassay to quantify the major peach allergen Pru p 3 in foodstuffs. Differential allergen release and stability under physiological conditions,” Journal of Agricultural and Food Chemistry, vol. 50, no. 26, pp. 7738–7741, 2002. View at Publisher · View at Google Scholar · View at Scopus
  18. R. D. J. Huby, R. J. Dearman, and I. Kimber, “Why are some proteins allergens?” Toxicological Sciences, vol. 55, no. 2, pp. 235–246, 2000. View at Google Scholar · View at Scopus
  19. S. B. Lehrer, W. E. Horner, and G. Reese, “Why are some proteins allergenic? Implications for biotechnology,” Critical Reviews in Food Science and Nutrition, vol. 36, no. 6, pp. 553–564, 1996. View at Google Scholar · View at Scopus
  20. L. C. van Loon, “Pathogenesis-related proteins,” Plant Molecular Biology, vol. 4, no. 2-3, pp. 111–116, 1985. View at Publisher · View at Google Scholar · View at Scopus
  21. J. Rigden and R. Coutts, “Pathogenesis-related proteins in plants,” Trends in Genetics, vol. 4, no. 4, pp. 87–89, 1988. View at Publisher · View at Google Scholar
  22. C. J. Lamb, M. A. Lawton, M. Dron, and R. A. Dixon, “Signals and transduction mechanisms for activation of plant defenses against microbial attack,” Cell, vol. 56, no. 2, pp. 215–224, 1989. View at Google Scholar · View at Scopus
  23. T. P. Delaney, S. Uknes, B. Vernooij et al., “A central role of salicylic acid in plant disease resistance,” Science, vol. 266, no. 5188, pp. 1247–1250, 1994. View at Google Scholar · View at Scopus
  24. X. Y. Xu Yi, L. Chang Pi Fang, L. D. Liu Dong et al., “Plant defense genes are synergistically induced by ethylene and methyl jasmonate,” Plant Cell, vol. 6, no. 8, pp. 1077–1085, 1994. View at Publisher · View at Google Scholar · View at Scopus
  25. H. J. Linthorst, L. C. van Loon, C. M. van Rossum et al., “Analysis of acidic and basic chitinases from tobacco and petunia and their constitutive expression in transgenic tobacco,” Molecular Plant-Microbe Interactions, vol. 3, no. 4, pp. 252–258, 1990. View at Google Scholar · View at Scopus
  26. T. Lotan, N. Ori, and R. Fluhr, “Pathogenesis-related proteins are developmentally regulated in tobacco flowers,” The Plant Cell, vol. 1, no. 9, pp. 881–887, 1989. View at Publisher · View at Google Scholar · View at Scopus
  27. L. C. van Loon, W. S. Pierpoint, T. Boller, and V. Conejero, “Recommendations for naming plant pathogenesis-related proteins,” Plant Molecular Biology Reporter, vol. 12, no. 3, pp. 245–264, 1994. View at Publisher · View at Google Scholar · View at Scopus
  28. L. C. van Loon and A. van Kammen, “Polyacrylamide disc electrophoresis of the soluble leaf proteins from Nicotiana tabacum var. “Samsun” and “Samsun NN”. II: changes in protein constitution after infection with tobacco mosaic virus,” Virology, vol. 40, no. 2, pp. 199–211, 1970. View at Google Scholar · View at Scopus
  29. L. C. van Loon and E. A. van Strien, “The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins,” Physiological and Molecular Plant Pathology, vol. 55, no. 2, pp. 85–97, 1999. View at Publisher · View at Google Scholar · View at Scopus
  30. A. S. Buchel and H. J. M. Linthorst, “PR-1: a group of plant proteins induced upon pathogen infection,” in Pathogenesis-Related Proteins in Plants, S. K. Datta and S. Muthukrishnan, Eds., pp. 21–47, CRC Press LLC, Boca Raton, Fla, USA, 1999. View at Google Scholar
  31. M. Ohshima, H. Itoh, M. Matsuoka, T. Murakami, and Y. Ohashi, “Analysis of stress-induced or salicylic acid-induced expression of the pathogenesis-related 1a protein gene in transgenic tobacco,” Plant Cell, vol. 2, no. 2, pp. 95–106, 1990. View at Google Scholar · View at Scopus
  32. N. Yalpani, P. Silverman, T. M. A. Wilson, D. A. Kleier, and I. Raskin, “Salicylic acid is a systemic signal and an inducer of pathogenesis-related proteins in virus-infected tobacco,” Plant Cell, vol. 3, no. 8, pp. 809–818, 1991. View at Google Scholar · View at Scopus
  33. S. Chamnongpol, H. Willekens, W. Moeder et al., “Defense activation and enhanced pathogen tolerance induced by H2O2 in transgenic tobacco,” Proceedings of the National Academy of Sciences of the United States of America, vol. 95, no. 10, pp. 5818–5823, 1998. View at Publisher · View at Google Scholar · View at Scopus
  34. S. Kitajima and F. Sato, “Plant pathogenesis-related proteins: molecular mechanisms of gene expression and protein function,” Journal of Biochemistry, vol. 125, no. 1, pp. 1–8, 1999. View at Google Scholar · View at Scopus
