Structure, Allergenicity, and Cross-Reactivity of Plant Allergens

Chapter
Part of the Immunomics Reviews book series (IMMUN, volume 2)

Abstract

Within the last two decades, hundreds of allergenic proteins from diverse sources have been identified. The availability of numerous allergen sequences provided the basis for classifying allergens into families of evolutionary and structurally related proteins. This chapter gives an introduction into the protein family classification of allergens of plant origin. Our analysis showed that the majority of plant allergens could be grouped into a small number of protein families. The most important families of plant allergens are the prolamin superfamily, which contains several groups of important food and respiratory allergens, the profilins and the Bet v 1-related proteins, two families of allergens responsible for cross-reactivity between pollen and plant foods, and the seed storage globulins, major allergenic components of legumes, tree nuts, and other dicotyledonous seeds. The molecular classification of allergens can be used to establish a correlation between sequence and structural similarity and cross-reactivity among homologous allergens, delineate common properties of allergens, and deduce possible factors that make proteins allergenic.

Keywords

Food allergy Pollen allergy Allergens Protein families 

Abbreviations

HMM

hidden Markov model

IgE

immunoglobulin

nsLTP

non-specific lipid transfer protein

PR-10

pathogenesis-related proteins family 10.

Notes

Acknowledgments

The authors wish to acknowledge the support of the Austrian Science Fund grant SFB F01802.

References

  1. Adachi, M., Takenaka, Y., Gidamis, A.B., Mikami, B. and Utsumi, S. (2001) Crystal structure of soybean proglycinin A1aB1b homotrimer. J. Mol. Biol. 305, 291–305.PubMedGoogle Scholar
  2. Adachi, M., Kanamori, J., Masuda, T., Yagasaki, K., Kitamura, K., Mikami, B. and Utsumi, S. (2003) Crystal structure of soybean 11S globulin: glycinin A3B4 homohexamer. Proc. Natl. Acad. Sci. U. S. A. 100, 7395–7400.PubMedGoogle Scholar
  3. Alcocer, M.J., Murtagh, G.J., Bailey, K., Dumoulin, M., Meseguer, A.S., Parker, M.J. and Archer, D.B. (2002) The disulphide mapping, folding and characterisation of recombinant Ber e 1, an allergenic protein, and SFA8, two sulphur-rich 2S plant albumins. J. Mol. Biol. 324, 165–175.PubMedGoogle Scholar
  4. Andersson, K. and Lidholm, J. (2003) Characteristics and immunobiology of grass pollen allergens. Int. Arch. Allergy Immunol. 130, 87–107.PubMedGoogle Scholar
  5. Asero, R., Mistrello, G., Roncarolo, D., Amato, S. and van Ree, R. (2001) A case of allergy to beer showing cross-reactivity between lipid transfer proteins. Ann. Allergy. Asthma. Immunol. 87, 65–67.PubMedGoogle Scholar
  6. Asero, R., Mistrello, G., Roncarolo, D., Amato, S., Zanoni, D., Barocci, F. and Caldironi, G. (2003) Detection of clinical markers of sensitization to profilin in patients allergic to plant-derived foods. J. Allergy Clin. Immunol. 112, 427–432.PubMedGoogle Scholar
  7. Bartolome, B., Mendez, J.D., Armentia, A., Vallverdu, A. and Palacios, R. (1997) Allergens from Brazil nut: immunochemical characterization. Allergol. Immunopathol. (Madr). 25, 135–144.Google Scholar
  8. Beardslee, T.A., Zeece, M.G., Sarath, G. and Markwell, J.P. (2000) Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int. Arch. Allergy Immunol. 123, 299–307.PubMedGoogle Scholar
  9. Behnke, C.A., Yee, V.C., Trong, I.L., Pedersen, L.C., Stenkamp, R.E., Kim, S.S., Reeck, G.R. and Teller, D.C. (1998) Structural determinants of the bifunctional corn Hageman factor inhibitor: x-ray crystal structure at 1.95 A resolution. Biochemistry (Mosc). 37, 15277–15288.Google Scholar
  10. Beyer, K., Bardina, L., Grishina, G. and Sampson, H.A. (2002) Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: seed storage proteins as common food allergens. J. Allergy Clin. Immunol. 110, 154–159.PubMedGoogle Scholar
  11. Björklund, A.K., Soeria-Atmadja, D., Zorzet, A., Hammerling, U. and Gustafsson, M.G. (2005) Supervised identification of allergen-representative peptides for in silico detection of potentially allergenic proteins. Bioinformatics 21, 39–50.PubMedGoogle Scholar
  12. Breiteneder, H., Pettenburger, K., Bito, A., Valenta, R., Kraft, D., Rumpold, H., Scheiner, O. and Breitenbach, M. (1989) The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene. EMBO J. 8, 1935–1938.PubMedGoogle Scholar
  13. Breiteneder, H., Hoffmann-Sommergruber, K., O'Riordain, G., Susani, M., Ahorn, H., Ebner, C., Kraft, D. and Scheiner, O. (1995) 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. 233, 484–489.PubMedGoogle Scholar
  14. Breiteneder, H. and Radauer, C. (2004) A classification of plant food allergens. J. Allergy Clin. Immunol. 113, 821–830.PubMedGoogle Scholar
  15. Breiteneder, H. and Mills, C. (2005a) Nonspecific lipid-transfer proteins in plant foods and pollens: an important allergen class. Curr. Opin. Allergy Clin. Immunol. 5, 275–279.Google Scholar
  16. Breiteneder, H. and Mills, E.N. (2005b) Molecular properties of food allergens. J. Allergy Clin. Immunol. 115, 14–23.Google Scholar
  17. Breiteneder, H. and Mills, E.N. (2005c) Plant food allergens – structural and functional aspects of allergenicity. Biotechnol. Adv. 23, 395–399.Google Scholar
  18. Brenna, O., Pompei, C., Ortolani, C., Pravettoni, V., Farioli, L. and Pastorello, E.A. (2000) Technological processes to decrease the allergenicity of peach juice and nectar. J. Agric. Food Chem. 48, 493–497.PubMedGoogle Scholar
  19. Burks, A.W., Williams, L.W., Helm, R.M., Connaughton, C., Cockrell, G. and O'Brien, T. (1991) Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. J. Allergy Clin. Immunol. 88, 172–179.PubMedGoogle Scholar
  20. Castillo, R.M., Mizuguchi, K., Dhanaraj, V., Albert, A., Blundell, T.L. and Murzin, A.G. (1999) A six-stranded double-psi beta barrel is shared by several protein superfamilies. Structure 7, 227–236.PubMedGoogle Scholar
  21. Cheng, C.S., Samuel, D., Liu, Y.J., Shyu, J.C., Lai, S.M., Lin, K.F. and Lyu, P.C. (2004) Binding mechanism of nonspecific lipid transfer proteins and their role in plant defense. Biochemistry (Mosc). 43, 13628–13636.Google Scholar
  22. Cosgrove, D.J. (2000) Loosening of plant cell walls by expansins. Nature 407, 321–326.PubMedGoogle Scholar
  23. D'Amato, G., Liccardi, G., D'Amato, M. and Holgate, S. (2005) Environmental risk factors and allergic bronchial asthma. Clin. Exp. Allergy 35, 1113–1124.PubMedGoogle Scholar