  35. S. K. Datta and S. Muthukrishnan, Pathogenesis-Related Proteins in Plants, CRC Press, Boca Raton, Fla, USA, 1999.
  36. L. C. van Loon, M. Rep, and C. M. J. Pieterse, “Significance of inducible defense-related proteins in infected plants,” Annual Review of Phytopathology, vol. 44, pp. 135–162, 2006. View at Publisher · View at Google Scholar · View at Scopus
  37. J. Hejgaard, S. Jacobsen, and I. Svendsen, “Two antifungal thaumatin-like proteins from barley grain,” FEBS Letters, vol. 291, no. 1, pp. 127–131, 1991. View at Publisher · View at Google Scholar · View at Scopus
  38. C. Caruso, C. Caporale, G. Chilosi et al., “Structural and antifungal properties of a pathogenesis-related protein from wheat kernel,” Journal of Protein Chemistry, vol. 15, no. 1, pp. 35–44, 1996. View at Publisher · View at Google Scholar · View at Scopus
  39. J. R. Cutt, M. H. Harpster, D. C. Dixon, J. P. Carr, P. Dunsmuir, and D. F. Klessig, “Disease response to tobacco mosaic virus in transgenic tobacco plants that constitutively express the pathogenesis-related PR1b gene,” Virology, vol. 173, no. 1, pp. 89–97, 1989. View at Google Scholar · View at Scopus
  40. A. Edreva, “Pathogenesis-related proteins: research progress in the last 15 years,” General and Applied Plant Physiology, vol. 31, no. 1-2, pp. 105–124, 2005. View at Google Scholar
  41. E. Kombrink, M. Schroder, and K. Hahlbrock, “Several ”pathogenesis-related“ proteins in potato are 1,3-β-glucanases and chitinases,” Proceedings of the National Academy of Sciences of the United States of America, vol. 85, no. 3, pp. 782–786, 1988. View at Publisher · View at Google Scholar
  42. T. Heitz, S. Segond, S. Kauffmann et al., “Molecular characterization of a novel tobacco pathogenesis-related (PR) protein: a new plant chitinase/lysozyme,” Molecular and General Genetics, vol. 245, no. 2, pp. 246–254, 1994. View at Google Scholar · View at Scopus
  43. F. T. Lay and M. A. Anderson, “Defensins—components of the innate immune system in plants,” Current Protein and Peptide Science, vol. 6, no. 1, pp. 85–101, 2005. View at Publisher · View at Google Scholar · View at Scopus
  44. M. C. Regente, A. M. Giudici, J. Villalaín, and L. de la Canal, “The cytotoxic properties of a plant lipid transfer protein involve membrane permeabilization of target cells,” Letters in Applied Microbiology, vol. 40, no. 3, pp. 183–189, 2005. View at Publisher · View at Google Scholar · View at Scopus
  45. T. Heitz, P. Geoffroy, B. Fritig, and M. Legrand, “Two apoplastic α-amylases are induced in tobacco by virus infection,” Plant Physiology, vol. 97, no. 2, pp. 651–655, 1991. View at Google Scholar · View at Scopus
  46. G. De Lorenzo, R. D'Ovidio, and F. Cervone, “The role of polygalacturonase-inhibiting proteins (PGIPS) in defense against pathogenic fungi,” Annual Review of Phytopathology, vol. 39, pp. 313–335, 2001. View at Publisher · View at Google Scholar · View at Scopus
  47. S. Deepak, S. Shailasree, R. K. Kini, B. Hause, S. H. Shetty, and A. Mithöfer, “Role of hydroxyproline-rich glycoproteins in resistance of pearl millet against downy mildew pathogen Sclerospora graminicola,” Planta, vol. 226, no. 2, pp. 323–333, 2007. View at Publisher · View at Google Scholar · View at Scopus
  48. A. Akram, M. Ongena, F. Duby, J. Dommes, and P. Thonart, “Systemic resistance and lipoxygenase-related defence response induced in tomato by Pseudomonas putida strain BTP1,” BMC Plant Biology, vol. 8, article 113, 2008. View at Publisher · View at Google Scholar · View at Scopus
  49. S. Cândido Ede, M. F. Pinto, P. B. Pelegrini et al., “Plant storage proteins with antimicrobial activity: novel insights into plant defense mechanisms,” FASEB Journal, vol. 25, no. 10, pp. 3290–3305, 2011. View at Publisher · View at Google Scholar
  50. W. J. Peumans and E. J. van Damme, “Lectins as plant defense proteins,” Plant Physiology, vol. 109, no. 2, pp. 347–352, 1995. View at Google Scholar · View at Scopus
  51. W. J. Peumans, Q. Hao, and E. J. M. van Damme, “Ribosome-inactivating proteins from plants: more than RNA N-glycosidases?” FASEB Journal, vol. 15, no. 9, pp. 1493–1506, 2001. View at Publisher · View at Google Scholar · View at Scopus
  52. W. F. Broekaert, F. R. G. Terras, and B. P. A. Cammue, “Induced and preformed antimicrobial proteins,” in Mechanisms of Resistance to Plant Diseases, A. J. Slusarenko, R. S. Fraser, and L. C. van Loon, Eds., pp. 371–477, Kluwer Academic Publishers, Dordrecht, The Netherlands, 2000. View at Google Scholar
  53. K. Hoffmann-Sommergruber, “Plant allergens and pathogenesis-related proteins: what do they have in common?” International Archives of Allergy and Immunology, vol. 122, no. 3, pp. 155–166, 2000. View at Google Scholar · View at Scopus
  54. C. Ebner, K. Hoffmann-Sommergruber, and H. Breiteneder, “Plant food allergens homologous to pathogenesis-related proteins,” Allergy, Supplement, vol. 56, no. 67, pp. 43–44, 2001. View at Google Scholar · View at Scopus
  55. T. Midoro-Horiuti, E. G. Brooks, and R. M. Goldblum, “Pathogenesis-related proteins of plants as allergens,” Annals of Allergy, Asthma and Immunology, vol. 87, no. 4, pp. 261–271, 2001. View at Google Scholar · View at Scopus
  56. K. Hoffmann-Sommergruber, “Pathogenesis-related (PR)-proteins identified as allergens,” Biochemical Society Transactions, vol. 30, no. 6, pp. 930–935, 2002. View at Publisher · View at Google Scholar · View at Scopus
  57. L. Halmepuro, K. Vuontela, K. Kalimo, and F. Bjorksten, “Cross-reactivity of IgE antibodies with allergens in birch pollen, fruits and vegetables,” International Archives of Allergy and Applied Immunology, vol. 74, no. 3, pp. 235–240, 1984. View at Google Scholar · View at Scopus
  58. C. Blanco, T. Carrillo, R. Castillo, J. Quiralte, and M. Cuevas, “Latex allergy: clinical features and cross-reactivity with fruits,” Annals of Allergy, vol. 73, no. 4, pp. 309–314, 1994. View at Google Scholar · View at Scopus
  59. R. Asero, “Lipid transfer protein cross-reactivity assessed in vivo and in vitro in the office: pros and cons,” Journal of Investigational Allergology and Clinical Immunology, vol. 21, no. 2, pp. 129–136, 2011. View at Google Scholar · View at Scopus
  60. R. E. Rossi, G. Monasterolo, D. Operti, and M. Corsi, “Evaluation of recombinant allergens Bet v 1 and Bet v 2 (profilin) by Pharmacia CAP System in patients with pollen-related allergy to birch and apple,” Allergy, vol. 51, no. 12, pp. 940–945, 1996. View at Google Scholar · View at Scopus