  24. Douliez, J.P., Jegou, S., Pato, C., Molle, D., Tran, V. and Marion, D. (2001) Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling. Eur. J. Biochem. 268, 384–388.PubMedGoogle Scholar
  25. Douliez, J.P., Sy, D., Vovelle, F. and Marion, D. (2002) Interaction of surfactants and polymer-grafted lipids with a plant lipid transfer protein, LTP1. Langmuir 18, 7309–7312.Google Scholar
  26. Dunwell, J.M. (1998) Cupins: a new superfamily of functionally diverse proteins that include germins and plant storage proteins. Biotechnol. Genet. Eng. Rev. 15, 1–32.PubMedGoogle Scholar
  27. Dunwell, J.M., Khuri, S. and Gane, P.J. (2000) Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily. Microbiol. Mol. Biol. Rev. 64, 153–179.PubMedGoogle Scholar
  28. Dunwell, J.M., Purvis, A. and Khuri, S. (2004) Cupins: the most functionally diverse protein superfamily? Phytochemistry 65, 7–17.PubMedGoogle Scholar
  29. Engel, E., Richter, K., Obermeyer, G., Briza, P., Kungl, A.J., Simon, B., Auer, M., Ebner, C., Rheinberger, H.J., Breitenbach, M. and Ferreira, F. (1997) Immunological and biological properties of Bet v 4, a novel birch pollen allergen with two EF-hand calcium-binding domains. J. Biol. Chem. 272, 28630–28637.PubMedGoogle Scholar
  30. Fedorov, A.A., Ball, T., Mahoney, N.M., Valenta, R. and Almo, S.C. (1997) The molecular basis for allergen cross-reactivity: crystal structure and IgE-epitope mapping of birch pollen profilin. Structure 5, 33–45.PubMedGoogle Scholar
  31. Ferreira, F., Hirtenlehner, K., Jilek, A., Godnik-Cvar, J., Breiteneder, H., Grimm, R., Hoffmann-Sommergruber, K., Scheiner, O., Kraft, D., Breitenbach, M., Rheinberger, H.J. and Ebner, C. (1996) Dissection of immunoglobulin E and T lymphocyte reactivity of isoforms of the major birch pollen allergen Bet v 1: potential use of hypoallergenic isoforms for immunotherapy. J. Exp. Med. 183, 599–609.PubMedGoogle Scholar
  32. Finn, R.D., Mistry, J., Schuster-Bockler, B., Griffiths-Jones, S., Hollich, V., Lassmann, T., Moxon, S., Marshall, M., Khanna, A., Durbin, R., Eddy, S.R., Sonnhammer, E.L. and Bateman, A. (2006) Pfam: clans, web tools and services. Nucleic Acids Res. 34, D247–251.PubMedGoogle Scholar
  33. Fujino, K., Funatsuki, H., Inada, M., Shimono, Y. and Kikuta, Y. (2001) Expression, cloning, and immunological analysis of buckwheat (Fagopyrum esculentum Moench) seed storage proteins. J. Agric. Food Chem. 49, 1825–1829.PubMedGoogle Scholar
  34. Garcia-Robaina, J.C., de la Torre-Morin, F., Sanchez-Machin, I., Sanchez-Monge, R., Barber, D. and Lombardero, M. (2001) Anaphylaxis induced by exercise and wine. Allergy 56, 357–358.PubMedGoogle Scholar
  35. Genov, N., Goshev, I., Nikolova, D., Georgieva, D.N., Filippi, B. and Svendsen, I. (1997) A novel thermostable inhibitor of trypsin and subtilisin from the seeds of Brassica nigra: amino acid sequence, inhibitory and spectroscopic properties and thermostability. Biochim. Biophys. Acta 1341, 157–164.PubMedGoogle Scholar
  36. Gourinath, S., Alam, N., Srinivasan, A., Betzel, C. and Singh, T.P. (2000) Structure of the bifunctional inhibitor of trypsin and alpha-amylase from ragi seeds at 2.2 A resolution. Acta Crystallogr. D. Biol. Crystallogr. 56, 287–293.Google Scholar
  37. Grabarek, Z. (2006) Structural basis for diversity of the EF-hand calcium-binding proteins. J. Mol. Biol. 359, 509–525.PubMedGoogle Scholar
  38. Guerbette, F., Grosbois, M., Jolliot-Croquin, A., Kader, J.C. and Zachowski, A. (1999) Lipid-transfer proteins from plants: structure and binding properties. Mol. Cell. Biochem. 192, 157–161.PubMedGoogle Scholar
  39. Hayek, B., Vangelista, L., Pastore, A., Sperr, W.R., Valent, P., Vrtala, S., Niederberger, V., Twardosz, A., Kraft, D. and Valenta, R. (1998) Molecular and immunologic characterization of a highly cross-reactive two EF-hand calcium-binding alder pollen allergen, Aln g 4: structural basis for calcium-modulated IgE recognition. J. Immunol. 161, 7031–7039.PubMedGoogle Scholar
  40. Helm, R.M., Cockrell, G., Connaughton, C., Sampson, H.A., Bannon, G.A., Beilinson, V., Livingstone, D., Nielsen, N.C. and Burks, A.W. (2000) A soybean G2 glycinin allergen. 1. Identification and characterization. Int. Arch. Allergy Immunol. 123, 205–212.PubMedGoogle Scholar
  41. Hindley, J., Wunschmann, S., Satinover, S.M., Woodfolk, J.A., Chew, F.T., Chapman, M.D. and Pomes, A. (2006) Bla g 6: a troponin C allergen from Blattella germanica with IgE binding calcium dependence. J. Allergy Clin. Immunol. 117, 1389–1395.PubMedGoogle Scholar
  42. Hoffmann-Sommergruber, K., O'Riordain, G., Ahorn, H., Ebner, C., Laimer Da Camara Machado, M., Pühringer, H., Scheiner, O. and Breiteneder, H. (1999) Molecular characterization of Dau c 1, the Bet v 1 homologous protein from carrot and its cross-reactivity with Bet v 1 and Api g 1. Clin. Exp. Allergy 29, 840–847.PubMedGoogle Scholar