  61. S. Wagner and H. Breiteneder, “The latex-fruit syndrome,” Biochemical Society Transactions, vol. 30, part 6, pp. 935–940, 2002. View at Google Scholar
  62. A. Leitner, E. Jensen-Jarolim, R. Grimm et al., “Allergens in pepper and paprika: immunologic investigation of the celery-birch-mugwort-spice syndrome,” Allergy, vol. 53, no. 1, pp. 36–41, 1998. View at Google Scholar · View at Scopus
  63. T. Midoro-Horiuti, R. M. Goldblum, A. Kurosky, T. G. Wood, and E. G. Brooks, “Variable expression of pathogenesis-related protein allergen in mountain cedar (Juniperus ashei) pollen,” Journal of Immunology, vol. 164, no. 4, pp. 2188–2192, 2000. View at Google Scholar · View at Scopus
  64. B. J. Cornelissen, R. A. Hooft van Huijsduijnen, L. C. van Loon, and J. F. Bol, “Molecular characterization of messenger RNAs for “pathogenesis related” proteins la, lb and lc, induced by TMV infection of tobacco,” The EMBO Journal, vol. 5, no. 1, pp. 37–40, 1986. View at Google Scholar · View at Scopus
  65. M. H. A. J. Joosten, C. J. B. Bergmans, E. J. S. Meulenhoff, B. J. C. Cornelissen, and P. J. G. M. De Wit, “Purification and serological characterization of three basic 15-kilodalton pathogenesis-related proteins from tomato,” Plant Physiology, vol. 94, no. 2, pp. 585–591, 1990. View at Google Scholar · View at Scopus
  66. T. Niderman, I. Genetet, T. Bruyere et al., “Pathogenesis-related PR-1 proteins are antifungal. Isolation and characterization of three 14-kilodalton proteins of tomato and of a basic PR-1 of tobacco with inhibitory activity against Phytophthora infestans,” Plant Physiology, vol. 108, no. 1, pp. 17–27, 1995. View at Google Scholar · View at Scopus
  67. J. W. Gillikin, W. Burkhart, and J. S. Graham, “Complete amino acid sequence of a polypeptide from Zea mays similar to the pathogenesis-related-1 family,” Plant Physiology, vol. 96, no. 4, pp. 1372–1375, 1991. View at Google Scholar · View at Scopus
  68. Q. Liu and Q. Xue, “Computational identification of novel PR-1-type genes in Oryza sativa,” Journal of Genetics, vol. 85, no. 3, pp. 193–198, 2006. View at Publisher · View at Google Scholar · View at Scopus
  69. T. Asensio, J. F. Crespo, R. Sanchez-Monge et al., “Novel plant pathogenesis-related protein family involved in food allergy,” Journal of Allergy and Clinical Immunology, vol. 114, no. 4, pp. 896–899, 2004. View at Publisher · View at Google Scholar · View at Scopus
  70. P. B. Hoj and G. B. Fincher, “Molecular evolution of plant beta-glucan endohydrolases,” Plant Journal, vol. 7, no. 3, pp. 367–379, 1995. View at Google Scholar · View at Scopus
  71. R. G. Fulcher, M. E. Mc Cully, G. Setterfield, and J. Sutherland, “β-1,3-glucans may be associated with cell plate formation during cytokinesis,” Canadian Journal Botany, vol. 54, pp. 459–542, 1976. View at Google Scholar
  72. P. A. Bucciaglia and A. G. Smith, “Cloning and characterization of Tag 1, a tobacco anther beta-1,3-glucanase expressed during tetrad dissolution,” Plant Molecular Biology, vol. 24, no. 6, pp. 903–914, 1994. View at Google Scholar · View at Scopus
  73. P. J. Meikle, I. Bonig, N. J. Hoogenraad, A. E. Clarke, and B. A. Stone, “The location of (1→3)-β-glucans in the walls of pollen tubes of Nicotiana alata using a (1→3)-β-glucan-specific monoclonal antibody,” Planta, vol. 185, no. 1, pp. 1–8, 1991. View at Publisher · View at Google Scholar · View at Scopus
  74. S. Helleboid, G. Bauw, L. Belingheri, J. Vasseur, and J. L. Fulbert, “Extracellular β-1,3-glucanases are induced during early somatic embryogenesis in Cichorium,” Planta, vol. 205, no. 1, pp. 56–63, 1998. View at Publisher · View at Google Scholar · View at Scopus
  75. G. Leubner-Metzger, C. Frundt, R. Vogeli-Lange, and F. Meins Jnr, “Class I beta-1,3-glucanases in the endosperm of tobacco during germination,” Plant Physiology, vol. 109, no. 3, pp. 751–759, 1995. View at Google Scholar · View at Scopus
  76. G. B. Fincher and B. A. Stone, “Physiology and biochemistry of germination in barley,” in Barley: Chemistry and Technology, A. W. MacGregor and R. S. Bhatty, Eds., pp. 247–295, St. Paul, American Association of Cereal Chemists, 1993. View at Google Scholar
  77. M. Thalmair, G. Bauw, S. Thiel, T. Döhring, C. Langebartels, and H. Sandermann Jr., “Ozone and ultraviolet B effects on the defense-related proteins β-1,3-glucanase and chitinase in Tobacco,” Journal of Plant Physiology, vol. 148, no. 1-2, pp. 222–228, 1996. View at Google Scholar · View at Scopus
  78. D. K. Hincha, F. Meins Jr., and J. M. Schmitt, “β-1,3-glucanase is cryoprotective in vitro and is accumulated in leaves during cold acclimation,” Plant Physiology, vol. 114, no. 3, pp. 1077–1083, 1997. View at Google Scholar · View at Scopus
  79. F. T. Brederode, H. J. M. Linthorst, and J. F. Bol, “Differential induction of acquired resistance and PR gene expression in tobacco by virus infection, ethephon treatment, UV light and wounding,” Plant Molecular Biology, vol. 17, no. 6, pp. 1117–1125, 1991. View at Publisher · View at Google Scholar · View at Scopus
  80. G. Payne, E. Ward, T. Gaffney et al., “Evidence for a third structural class of β-1,3-glucanase in tobacco,” Plant Molecular Biology, vol. 15, no. 6, pp. 797–808, 1990. View at Publisher · View at Google Scholar · View at Scopus
  81. M. V. Bulcke, G. Bauw, C. Castresana, M. van Montagu, and J. Vandekerckhove, “Characterization of vacuolar and extracellular β-(1,3)-glucanases of tobacco: evidence for a strictly compartmentalized plant defense system,” Proceedings of the National Academy of Sciences of the United States of America, vol. 86, no. 8, pp. 2673–2677, 1989. View at Publisher · View at Google Scholar
  82. C. R. Simmons, “The physiology and molecular biology of plant 1,3-β-D-glucanases and 1,3;1,4-β-D-glucanases,” Critical Reviews in Plant Sciences, vol. 13, no. 4, pp. 325–387, 1994. View at Publisher · View at Google Scholar
  83. L. Sticher, U. Hinz, A. D. Meyer, and F. Meins Jr., “Intracellular transport and processing of a tobacco vacuolar β-1,3-glucanase,” Planta, vol. 188, no. 4, pp. 559–565, 1992. View at Publisher · View at Google Scholar · View at Scopus
  84. C. A. Hirshman, “Latex anaphylaxis,” Anesthesiology, vol. 77, no. 2, pp. 223–225, 1992. View at Google Scholar · View at Scopus
  85. R. De Zotti, F. Larese, and A. Fiorito, “Asthma and contact urticaria from latex gloves in a hospital nurse,” British Journal of Industrial Medicine, vol. 49, no. 8, pp. 596–598, 1992. View at Google Scholar · View at Scopus