  43. Itoh, T., Garcia, R.N., Adachi, M., Maruyama, Y., Tecson-Mendoza, E.M., Mikami, B. and Utsumi, S. (2006) Structure of 8Salpha globulin, the major seed storage protein of mung bean. Acta Crystallogr. D. Biol. Crystallogr. 62, 824–832.Google Scholar
  44. James, J.M., Sixbey, J.P., Helm, R.M., Bannon, G.A. and Burks, A.W. (1997) Wheat alpha-amylase inhibitor: a second route of allergic sensitization. J. Allergy Clin. Immunol. 99, 239–244.PubMedGoogle Scholar
  45. Jenkins, J.A., Griffiths-Jones, S., Shewry, P.R., Breiteneder, H. and Mills, E.N. (2005) Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis. J. Allergy Clin. Immunol. 115, 163–170.PubMedGoogle Scholar
  46. Jiang, S.Y., Jasmin, P.X., Ting, Y.Y. and Ramachandran, S. (2005) Genome-wide Identification and Molecular Characterization of Ole_e_I, Allerg_1 and Allerg_2 Domain-containing Pollen-Allergen-like Genes in Oryza sativa. DNA Res. 12, 167–179.PubMedGoogle Scholar
  47. Jones, S.M., Magnolfi, C.F., Cooke, S.K. and Sampson, H.A. (1995) Immunologic cross-reactivity among cereal grains and grasses in children with food hypersensitivity. J. Allergy Clin. Immunol. 96, 341–351.PubMedGoogle Scholar
  48. Karamloo, F., Scheurer, S., Wangorsch, A., May, S., Haustein, D. and Vieths, S. (2001) Pyr c 1, the major allergen from pear (Pyrus communis), is a new member of the Bet v 1 allergen family. J. Chromatogr. B. Biomed. Sci. Appl. 756, 281–293.PubMedGoogle Scholar
  49. Kelly, J.D. and Hefle, S.L. (2000) 2S methionine-rich protein (SSA) from sunflower seed is an IgE-binding protein. Allergy 55, 556–560.PubMedGoogle Scholar
  50. Kleber-Janke, T., Crameri, R., Appenzeller, U., Schlaak, M. and Becker, W.M. (1999) Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology. Int. Arch. Allergy Immunol. 119, 265–274.PubMedGoogle Scholar
  51. Kleine-Tebbe, J., Vogel, L., Crowell, D.N., Haustein, U.F. and Vieths, S. (2002) Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1-related PR-10 protein in soybean, SAM22. J. Allergy Clin. Immunol. 110, 797–804.PubMedGoogle Scholar
  52. Ko, T.P., Day, J. and McPherson, A. (2000) The refined structure of canavalin from jack bean in two crystal forms at 2.1 and 2.0 A resolution. Acta Crystallogr. D. Biol. Crystallogr. 56, 411–420.PubMedGoogle Scholar
  53. Ko, T.P., Kuznetsov, Y.G., Malkin, A.J., Day, J. and McPherson, A. (2001) X-ray diffraction and atomic force microscopy analysis of twinned crystals: rhombohedral canavalin. Acta Crystallogr. D. Biol. Crystallogr. 57, 829–839.PubMedGoogle Scholar
  54. Kreis, M., Forde, B.G., Rahman, S., Miflin, B.J. and Shewry, P.R. (1985) Molecular evolution of the seed storage proteins of barley, rye and wheat. J. Mol. Biol. 183, 499–502.PubMedGoogle Scholar
  55. Lauer, I., Foetisch, K., Kolarich, D., Ballmer-Weber, B.K., Conti, A., Altmann, F., Vieths, S. and Scheurer, S. (2004) Hazelnut (Corylus avellana) vicilin Cor a 11: molecular characterization of a glycoprotein and its allergenic activity. Biochem. J. 383, 327–334.PubMedGoogle Scholar
  56. Lawrence, M.C., Izard, T., Beuchat, M., Blagrove, R.J. and Colman, P.M. (1994) Structure of phaseolin at 2.2 A resolution. Implications for a common vicilin/legumin structure and the genetic engineering of seed storage proteins. J. Mol. Biol. 238, 748–776.PubMedGoogle Scholar
  57. Ledesma, A., Barderas, R., Westritschnig, K., Quiralte, J., Pascual, C.Y., Valenta, R., Villalba, M. and Rodriguez, R. (2006) A comparative analysis of the cross-reactivity in the polcalcin family including Syr v 3, a new member from lilac pollen. Allergy 61, 477–484.PubMedGoogle Scholar
  58. Lehmann, K., Schweimer, K., Reese, G., Randow, S., Suhr, M., Becker, W.M., Vieths, S. and Rosch, P. (2006) Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. Biochem. J. 395, 463–472.PubMedGoogle Scholar
  59. Leonard, R., Petersen, B.O., Himly, M., Kaar, W., Wopfner, N., Kolarich, D., van Ree, R., Ebner, C., Duus, J.O., Ferreira, F. and Altmann, F. (2005) Two novel types of O-glycans on the mugwort pollen allergen Art v 1 and their role in antibody binding. J. Biol. Chem. 280, 7932–7940.PubMedGoogle Scholar
  60. Liscombe, D.K., MacLeod, B.P., Loukanina, N., Nandi, O.I. and Facchini, P.J. (2005) Evidence for the monophyletic evolution of benzylisoquinoline alkaloid biosynthesis in angiosperms. Phytochemistry 66, 2501–2520.PubMedGoogle Scholar
  61. Lopez-Torrejon, G., Salcedo, G., Martin-Esteban, M., Diaz-Perales, A., Pascual, C.Y. and Sanchez-Monge, R. (2003) Len c 1, a major allergen and vicilin from lentil seeds: protein isolation and cDNA cloning. J. Allergy Clin. Immunol. 112, 1208–1215.PubMedGoogle Scholar
  62. Malandain, H. (2005) IgE-reactive carbohydrate epitopes – classification, cross-reactivity, and clinical impact. Allerg. Immunol. (Paris). 37, 122–128.Google Scholar
  63. Maleki, S.J. and Hurlburt, B.K. (2004) Structural and functional alterations in major peanut allergens caused by thermal processing. J. AOAC Int. 87, 1475–1479.PubMedGoogle Scholar