  86. M. L. Chye and K. Y. Cheung, “β-1,3-glucanase is highly-expressed in laticifers of Hevea brasiliensis,” Plant Molecular Biology, vol. 29, no. 2, pp. 397–402, 1995. View at Google Scholar · View at Scopus
  87. E. Sunderasan, S. Hamzah, S. Hamid et al., “Latex B-serum β-1,3-glucanase (Hev b 2) and a component of the microhelix (Hev b 4) are major latex allergens,” Journal of Natural Rubber Research, vol. 10, pp. 82–99, 1996. View at Google Scholar
  88. V. P. Kurup, H. Y. Yeang, G. L. Sussman et al., “Detection of immunoglobulin antibodies in the sera of patients using purified latex allergens,” Clinical and Experimental Allergy, vol. 30, no. 3, pp. 359–369, 2000. View at Publisher · View at Google Scholar · View at Scopus
  89. V. P. Kurup, G. L. Sussman, H. Y. Yeang et al., “Specific IgE response to purified and recombinant allergens in latex allergy,” Clinical and Molecular Allergy, vol. 3, article 11, 2005. View at Publisher · View at Google Scholar · View at Scopus
  90. A. Barre, R. Culerrier, C. Granier et al., “Mapping of IgE-binding epitopes on the major latex allergen Hev b 2 and the cross-reacting 1,3-β-glucanase fruit allergens as a molecular basis for the latex-fruit syndrome,” Molecular Immunology, vol. 46, no. 8-9, pp. 1595–1604, 2009. View at Publisher · View at Google Scholar · View at Scopus
  91. C. Blanco, T. Carrillo, R. Castillo, J. Quiralte, and M. Cuevas, “Avocado hypersensitivity,” Allergy, vol. 49, no. 6, pp. 454–459, 1994. View at Google Scholar · View at Scopus
  92. R. Brehler, U. Theissen, C. Mohr, and T. Luger, “‘Latex-fruit syndrome’: frequency of cross-reacting IgE antibodies,” Allergy, vol. 52, no. 4, pp. 404–410, 1997. View at Google Scholar · View at Scopus
  93. S. Wagner, C. Radauer, C. Hafner et al., “Characterization of cross-reactive bell pepper allergens involved in the latex-fruit syndrome,” Clinical and Experimental Allergy, vol. 34, no. 11, pp. 1739–1746, 2004. View at Publisher · View at Google Scholar · View at Scopus
  94. S. K. Clendennen and G. D. May, “Differential gene expression in ripening banana fruit,” Plant Physiology, vol. 115, no. 2, pp. 463–469, 1997. View at Google Scholar · View at Scopus
  95. S. Huecas, M. Villalba, and R. Rodríguez, “Ole e 9, a major olive pollen allergen is a 1,3-β-glucanase: isolation, characterization, amino acid sequence, and tissue specificity,” Journal of Biological Chemistry, vol. 276, no. 30, pp. 27959–27966, 2001. View at Publisher · View at Google Scholar · View at Scopus
  96. M. Á. Treviño, O. Palomares, I. Castrillo et al., “Solution structure of the C-terminal domain of Ole e 9, a major allergen of olive pollen,” Protein Science, vol. 17, no. 2, pp. 371–376, 2008. View at Publisher · View at Google Scholar · View at Scopus
  97. P. Jollès and R. A. A. Muzzarelli, Chitin and Chitinases, Birkhauser, Basel, Switzerland, 1999.
  98. J. M. Neuhaus, L. Sticher, F. Meins Jr., and T. Boller, “A short C-terminal sequence is necessary and sufficient for the targeting of chitinases to the plant vacuole,” Proceedings of the National Academy of Sciences of the United States of America, vol. 88, no. 22, pp. 10362–10366, 1991. View at Google Scholar · View at Scopus
  99. L. S. Graham and M. B. Sticklen, “Plant chitinases,” Canadian Journal of Botany, vol. 72, no. 8, pp. 1057–1083, 1994. View at Google Scholar · View at Scopus
  100. A. Diaz-Perales, C. Collada, C. Blanco et al., “Class I chitinases with hevein-like domain, but not class II enzymes, are relevant chestnut and avocado allergens,” Journal of Allergy and Clinical Immunology, vol. 102, no. 1, pp. 127–133, 1998. View at Publisher · View at Google Scholar · View at Scopus
  101. S. Sowka, L. S. Hsieh, M. Krebitz et al., “Identification and cloning of Prs a 1, a 32-kDa endochitinase and major allergen of avocado, and its expression in the yeast Pichia pastoris,” Journal of Biological Chemistry, vol. 273, no. 43, pp. 28091–28097, 1998. View at Publisher · View at Google Scholar · View at Scopus
  102. A. Posch, C. H. Wheeler, Z. Chen et al., “Class I endochitinase containing a hevein domain is the causative allergen in latex-associated avocado allergy,” Clinical and Experimental Allergy, vol. 29, no. 5, pp. 667–672, 1999. View at Publisher · View at Google Scholar
  103. R. Sanchez-Monge, C. Blanco, A. Dïaz-Perales et al., “Isolation and characterization of major banana allergens: identification as fruit class I chitinases,” Clinical and Experimental Allergy, vol. 29, no. 5, pp. 673–680, 1999. View at Publisher · View at Google Scholar · View at Scopus
  104. A. S. Ponstein, S. A. Bres-Vloemans, M. B. Sela-Buurlage, P. J. M. van den Elzen, L. S. Melchers, and B. J. C. Cornelissen, “A novel pathogen- and wound-inducible tobacco (Nicotiana tabacum) protein with antifungal activity,” Plant Physiology, vol. 104, no. 1, pp. 109–118, 1994. View at Google Scholar · View at Scopus
  105. S. Ludvigsen and F. M. Poulsen, “Three-dimensional structure in solution of barwin, a protein from barley seed,” Biochemistry, vol. 31, no. 37, pp. 8783–8789, 1992. View at Google Scholar · View at Scopus
  106. H. Alenius, N. Kalkkinen, M. Lukka et al., “Prohevein from the rubber tree (Hevea brasiliensis) is a major latex allergen,” Clinical and Experimental Allergy, vol. 25, no. 7, pp. 659–665, 1995. View at Publisher · View at Google Scholar · View at Scopus
  107. M. Raulf-Heimsoth, P. Rozynek, T. Brüning, and H. P. Rihs, “Characterization of B- and T-cell responses and HLA-DR4 binding motifs of the latex allergen Hev b 6.01 (prohevein) and its post-transcriptionally formed proteins Hev b 6.02 and Hev b 6.03,” Allergy, vol. 59, no. 7, pp. 724–733, 2004. View at Publisher · View at Google Scholar · View at Scopus
  108. P. Karisola, A. Kotovuori, S. Poikonen et al., “Isolated hevein-like domains, but not 31-kd endochitinases, are responsible for IgE-mediated in vitro and in vivo reactions in latex-fruit syndrome,” Journal of Allergy and Clinical Immunology, vol. 115, no. 3, pp. 598–605, 2005. View at Publisher · View at Google Scholar · View at Scopus
  109. Z. Chen, A. Posch, R. Cremer, M. Raulf-Heimsoth, and X. Baur, “Identification of hevein (Hev b 6.02) in Hevea latex as a major cross-reacting allergen with avocado fruit in patients with latex allergy,” Journal of Allergy and Clinical Immunology, vol. 102, no. 3, pp. 476–481, 1998. View at Google Scholar · View at Scopus
  110. C. A. Reyes-López, A. Hernández-Santoyo, M. Pedraza-Escalona, G. Mendoza, A. Hernández-Arana, and A. Rodríguez-Romero, “Insights into a conformational epitope of Hev b 6.02 (hevein),” Biochemical and Biophysical Research Communications, vol. 314, no. 1, pp. 123–130, 2004. View at Publisher · View at Google Scholar · View at Scopus
  111. A. C. Drew, N. P. Eusebius, L. Kenins et al., “Hypoallergenic variants of the major latex allergen Hev b 6.01 retaining human T lymphocyte reactivity,” Journal of Immunology, vol. 173, no. 9, pp. 5872–5879, 2004. View at Google Scholar · View at Scopus
  112. H. J. Linthorst, N. Danhash, F. T. Brederode, J. A. van Kan, P. J. De Wit, and J. F. Bol, “Tobacco and tomato PR proteins homologous to win and pro-hevein lack the “hevein” domain,” Molecular Plant-Microbe Interactions, vol. 4, no. 6, pp. 586–592, 1991. View at Google Scholar · View at Scopus
  113. A. R. Hänninen, J. H. Mikkola, N. Kalkkinen et al., “Increased allergen production in turnip (Brassica rapa) by treatments activating defense mechanisms,” Journal of Allergy and Clinical Immunology, vol. 104, no. 1, pp. 194–201, 1999. View at Publisher · View at Google Scholar · View at Scopus
  114. W. F. Daniell, “On the Synsepalum dulcificum, Decand, or miraculous berry of Western Africa,” Pharmaceutical Journal, vol. 11, pp. 445–448, 1852. View at Google Scholar
  115. B. J. C. Cornelissen, R. A. M. Hooft van Huijsduijen, and J. F. Bol, “A tobacco mosaic virus-induced tobacco protein is homologous to the sweet-tasting protein thaumatin,” Nature, vol. 321, no. 6069, pp. 531–532, 1986. View at Google Scholar · View at Scopus
  116. N. K. Singh, C. A. Bracker, P. M. Hasegawa et al., “Characterization of osmotin: a thaumatin-like protein associated with osmotic adaptation in plant cells,” Plant Physiology, vol. 85, no. 2, pp. 529–536, 1987. View at Publisher · View at Google Scholar
  117. R. Pressey, “Two isoforms of NP24: a thaumatin-like protein in tomato fruit,” Phytochemistry, vol. 44, no. 7, pp. 1241–1245, 1997. View at Publisher · View at Google Scholar · View at Scopus
  118. N. E. Cheong, Y. O. Choi, W. Y. Kim, S. C. Kim, M. J. Cho, and S. Y. Lee, “Purification of an antifungal PR-5 protein from flower buds of Brassica campestris and cloning of its gene,” Physiologia Plantarum, vol. 101, no. 3, pp. 583–590, 1997. View at Publisher · View at Google Scholar · View at Scopus
  119. B. R. Fils-Lycaon, P. A. Wiersma, K. C. Eastwell, and P. Sautiere, “A cherry protein and its gene, abundantly expressed in ripening fruit, have been identified as thaumatin-like,” Plant Physiology, vol. 111, no. 1, pp. 269–273, 1996. View at Google Scholar · View at Scopus
  120. W. K. Roberts and C. P. Selitrennikoff, “Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity,” Journal of General Microbiology, vol. 136, no. 9, pp. 1771–1778, 1990. View at Google Scholar · View at Scopus
  121. A. J. Vigers, W. K. Roberts, and C. P. Selitrennikoff, “A new family of plant antifungal proteins,” Molecular Plant-Microbe Interactions, vol. 4, no. 4, pp. 315–323, 1991. View at Google Scholar · View at Scopus
  122. N. Futamura, Y. Mukai, M. Sakaguchi et al., “Isolation and characterization of cDNAs that encode homologs of a pathogenesis-related protein allergen from Cryptomeria japonica,” Bioscience, Biotechnology and Biochemistry, vol. 66, no. 11, pp. 2495–2500, 2002. View at Google Scholar · View at Scopus
  123. I. Cortegano, E. Civantos, E. Aceituno et al., “Cloning and expression of a major allergen from Cupressus arizonica pollen, Cup a 3, a PR-5 protein expressed under polluted environment,” Allergy, vol. 59, no. 5, pp. 485–490, 2004. View at Publisher · View at Google Scholar · View at Scopus
  124. T. Midoro-Horiuti, R. M. Goldblum, and E. G. Brooks, “Identification of mutations in the genes for the pollen allergens of eastern red cedar (Juniperus virginiana),” Clinical and Experimental Allergy, vol. 31, no. 5, pp. 771–778, 2001. View at Publisher · View at Google Scholar · View at Scopus
  125. H. C. Fuchs, B. Bohle, Y. Dall'Antonia et al., “Natural and recombinant molecules of the cherry allergen Pru av 2 show diverse structural and B cell characteristics but similar T cell reactivity,” Clinical and Experimental Allergy, vol. 36, no. 3, pp. 359–368, 2006. View at Publisher · View at Google Scholar · View at Scopus
  126. M. D. Anliker, S. Borelli, and B. Wüthrich, “Occupational protein contact dermatitis from spices in a butcher: a new presentation of the mugwort-spice syndrome,” Contact Dermatitis, vol. 46, no. 2, pp. 72–74, 2002. View at Publisher · View at Google Scholar · View at Scopus
  127. M. Krebitz, B. Wagner, F. Ferreira et al., “Plant-based heterologous expression of Mal d 2, a thaumatin-like protein and allergen of apple (Malus domestica), and its characterization as an antifungal protein,” Journal of Molecular Biology, vol. 329, no. 4, pp. 721–730, 2003. View at Publisher · View at Google Scholar · View at Scopus
  128. A. Palacin, J. Rodriguez, C. Blanco et al., “Immunoglobulin e recognition patterns to purified kiwifruit (Actinidinia deliciosa) allergens in patients sensitized to kiwi with different clinical symptoms,” Clinical and Experimental Allergy, vol. 38, no. 7, pp. 1220–1228, 2008. View at Publisher · View at Google Scholar · View at Scopus
  129. A. Palacín, L. Tordesillas, P. Gamboa et al., “Characterization of peach thaumatin-like proteins and their identification as major peach allergens,” Clinical and Experimental Allergy, vol. 40, no. 9, pp. 1422–1430, 2010. View at Publisher · View at Google Scholar · View at Scopus
  130. G. Salcedo, S. Quirce, and A. Diaz-Perales, “Wheat allergens associated with Baker's asthma,” Journal of Investigational Allergology and Clinical Immunology, vol. 21, no. 2, pp. 81–92, 2011. View at Google Scholar · View at Scopus
  131. E. A. Pastorello, L. Farioli, V. Pravettoni et al., “Identification of grape and wine allergens as an endochitinase 4, a lipid-transfer protein, and a thaumatin,” Journal of Allergy and Clinical Immunology, vol. 111, no. 2, pp. 350–359, 2003. View at Publisher · View at Google Scholar · View at Scopus
  132. P. Leone, L. Menu-Bouaouiche, W. J. Peumans et al., “Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7-Å,” Biochimie, vol. 88, no. 1, pp. 45–52, 2006. View at Publisher · View at Google Scholar · View at Scopus
  133. S. Barthakur, V. Babu, and K. C. Bansal, “Over-expression of osmotin induces proline accumulation and confers tolerance to osmotic stress in transgenic tobacco,” Journal of Plant Biochemistry and Biotechnology, vol. 10, no. 1, pp. 31–37, 2001. View at Google Scholar · View at Scopus