  64. Mari, A. (2001) Multiple pollen sensitization: a molecular approach to the diagnosis. Int. Arch. Allergy Immunol. 125, 57–65.PubMedGoogle Scholar
  65. Mari, A. (2005) Importance of databases in experimental and clinical allergology. Int. Arch. Allergy Immunol. 138, 88–96.PubMedGoogle Scholar
  66. Markovic-Housley, Z., Degano, M., Lamba, D., von Roepenack-Lahaye, E., Clemens, S., Susani, M., Ferreira, F., Scheiner, O. and Breiteneder, H. (2003) 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. J. Mol. Biol. 325, 123–133.PubMedGoogle Scholar
  67. Maruyama, N., Adachi, M., Takahashi, K., Yagasaki, K., Kohno, M., Takenaka, Y., Okuda, E., Nakagawa, S., Mikami, B. and Utsumi, S. (2001) Crystal structures of recombinant and native soybean beta-conglycinin beta homotrimers. Eur. J. Biochem. 268, 3595–3604.PubMedGoogle Scholar
  68. Mena, M., Sanchez-Monge, R., Gomez, L., Salcedo, G. and Carbonero, P. (1992) A major barley allergen associated with baker's asthma disease is a glycosylated monomeric inhibitor of insect alpha-amylase: cDNA cloning and chromosomal location of the gene. Plant Mol. Biol. 20, 451–458.PubMedGoogle Scholar
  69. Menendez-Arias, L., Moneo, I., Dominguez, J. and Rodriguez, R. (1988) Primary structure of the major allergen of yellow mustard (Sinapis alba L.) seed, Sin a I. Eur. J. Biochem. 177, 159–166.PubMedGoogle Scholar
  70. Mills, E.N., Jenkins, J.A., Alcocer, M.J. and Shewry, P.R. (2004) Structural, biological, and evolutionary relationships of plant food allergens sensitizing via the gastrointestinal tract. Crit. Rev. Food Sci. Nutr. 44, 379–407.PubMedGoogle Scholar
  71. Mittag, D., Akkerdaas, J., Ballmer-Weber, B.K., Vogel, L., Wensing, M., Becker, W.M., Koppelman, S.J., Knulst, A.C., Helbling, A., Hefle, S.L., Van Ree, R. and Vieths, S. (2004) Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J. Allergy Clin. Immunol. 114, 1410–1417.PubMedGoogle Scholar
  72. Mittag, D., Vieths, S., Vogel, L., Wagner-Loew, D., Starke, A., Hunziker, P., Becker, W.M. and Ballmer-Weber, B.K. (2005) Birch pollen-related food allergy to legumes: identification and characterization of the Bet v 1 homologue in mungbean (Vigna radiata), Vig r 1. Clin. Exp. Allergy 35, 1049–1055.PubMedGoogle Scholar
  73. Mogensen, J.E., Wimmer, R., Larsen, J.N., Spangfort, M.D. and Otzen, D.E. (2002) The major birch allergen, Bet v 1, shows affinity for a broad spectrum of physiological ligands. J. Biol. Chem. 277, 23684–23692.PubMedGoogle Scholar
  74. Mondoulet, L., Paty, E., Drumare, M.F., Ah-Leung, S., Scheinmann, P., Willemot, R.M., Wal, J.M. and Bernard, H. (2005) Influence of thermal processing on the allergenicity of peanut proteins. J. Agric. Food Chem. 53, 4547–4553.PubMedGoogle Scholar
  75. Müntz, K. (1998) Deposition of storage proteins. Plant Mol. Biol. 38, 77–99.PubMedGoogle Scholar
  76. Nakase, M., Adachi, T., Urisu, A., Miyashita, T., Alvarez, A.M., Nagasaka, S., Aoki, N., Nakamura, R. and Matsuda, T. (1996) Rice (Oryza sativa L.) alpha amylase inhibitors of 14–16 kDa are potential allergens and products of a multi gene family. J. Agric. Food Chem. 44, 2624–2628.Google Scholar
  77. Neudecker, P., Schweimer, K., Nerkamp, J., Scheurer, S., Vieths, S., Sticht, H. and Rösch, P. (2001) Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1. J. Biol. Chem. 276, 22756–22763.PubMedGoogle Scholar
  78. Neudecker, P., Nerkamp, J., Eisenmann, A., Nourse, A., Lauber, T., Schweimer, K., Lehmann, K., Schwarzinger, S., Ferreira, F. and Rösch, P. (2004) Solution structure, dynamics, and hydrodynamics of the calcium-bound cross-reactive birch pollen allergen Bet v 4 reveal a canonical monomeric two EF-hand assembly with a regulatory function. J. Mol. Biol. 336, 1141–1157.PubMedGoogle Scholar
  79. Neuhaus, J. (1999) Plant Chitinases (PR-3, PR-4, PR-8, PR-11). In: S. Datta and S. Muthukrishnan (Eds.), Pathogenesis-related Proteins in Plants. CRC Press, Boca Raton, pp. 77–105.Google Scholar
  80. Niederberger, V., Hayek, B., Vrtala, S., Laffer, S., Twardosz, A., Vangelista, L., Sperr, W.R., Valent, P., Rumpold, H., Kraft, D., Ehrenberger, K., Valenta, R. and Spitzauer, S. (1999) Calcium-dependent immunoglobulin E recognition of the apo- and calcium-bound form of a cross-reactive two EF-hand timothy grass pollen allergen, Phl p 7. FASEB J. 13, 843–856.PubMedGoogle Scholar
  81. Oda, Y., Matsunaga, T., Fukuyama, K., Miyazaki, T. and Morimoto, T. (1997) Tertiary and quaternary structures of 0.19 alpha-amylase inhibitor from wheat kernel determined by X-ray analysis at 2.06 A resolution. Biochemistry (Mosc). 36, 13503–13511.Google Scholar
  82. Okada, T., Sasaki, Y., Ohta, R., Onozuka, N. and Toriyama, K. (2000) Expression of Bra r 1 gene in transgenic tobacco and Bra r 1 promoter activity in pollen of various plant species. Plant Cell Physiol. 41, 757–766.PubMedGoogle Scholar
  83. Onaderra, M., Monsalve, R.I., Mancheno, J.M., Villalba, M., Martinez del Pozo, A., Gavilanes, J.G. and Rodriguez, R. (1994) Food mustard allergen interaction with phospholipid vesicles. Eur. J. Biochem. 225, 609–615.PubMedGoogle Scholar
  84. Pantoja-Uceda, D., Bruix, M., Gimenez-Gallego, G., Rico, M. and Santoro, J. (2003) Solution structure of RicC3, a 2S albumin storage protein from Ricinus communis. Biochemistry (Mosc). 42, 13839–13847.Google Scholar
  85. Pantoja-Uceda, D., Shewry, P.R., Bruix, M., Tatham, A.S., Santoro, J. and Rico, M. (2004) Solution structure of a methionine-rich 2S albumin from sunflower seeds: relationship to its allergenic and emulsifying properties. Biochemistry (Mosc). 43, 6976–6986.Google Scholar
  86. Park, J.W., Kang, D.B., Kim, C.W., Koh, S.H., Yum, H.Y., Kim, K.E., Hong, C.S. and Lee, K.Y. (2000) Identification and characterization of the major allergens of buckwheat. Allergy 55, 1035–1041.PubMedGoogle Scholar
  87. Pasquato, N., Berni, R., Folli, C., Folloni, S., Cianci, M., Pantano, S., Helliwell, J.R. and Zanotti, G. (2006) 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. 356, 684–694.PubMedGoogle Scholar
  88. Pastorello, E.A., Farioli, L., Pravettoni, V., Ortolani, C., Ispano, M., Monza, M., Baroglio, C., Scibola, E., Ansaloni, R., Incorvaia, C. and Conti, A. (1999) The major allergen of peach (Prunus persica) is a lipid transfer protein. J. Allergy Clin. Immunol. 103, 520–526.PubMedGoogle Scholar
  89. Pastorello, E.A., Farioli, L., Pravettoni, V., Ispano, M., Scibola, E., Trambaioli, C., Giuffrida, M.G., Ansaloni, R., Godovac-Zimmermann, J., Conti, A., Fortunato, D. and Ortolani, C. (2000) The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein. J. Allergy Clin. Immunol. 106, 744–751.PubMedGoogle Scholar
  90. Pastorello, E.A., Varin, E., Farioli, L., Pravettoni, V., Ortolani, C., Trambaioli, C., Fortunato, D., Giuffrida, M.G., Rivolta, F., Robino, A., Calamari, A.M., Lacava, L. and Conti, A. (2001) The major allergen of sesame seeds (Sesamum indicum) is a 2S albumin. J. Chromatogr. B. Biomed. Sci. Appl. 756, 85–93.PubMedGoogle Scholar
  91. Pastorello, E.A. and Robino, A.M. (2004) Clinical role of lipid transfer proteins in food allergy. Mol. Nutr. Food Res. 48, 356–362.PubMedGoogle Scholar
  92. Pauli, G., Oster, J.P., Deviller, P., Heiss, S., Bessot, J.C., Susani, M., Ferreira, F., Kraft, D. and Valenta, R. (1996) Skin testing with recombinant allergens rBet v 1 and birch profilin, rBet v 2: diagnostic value for birch pollen and associated allergies. J. Allergy Clin. Immunol. 97, 1100–1109.PubMedGoogle Scholar
  93. Pedrosa, C., De Felice, F.G., Trisciuzzi, C. and Ferreira, S.T. (2000) Selective neoglycosylation increases the structural stability of vicilin, the 7S storage globulin from pea seeds. Arch. Biochem. Biophys. 382, 203–210.PubMedGoogle Scholar
  94. Poltronieri, P., Cappello, M.S., Dohmae, N., Conti, A., Fortunato, D., Pastorello, E.A., Ortolani, C. and Zacheo, G. (2002) Identification and characterisation of the IgE-binding proteins 2S albumin and conglutin gamma in almond (Prunus dulcis) seeds. Int. Arch. Allergy Immunol. 128, 97–104.PubMedGoogle Scholar
  95. Rabjohn, P., Helm, E.M., Stanley, J.S., West, C.M., Sampson, H.A., Burks, A.W. and Bannon, G.A. (1999) Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J. Clin. Invest. 103, 535–542.PubMedGoogle Scholar
  96. Radauer, C. and Hoffmann-Sommergruber, K. (2004) Profilins. In: E.N.C. Mills and P.R. Shewry (Eds.), Plant Food Allergens. Blackwell Publishing, Oxford, UK, pp. 105–124.Google Scholar
  97. Radauer, C. and Breiteneder, H. (2006a) Pollen allergens are restricted to few protein families and show distinct patterns of species distribution. J. Allergy Clin. Immunol. 117, 141–147.Google Scholar
  98. Radauer, C., Willerroider, M., Fuchs, H., Hoffmann-Sommergruber, K., Thalhamer, J., Ferreira, F., Scheiner, O. and Breiteneder, H. (2006b) Cross-reactive and species-specific immunoglobulin E epitopes of plant profilins: an experimental and structure-based analysis. Clin. Exp. Allergy 36, 920–929.Google Scholar
  99. Rautiainen, J., Rytkonen, M., Parkkinen, S., Pentikainen, J., Linnala-Kankkunen, A., Virtanen, T., Pelkonen, J. and Mantyjarvi, R. (1995) cDNA cloning and protein analysis of a bovine dermal allergen with homology to psoriasin. J. Invest. Dermatol. 105, 660–663.PubMedGoogle Scholar
  100. Redfern, O., Grant, A., Maibaum, M. and Orengo, C. (2005) Survey of current protein family databases and their application in comparative, structural and functional genomics. J Chromatogr B Biomed Sci 815, 97–107.Google Scholar
  101. Riaz, T., Hor, H.L., Krishnan, A., Tang, F. and Li, K.B. (2005) WebAllergen: a web server for predicting allergenic proteins. Bioinformatics 21, 2570–2571.PubMedGoogle Scholar