  134. P. Sharma, A. K. Singh, B. P. Singh, S. N. Gaur, and N. Arora, “Allergenicity assessment of osmotin, a pathogenesis-related protein, used for transgenic crops,” Journal of Agricultural and Food Chemistry, vol. 59, no. 18, pp. 9990–9995, 2011. View at Publisher · View at Google Scholar · View at Scopus
  135. P. Sharma, S. N. Gaur, and N. Arora, “In silico identification of IgE-binding epitopes of osmotin protein,” PLoS ONE, vol. 8, no. 1, Article ID e54755, 2013. View at Publisher · View at Google Scholar
  136. P. Bernasconi, R. Locher, P. E. Pilet, J. Jollès, and P. Jollès, “Purification and N-terminal amino-acid sequence of a basic lysozyme from Parthenocissus quinquifolia cultured in vitro,” Biochimica et Biophysica Acta, vol. 915, no. 2, pp. 254–260, 1987. View at Google Scholar · View at Scopus
  137. A. C. Terwisscha van Scheltinga, M. Hennig, and B. W. Dijkstra, “The 1.8 Å resolution structure of hevamine, a plant chitinase/lysozyme, and analysis of the conserved sequence and structure motifs of glycosyl hydrolase family 18,” Journal of Molecular Biology, vol. 262, no. 2, pp. 243–257, 1996. View at Publisher · View at Google Scholar · View at Scopus
  138. A. Perrakis, I. Tews, Z. Dauter et al., “Crystal structure of a bacterial chitinase at 2.3 Å resolution,” Structure, vol. 2, no. 12, pp. 1169–1180, 1994. View at Google Scholar · View at Scopus
  139. M. F. Lee, Y. H. Chen, H. C. Lin, H. L. Wang, G. Y. Hwang, and C. H. Wu, “Identification of hevamine and Hev b 1 as major latex allergens in Taiwan,” International Archives of Allergy and Immunology, vol. 139, no. 1, pp. 38–44, 2005. View at Publisher · View at Google Scholar · View at Scopus
  140. M. F. Lee, N. M. Wang, J. L. Han, S. J. Lin, J. J. Tsai, and Y. H. Chen, “Estimating allergenicity of latex gloves using Hev b 1 and hevamine,” Journal of Investigational Allergology and Clinical Immunology, vol. 20, no. 6, pp. 499–505, 2010. View at Google Scholar · View at Scopus
  141. M. F. Lee, G. Y. Hwang, Y. H. Chen, H. C. Lin, and C. H. Wu, “Molecular cloning of Indian jujube (Zizyphus mauritiana) allergen Ziz m 1 with sequence similarity to plant class III chitinases,” Molecular Immunology, vol. 43, no. 8, pp. 1144–1151, 2006. View at Publisher · View at Google Scholar · View at Scopus
  142. M. F. Lee, J. J. Tsai, G. Y. Hwang, S. J. Lin, and Y. H. Chen, “Identification of immunoglobulin E (IgE)-binding epitopes and recombinant IgE reactivities of a latex cross-reacting Indian jujube Ziz m 1 allergen,” Clinical and Experimental Immunology, vol. 152, no. 3, pp. 464–471, 2008. View at Publisher · View at Google Scholar · View at Scopus
  143. M. F. Lee, S. J. Lin, N. M. Wang, H. J. Wu, and Y. H. Chen, “Plant chitinase III Ziz m 1 stimulates multiple cytokines, most predominantly interleukin-13, from peripheral blood mononuclear cells of latex-fruit allergic patients,” Annals of Allergy, Asthma and Immunology, vol. 108, no. 2, pp. 113–116, 2012. View at Publisher · View at Google Scholar · View at Scopus
  144. N. Manavski, U. Peters, R. Brettschneider, M. Oldenburg, X. Baur, and C. Bittner, “Cof a 1: identification, expression and immunoreactivity of the first coffee allergen,” International Archives of Allergy and Immunology, vol. 159, no. 3, pp. 235–242, 2012. View at Publisher · View at Google Scholar
  145. S. A. J. Warner, R. Scott, and J. Draper, “Characterisation of a wound-induced transcript from the monocot asparagus that shares similarity with a class of intracellular pathogenesis-related (PR) proteins,” Plant Molecular Biology, vol. 19, no. 4, pp. 555–561, 1992. View at Publisher · View at Google Scholar · View at Scopus
  146. M. H. Walter, J. W. Liu, C. Grand, C. J. Lamb, and D. Hess, “Bean pathogenesis-related (PR) proteins deduced from elicitor-induced transcripts are members of a ubiquitous new class of conserved PR proteins including pollen allergens,” Molecular and General Genetics, vol. 222, no. 2-3, pp. 353–360, 1990. View at Publisher · View at Google Scholar · View at Scopus
  147. C. Breda, C. Sallaud, J. El-Turk et al., “Defense reaction in Medicago sativa: a gene encoding a class 10 PR protein is expressed in vascular bundles,” Molecular Plant-Microbe Interactions, vol. 9, no. 8, pp. 713–719, 1996. View at Google Scholar · View at Scopus
  148. I. E. Somssich, E. Schmelzer, P. Kawalleck, and K. Hahlbrock, “Gene structure and in situ transcript localization of pathogenesis-related protein 1 in parsley,” MGG Molecular & General Genetics, vol. 213, no. 1, pp. 93–98, 1988. View at Publisher · View at Google Scholar · View at Scopus
  149. A. K. M. Ekramoddoullah, “Physiology and molecular biology of a family of pathogenesis-related PR-10 proteins in conifers,” Journal of Crop Improvement, vol. 10, no. 1-2, pp. 261–280, 2004. View at Publisher · View at Google Scholar · View at Scopus
  150. H. Fernandes, K. Michalska, M. Sikorski, and M. Jaskolski, “Structural and functional aspects of PR-10 proteins,” FEBS Journal, vol. 280, no. 5, pp. 1169–1199, 2013. View at Publisher · View at Google Scholar
  151. N. Tokuriki and D. S. Tawfik, “Protein dynamism and evolvability,” Science, vol. 324, no. 5924, pp. 203–207, 2009. View at Publisher · View at Google Scholar · View at Scopus
  152. J. E. Mogensen, R. Wimmer, J. N. Larsen, M. D. Spangfort, and D. E. Otzen, “The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands,” Journal of Biological Chemistry, vol. 277, no. 26, pp. 23684–23692, 2002. View at Publisher · View at Google Scholar · View at Scopus
  153. H. Breiteneder, K. Pettenburger, A. Bito et al., “The gene coding for the major birch pollen allergen BetvI, is highly homologous to a pea disease resistance response gene,” EMBO Journal, vol. 8, no. 7, pp. 1935–1938, 1989. View at Google Scholar · View at Scopus
  154. M. F. Schenk, J. H. Cordewener, A. H. America, W. P. Van'T Westende, M. J. Smulders, and L. J. Gilissen, “Characterization of PR-10 genes from eight betula species and detection of Bet v 1 isoforms in birch pollen,” BMC Plant Biology, vol. 9, article 24, 2009. View at Publisher · View at Google Scholar · View at Scopus
  155. H. Breiteneder, K. Hoffmann-Sommergruber, G. O'Riordain 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,” European Journal of Biochemistry, vol. 233, no. 2, pp. 484–489, 1995. View at Google Scholar · View at Scopus