  102. Rico, M., Bruix, M., Gonzalez, C., Monsalve, R.I. and Rodriguez, R. (1996) 1H NMR assignment and global fold of napin BnIb, a representative 2S albumin seed protein. Biochemistry (Mosc). 35, 15672–15682.Google Scholar
  103. Saha, S. and Raghava, G.P. (2006) AlgPred: prediction of allergenic proteins and mapping of IgE epitopes. Nucleic Acids Res. 34, W202–209.PubMedGoogle Scholar
  104. Salcedo, G., Diaz-Perales, A. and Sanchez-Monge, R. (2001) The role of plant panallergens in sensitization to natural rubber latex. Curr. Opin. Allergy Clin. Immunol. 1, 177–183.PubMedGoogle Scholar
  105. Salcedo, G., Sanchez-Monge, R., Diaz-Perales, A., Garcia-Casado, G. and Barber, D. (2004) Plant non-specific lipid transfer proteins as food and pollen allergens. Clin. Exp. Allergy 34, 1336–1341.PubMedGoogle Scholar
  106. Sampedro, J. and Cosgrove, D.J. (2005) The expansin superfamily. Genome Biol. 6, 242.PubMedGoogle Scholar
  107. Sanchez-Monge, R., Gomez, L., Barber, D., Lopez-Otin, C., Armentia, A. and Salcedo, G. (1992) Wheat and barley allergens associated with baker's asthma. Glycosylated subunits of the alpha-amylase-inhibitor family have enhanced IgE-binding capacity. Biochem. J. 281, 401–405.PubMedGoogle Scholar
  108. Sanchez-Monge, R., Lombardero, M., Garcia-Selles, F.J., Barber, D. and Salcedo, G. (1999) Lipid-transfer proteins are relevant allergens in fruit allergy. J. Allergy Clin. Immunol. 103, 514–519.PubMedGoogle Scholar
  109. Sanchez-Monge, R., Lopez-Torrejon, G., Pascual, C.Y., Varela, J., Martin-Esteban, M. and Salcedo, G. (2004) Vicilin and convicilin are potential major allergens from pea. Clin. Exp. Allergy 34, 1747–1753.PubMedGoogle Scholar
  110. Sandiford, C.P., Tatham, A.S., Fido, R., Welch, J.A., Jones, M.G., Tee, R.D., Shewry, P.R. and Newman Taylor, A.J. (1997) Identification of the major water/salt insoluble wheat proteins involved in cereal hypersensitivity. Clin. Exp. Allergy 27, 1120–1129.Google Scholar
  111. Schäppi, G.F., Suphioglu, C., Taylor, P.E. and Knox, R.B. (1997) Concentrations of the major birch tree allergen Bet v 1 in pollen and respirable fine particles in the atmosphere. J. Allergy Clin. Immunol. 100, 656–661.PubMedGoogle Scholar
  112. Scheurer, S., Metzner, K., Haustein, D. and Vieths, S. (1997) Molecular cloning, expression and characterization of Pru a 1, the major cherry allergen. Mol. Immunol. 34, 619–629.PubMedGoogle Scholar
  113. Shewry, P.R., Napier, J.A. and Tatham, A.S. (1995) Seed storage proteins: structures and biosynthesis. Plant Cell 7, 945–956.PubMedGoogle Scholar
  114. Shin, D.H., Lee, J.Y., Hwang, K.Y., Kim, K.K. and Suh, S.W. (1995) High-resolution crystal structure of the non-specific lipid-transfer protein from maize seedlings. Structure 3, 189–199.PubMedGoogle Scholar
  115. Silvanovich, A., Nemeth, M.A., Song, P., Herman, R., Tagliani, L. and Bannon, G.A. (2006) The value of short amino acid sequence matches for prediction of protein allergenicity. Toxicol. Sci. 90, 252–258.PubMedGoogle Scholar
  116. Stadler, M.B. and Stadler, B.M. (2003) Allergenicity prediction by protein sequence. FASEB J. 17, 1141–1143.PubMedGoogle Scholar
  117. Subriade, M., Salesse, D., Marion, D. and Pézolet, M. (1999) Interaction of non-specific wheat lipid transfer protein with phospholipid monolyers imaged by fluorescence microscopy and studied by infrared spectroscopy. Biophys. J. 69, 974–988.Google Scholar
  118. Svendsen, I., Nicolova, D., Goshev, I. and Genov, N. (1994) Primary structure, spectroscopic and inhibitory properties of a two-chain trypsin inhibitor from the seeds of charlock (Sinapis arvensis L), a member of the napin protein family. Int. J. Pept. Protein Res. 43, 425–430.PubMedGoogle Scholar
  119. Swoboda, I., Grote, M., Verdino, P., Keller, W., Singh, M.B., De Weerd, N., Sperr, W.R., Valent, P., Balic, N., Reichelt, R., Suck, R., Fiebig, H., Valenta, R. and Spitzauer, S. (2004) Molecular characterization of polygalacturonases as grass pollen-specific marker allergens: expulsion from pollen via submicronic respirable particles. J. Immunol. 172, 6490–6500.PubMedGoogle Scholar
  120. Tai, S.S., Wu, L.S., Chen, E.C. and Tzen, J.T. (1999) Molecular cloning of 11S globulin and 2S albumin, the two major seed storage proteins in sesame. J. Agric. Food Chem. 47, 4932–4938.PubMedGoogle Scholar
  121. Tamburrini, M., Cerasuolo, I., Carratore, V., Stanziola, A.A., Zofra, S., Romano, L., Camardella, L. and Ciardiello, M.A. (2005) Kiwellin, a novel protein from kiwi fruit. Purification, biochemical characterization and identification as an allergen. Protein J. 24, 423–429.Google Scholar
  122. Tassin, S., Broekaert, W.F., Marion, D., Acland, D.P., Ptak, M., Vovelle, F. and Sodano, P. (1998) Solution structure of Ace-AMP1, a potent antimicrobial protein extracted from onion seeds. Structural analogies with plant nonspecific lipid transfer proteins. Biochemistry (Mosc). 37, 3623–3637.Google Scholar