  156. M. Vanek-Krebitz, K. Hoffmann-Sommergruber, M. Laimer da Camara Machado et al., “Cloning and sequencing of Mal d 1, the major allergen from apple (Malus domestica), and its immunological relationship to Bet v 1, the major birch pollen allergen,” Biochemical and Biophysical Research Communications, vol. 214, no. 2, pp. 538–551, 1995. View at Publisher · View at Google Scholar · View at Scopus
  157. E. Jarolim, M. Tejkl, M. Rohac et al., “Monoclonal antibodies against birch pollen allergens: characterization by immunoblotting and use for single-step affinity purification of the major allergen Bet v I,” International Archives of Allergy and Applied Immunology, vol. 90, no. 1, pp. 54–60, 1989. View at Google Scholar · View at Scopus
  158. I. Swoboda, A. Jilek, F. Ferreira et al., “Isoforms of Bet v 1, the major birch pollen allergen, analyzed by liquid chromatography, mass spectrometry, and cDNA cloning,” Journal of Biological Chemistry, vol. 270, no. 6, pp. 2607–2613, 1995. View at Publisher · View at Google Scholar · View at Scopus
  159. P. Neudecker, K. Schweimer, J. Nerkamp et al., “Allergic cross-reactivity made visible. Solution structure of the major cherry allergen Pru av 1,” Journal of Biological Chemistry, vol. 276, no. 25, pp. 22756–22763, 2001. View at Publisher · View at Google Scholar · View at Scopus
  160. Z. Marković-Housley, A. Basle, S. Padavattan, B. Maderegger, T. Schirmer, and K. Hoffmann-Sommergruber, “Structure of the major carrot allergen Dau c 1,” Acta Crystallographica D, vol. 65, part 11, pp. 1206–1212, 2009. View at Publisher · View at Google Scholar · View at Scopus
  161. A. Botton, C. Andreotti, G. Costa, and A. Ramina, “Peach (Prunus persica L. Batsch) allergen-encoding genes are developmentally regulated and affected by fruit load and light radiation,” Journal of Agricultural and Food Chemistry, vol. 57, no. 2, pp. 724–734, 2009. View at Publisher · View at Google Scholar · View at Scopus
  162. F. Karamloo, S. Scheurer, A. Wangorsch, S. May, D. Haustein, and S. Vieths, “Pyr c 1, the major allergen from pear (Pyrus communis), is a new member of the Bet v 1 allergen family,” Journal of Chromatography B, vol. 756, no. 1-2, pp. 281–293, 2001. View at Publisher · View at Google Scholar · View at Scopus
  163. O. Mirza, A. Henriksen, H. Ipsen 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,” Journal of Immunology, vol. 165, no. 1, pp. 331–338, 2000. View at Google Scholar · View at Scopus
  164. M. Berneder, M. Bublin, K. Hoffmann-Sommergruber, T. Hawranek, and R. Lang, “Allergen chip diagnosis for soy-allergic patients: Gly m 4 as a marker for severe food-allergic reactions to soy,” International Archives of Allergy and Immunology, vol. 161, no. 3, pp. 229–233, 2013. View at Publisher · View at Google Scholar
  165. S. Riecken, B. Lindner, A. Petersen, U. Jappe, and W. M. Becker, “Purification and characterization of natural Ara h 8, the Bet v 1 homologous allergen from peanut, provides a novel isoform,” Biological Chemistry, vol. 389, no. 4, pp. 415–423, 2008. View at Publisher · View at Google Scholar · View at Scopus
  166. D. Mittag, S. Vieths, L. Vogel et al., “Birch pollen-related food allergy to legumes: identification and characterization of the Bet v 1 homologue in mungbean (Vigna radiata), Vig r 1,” Clinical and Experimental Allergy, vol. 35, no. 8, pp. 1049–1055, 2005. View at Publisher · View at Google Scholar · View at Scopus
  167. R. Hirschwehr, R. Valenta, C. Ebner et al., “Identification of common allergenic structures in hazel pollen and hazelnuts: a possible explanation for sensitivity to hazelnuts in patients allergic to tree pollen,” Journal of Allergy and Clinical Immunology, vol. 90, no. 6, part 1, pp. 927–936, 1992. View at Publisher · View at Google Scholar · View at Scopus
  168. R. Hirschwehr, S. Jäger, F. Horak et al., “Allergenss from birch pollen and pollen of the European chestnut share common epitopes,” Clinical and Experimental Allergy, vol. 23, no. 9, pp. 755–761, 1993. View at Google Scholar · View at Scopus
  169. M. Gajhede, P. Osmark, F. M. Poulsen et al., “X-ray and NMR structure of bet v 1, the origin of birch pollen allergy,” Nature Structural Biology, vol. 3, no. 12, pp. 1040–1045, 1996. View at Publisher · View at Google Scholar · View at Scopus
  170. Z. Marković-Housley, M. Degano, D. Lamba et al., “Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier,” Journal of Molecular Biology, vol. 325, no. 1, pp. 123–133, 2003. View at Publisher · View at Google Scholar · View at Scopus
  171. S. Kofler, C. Asam, U. Eckhard, M. Wallner, F. Ferreira, and H. Brandstetter, “Crystallographically mapped ligand binding differs in high and low IgE binding isoforms of birch pollen allergen Bet v 1,” Journal of Molecular Biology, vol. 422, no. 1, pp. 109–123, 2012. View at Publisher · View at Google Scholar
  172. M. D. Spangfort, O. Mirza, H. Ipsen, R. J. J. van Neerven, M. Gajhede, and J. N. Larsen, “Dominating IgE-binding epitope of Bet v 1, the major allergen of birch pollen, characterized by x-ray crystallography and site-directed mutagenesis,” Journal of Immunology, vol. 171, no. 6, pp. 3084–3090, 2003. View at Google Scholar · View at Scopus
  173. P. Neudecker, K. Lehmann, J. Nerkamp et al., “Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure,” Biochemical Journal, vol. 376, part 1, pp. 97–107, 2003. View at Publisher · View at Google Scholar · View at Scopus
  174. R. Crameri, “Correlating IgE reactivity with three-dimensional structure,” The Biochemical Journal, vol. 376, part 1, pp. e1–e2, 2003. View at Publisher · View at Google Scholar · View at Scopus
  175. T. Schirmer, K. Hoffimann-Sommergrube, M. Susani, H. Breiteneder, and Z. Marković-Housley, “Crystal structure of the major celery allergen Api g 1: molecular analysis of cross-reactivity,” Journal of Molecular Biology, vol. 351, no. 5, pp. 1101–1109, 2005. View at Publisher · View at Google Scholar · View at Scopus
  176. R. Fritsch, B. Bohle, U. Vollmann et al., “Bet v 1, the major birch pollen allergen, and Mal d 1, the major apple allergen, cross-react at the level of allergen-specific T helper cells,” Journal of Allergy and Clinical Immunology, vol. 102, no. 4, part 1, pp. 679–686, 1998. View at Google Scholar · View at Scopus
  177. D. B. Zilversmit, “Lipid transfer proteins,” Journal of Lipid Research, vol. 25, no. 13, pp. 1563–1569, 1984. View at Google Scholar · View at Scopus
  178. J. C. Kader, “Lipid-transfer proteins in plants,” Annual Review of Plant Physiology and Plant Molecular Biology, vol. 47, no. 1, pp. 627–654, 1996. View at Google Scholar · View at Scopus