  123. Taylor, P.E., Flagan, R.C., Miguel, A.G., Valenta, R. and Glovsky, M.M. (2004) Birch pollen rupture and the release of aerosols of respirable allergens. Clin. Exp. Allergy 34, 1591–1596.PubMedGoogle Scholar
  124. Terras, F.R., Schoofs, H.M., De Bolle, M.F., Van Leuven, F., Rees, S.B., Vanderleyden, J., Cammue, B.P. and Broekaert, W.F. (1992) Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. J. Biol. Chem. 267, 15301–15309.PubMedGoogle Scholar
  125. Teuber, S.S., Dandekar, A.M., Peterson, W.R. and Sellers, C.L. (1998) Cloning and sequencing of a gene encoding a 2S albumin seed storage protein precursor from English walnut (Juglans regia), a major food allergen. J. Allergy Clin. Immunol. 101, 807–814.PubMedGoogle Scholar
  126. Teuber, S.S., Jarvis, K.C., Dandekar, A.M., Peterson, W.R. and Ansari, A.A. (1999) Identification and cloning of a complementary DNA encoding a vicilin-like proprotein, Jug r 2, from english walnut kernel (Juglans regia), a major food allergen. J. Allergy Clin. Immunol. 104, 1311–1320.PubMedGoogle Scholar
  127. Teuber, S.S., Sathe, S.K., Peterson, W.R. and Roux, K.H. (2002) Characterization of the soluble allergenic proteins of cashew nut (Anacardium occidentale L.). J. Agric. Food Chem. 50, 6543–6549.PubMedGoogle Scholar
  128. Thorn, K.S., Christensen, H.E., Shigeta, R., Huddler, D., Shalaby, L., Lindberg, U., Chua, N.H. and Schutt, C.E. (1997) The crystal structure of a major allergen from plants. Structure 5, 19–32.PubMedGoogle Scholar
  129. Tinghino, R., Twardosz, A., Barletta, B., Puggioni, E.M., Iacovacci, P., Butteroni, C., Afferni, C., Mari, A., Hayek, B., Di Felice, G., Focke, M., Westritschnig, K., Valenta, R. and Pini, C. (2002) Molecular, structural, and immunologic relationships between different families of recombinant calcium-binding pollen allergens. J. Allergy Clin. Immunol. 109, 314–320.PubMedGoogle Scholar
  130. Valenta, R., Duchene, M., Pettenburger, K., Sillaber, C., Valent, P., Bettelheim, P., Breitenbach, M., Rumpold, H., Kraft, D. and Scheiner, O. (1991) Identification of profilin as a novel pollen allergen; IgE autoreactivity in sensitized individuals. Science 253, 557–560.PubMedGoogle Scholar
  131. Vanek-Krebitz, M., Hoffmann-Sommergruber, K., Laimer da Camara Machado, M., Susani, M., Ebner, C., Kraft, D., Scheiner, O. and Breiteneder, H. (1995) 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. Biochem. Biophys. Res. Commun. 214, 538–551.Google Scholar
  132. Verdino, P., Westritschnig, K., Valenta, R. and Keller, W. (2002) The cross-reactive calcium-binding pollen allergen, Phl p 7, reveals a novel dimer assembly. EMBO J. 21, 5007–5016.PubMedGoogle Scholar
  133. Vieths, S., Scheurer, S. and Ballmer-Weber, B. (2002) Current understanding of cross-reactivity of food allergens and pollen. Ann. N. Y. Acad. Sci. 964, 47–68.PubMedGoogle Scholar
  134. Vioque, J., Sanchez-Vioque, R., Clemente, A., Pedroche, J., Bautista, J. and Millan, F. (1999) Purification and partial characterization of chickpea 2S albumin. J. Agric. Food Chem. 47, 1405–1409.PubMedGoogle Scholar
  135. Vrtala, S., Grote, M., Duchene, M., van Ree, R., Kraft, D., Scheiner, O. and Valenta, R. (1993) Properties of tree and grass pollen allergens: reinvestigation of the linkage between solubility and allergenicity. Int. Arch. Allergy Immunol. 102, 160–169.PubMedGoogle Scholar
  136. Wang, F., Robotham, J.M., Teuber, S.S., Tawde, P., Sathe, S.K. and Roux, K.H. (2002) Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family. J. Allergy Clin. Immunol. 110, 160–166.PubMedGoogle Scholar
  137. Weber, R.W. (2005) Cross-reactivity of pollen allergens: recommendations for immunotherapy vaccines. Curr. Opin. Allergy Clin. Immunol. 5, 563–569.PubMedGoogle Scholar
  138. Wensing, M., Akkerdaas, J.H., van Leeuwen, W.A., Stapel, S.O., Bruijnzeel-Koomen, C.A., Aalberse, R.C., Bast, B.J., Knulst, A.C. and van Ree, R. (2002) IgE to Bet v 1 and profilin: cross-reactivity patterns and clinical relevance. J. Allergy Clin. Immunol. 110, 435–442.PubMedGoogle Scholar
  139. Wicklein, D., Lindner, B., Moll, H., Kolarich, D., Altmann, F., Becker, W.M. and Petersen, A. (2004) Carbohydrate moieties can induce mediator release: a detailed characterization of two major timothy grass pollen allergens. Biol. Chem. 385, 397–407.PubMedGoogle Scholar
  140. Wild, L.G. and Lehrer, S.B. (2005) Fish and shellfish allergy. Curr. Allergy Asthma Rep. 5, 74–79.PubMedGoogle Scholar
  141. Witke, W. (2004) The role of profilin complexes in cell motility and other cellular processes. Trends Cell Biol. 14, 461–469.PubMedGoogle Scholar

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© Springer Science+Business Media, LLC 2009

Authors and Affiliations

  1. 1.Department of Pathophysiology, Center of Physiology and PathophysiologyMedical University of ViennaAustria

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