  179. J. Nieuwland, R. Feron, B. A. H. Huisman et al., “Lipid transfer proteins enhance cell wall extension in tobacco,” Plant Cell, vol. 17, no. 7, pp. 2009–2019, 2005. View at Publisher · View at Google Scholar · View at Scopus
  180. G. Salcedo, R. Sánchez-Monge, D. Barber, and A. Díaz-Perales, “Plant non-specific lipid transfer proteins: an interface between plant defence and human allergy,” Biochimica et Biophysica Acta, vol. 1771, no. 6, pp. 781–791, 2007. View at Publisher · View at Google Scholar · View at Scopus
  181. R. van Ree, “Clinical importance of non-specific lipid transfer proteins as food allergens,” Biochemical Society Transactions, vol. 30, part 6, pp. 910–913, 2002. View at Publisher · View at Google Scholar · View at Scopus
  182. E. A. Pastorello, V. Pravettoni, L. Farioli et al., “Clinical role of a lipid transfer protein that acts as a new apple-specific allergen,” Journal of Allergy and Clinical Immunology, vol. 104, pp. 1099–1106, 1999. View at Publisher · View at Google Scholar
  183. E. A. Pastorello, F. P. D'Ambrosio, V. Pravettoni et al., “Evidence for a lipid transfer protein as the major allergen of apricot,” Journal of Allergy and Clinical Immunology, vol. 105, no. 2, part 1, pp. 371–377, 2000. View at Google Scholar · View at Scopus
  184. S. Scheurer, I. Lauer, K. Foetisch et al., “Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion,” Journal of Allergy and Clinical Immunology, vol. 114, no. 4, pp. 900–907, 2004. View at Publisher · View at Google Scholar · View at Scopus
  185. E. A. Pastorello, L. Farioli, V. Pravettoni et al., “Characterization of the major allergen of plum as a lipid transfer protein,” Journal of Chromatography B, vol. 756, no. 1-2, pp. 95–103, 2001. View at Publisher · View at Google Scholar · View at Scopus
  186. M. Fernández-Rivas, R. van Ree, and M. Cuevas, “Allergy to Rosaceae fruits without related pollinosis,” Journal of Allergy and Clinical Immunology, vol. 100, no. 6, part 1, pp. 728–733, 1997. View at Publisher · View at Google Scholar · View at Scopus
  187. N. Pasquato, R. Berni, C. Folli et al., “Crystal structure of peach Pru p 3, the prototypic member of the family of plant non-specific lipid transfer protein pan-allergens,” Journal of Molecular Biology, vol. 356, no. 3, pp. 684–694, 2006. View at Publisher · View at Google Scholar · View at Scopus
  188. G. García-Casado, L. F. Pacios, A. Díaz-Perales et al., “Identification of IgE-binding epitopes of the major peach allergen Pru p 3,” Journal of Allergy and Clinical Immunology, vol. 112, no. 3, pp. 599–605, 2003. View at Publisher · View at Google Scholar · View at Scopus
  189. M. Egger, M. Hauser, A. Mari, F. Ferreira, and G. Gadermaier, “The role of lipid transfer proteins in allergic diseases,” Current Allergy and Asthma Reports, vol. 10, no. 5, pp. 326–335, 2010. View at Publisher · View at Google Scholar · View at Scopus
  190. F. Schocker, D. Lüttkopf, S. Scheurer et al., “Recombinant lipid transfer protein Cor a 8 from hazelnut: a new tool for in vitro diagnosis of potentially severe hazelnut allergy,” Journal of Allergy and Clinical Immunology, vol. 113, no. 1, pp. 141–147, 2004. View at Publisher · View at Google Scholar · View at Scopus
  191. K. H. Roux, S. S. Teuber, and S. K. Sathe, “Tree nut allergens,” International Archives of Allergy and Immunology, vol. 131, no. 4, pp. 234–244, 2003. View at Publisher · View at Google Scholar · View at Scopus
  192. E. A. Pastorello, L. Farioli, V. Pravettoni et al., “The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein,” Journal of Allergy and Clinical Immunology, vol. 106, no. 4, pp. 744–751, 2000. View at Google Scholar · View at Scopus
  193. A. Nemni, J. P. Borges, P. Rougé, A. Barre, and J. Just, “Barley's lipid transfer protein: a new emerging allergen in pediatric anaphylaxis,” Pediatric Allergy and Immunology, vol. 24, no. 4, pp. 410–411, 2013. View at Publisher · View at Google Scholar
  194. P. Colombo, D. Kennedy, T. Ramsdale et al., “Identification of an immunodominant IgE epitope of the Parietaria judaica major allergen,” Journal of Immunology, vol. 160, no. 6, pp. 2780–2785, 1998. View at Google Scholar · View at Scopus
  195. D. A. Dempsey, H. Silva, and D. F. Klessig, “Engineering disease and pest resistance in plants,” Trends in Microbiology, vol. 6, no. 2, pp. 54–61, 1998. View at Publisher · View at Google Scholar · View at Scopus
  196. D. Liu, K. G. Raghothama, P. M. Hasegawa, and R. A. Bressan, “Osmotin overexpression in potato delays development of disease symptoms,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 5, pp. 1888–1892, 1994. View at Google Scholar · View at Scopus
  197. D. Alexander, R. M. Goodman, M. Gut-Rella et al., “Increased tolerance to two oomycete pathogens in transgenic tobacco expressing pathogenesis-related protein 1a,” Proceedings of the National Academy of Sciences of the United States of America, vol. 90, no. 15, pp. 7327–7331, 1993. View at Google Scholar · View at Scopus
  198. V. Balasubramanian, D. Vashisht, J. Cletus, and N. Sakthivel, “Plant β-1,3-glucanases: their biological functions and transgenic expression against phytopathogenic fungi,” Biotechnology Letters, vol. 34, no. 11, pp. 1983–1990, 2012. View at Publisher · View at Google Scholar
  199. A. Anand, T. Zhou, H. N. Trick, B. S. Gill, W. W. Bockus, and S. Muthukrishnan, “Greenhouse and field testing of transgenic wheat plants stably expressing genes for thaumatin-like protein, chitinase and glucanase against Fusarium graminearum,” Journal of Experimental Botany, vol. 54, no. 384, pp. 1101–1111, 2003. View at Publisher · View at Google Scholar · View at Scopus
  200. G. J. Young, S. Zhang, H. P. Mirsky et al., “Assessment of possible allergenicity of hypothetical ORFs in common food crops using current bioinformatic guidelines and its implications for the safety assessment of GM crops,” Food and Chemical Toxicology, vol. 50, no. 10, pp. 3741–3751, 2012. View at Publisher · View at Google Scholar
  201. D. D. Metcalfe, “Genetically modified crops and allergenicity,” Nature Immunology, vol. 6, no. 9, pp. 857–860, 2005. View at Publisher · View at Google Scholar · View at Scopus
  202. S. L. Taylor, “Protein allergenicity assessment of foods produced through agricultural biotechnology,” Annual Review of Pharmacology and Toxicology, vol. 42, pp. 99–112, 2002. View at Publisher · View at Google Scholar · View at Scopus