Table of Contents Author Guidelines Submit a Manuscript
Mediators of Inflammation
Volume 2014, Article ID 291618, 11 pages
http://dx.doi.org/10.1155/2014/291618
Research Article

Reduction of the Number of Major Representative Allergens: From Clinical Testing to 3-Dimensional Structures

1Guangdong Provincial Key Laboratory of Allergy & Immunology, The State Key Laboratory of Respiratory Disease, The Second Affiliated Hospital of Guangzhou Medical University, 250 Changgang Road East, Guangzhou 510260, China
2Plant Biotechnology Research Center, School of Agriculture and Biology, Shanghai Jiao Tong University, Shanghai 200030, China
3Guangdong Provincial Key Laboratory of Allergy & Immunology, The State Key Laboratory of Respiratory Disease, The First Affiliated Hospital of Guangzhou Medical University, 151 Yanjiang Road, Guangzhou 510120, China

Received 10 December 2013; Accepted 7 February 2014; Published 23 March 2014

Academic Editor: Huiyun Zhang

Copyright © 2014 Ying He 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. F. Ferreira, T. Hawranek, P. Gruber, N. Wopfner, and A. Mari, “Allergic cross-reactivity: from gene to the clinic,” Allergy, vol. 59, no. 3, pp. 243–267, 2004. View at Publisher · View at Google Scholar · View at Scopus
  2. C. Radauer and H. Breiteneder, “Pollen allergens are restricted to few protein families and show distinct patterns of species distribution,” Journal of Allergy and Clinical Immunology, vol. 117, no. 1, pp. 141–147, 2006. View at Publisher · View at Google Scholar · View at Scopus
  3. J. A. Jenkins, S. Griffiths-Jones, P. R. Shewry, H. Breiteneder, and E. N. C. Mills, “Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis,” Journal of Allergy and Clinical Immunology, vol. 115, no. 1, pp. 163–170, 2005. View at Publisher · View at Google Scholar · View at Scopus
  4. C. Radauer, M. Bublin, S. Wagner, A. Mari, and H. Breiteneder, “Allergens are distributed into few protein families and possess a restricted number of biochemical functions,” Journal of Allergy and Clinical Immunology, vol. 121, no. 4, pp. 847–852, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. A.-L. Tao and S.-H. He, “Cloning, expression, and characterization of pollen allergens from Humulus scandens (Lour) Merr and Ambrosia artemisiifolia L,” Acta Pharmacologica Sinica, vol. 26, no. 10, pp. 1225–1232, 2005. View at Publisher · View at Google Scholar · View at Scopus
  6. J. A. Nordlee, S. L. Taylor, J. A. Townsend, L. A. Thomas, and R. K. Bush, “Identification of a Brazil-nut allergen in transgenic soybeans,” The New England Journal of Medicine, vol. 334, no. 11, pp. 688–692, 1996. View at Publisher · View at Google Scholar · View at Scopus
  7. U. Seppälä, C. Dauly, S. Robinson, M. Hornshaw, J. N. Larsen, and H. Ipsen, “Absolute quantification of allergens from complex mixtures: a new sensitive tool for standardization of allergen extracts for specific immunotherapy,” Journal of Proteome Research, vol. 10, no. 4, pp. 2113–2122, 2011. View at Publisher · View at Google Scholar · View at Scopus
  8. C. Fernández, R. Cárdenas, D. Martín et al., “Analysis of skin testing and serum-specific immunoglobulin E to predict airway reactivity to cat allergens,” Clinical and Experimental Allergy, vol. 37, no. 3, pp. 391–399, 2007. View at Publisher · View at Google Scholar · View at Scopus
  9. B. Qiao, “Allergen preparation and dispensing,” in Allergology, Y. Shitai, Ed., pp. 713–750, Science Press, Beijing, China, 1998 (Chinese).
  10. W. R. Campbell and M. I. Hanna, “The determination of nitrogen by modified Kjeldahl Methods,” The Journal of Biological Chemistry, vol. 119, no. 1, pp. 1–7, 1937. View at Google Scholar
  11. D. A. Morrow, E. M. Antman, S. A. Murphy et al., “The risk score profile: a novel approach to characterising the risk of populations enrolled in clinical studies,” European Heart Journal, vol. 25, no. 13, pp. 1139–1145, 2004. View at Publisher · View at Google Scholar · View at Scopus
  12. M. A. Larkin, G. Blackshields, N. P. Brown et al., “Clustal W and clustal X version 2.0,” Bioinformatics, vol. 23, no. 21, pp. 2947–2948, 2007. View at Publisher · View at Google Scholar · View at Scopus
  13. S. Kumar, M. Nei, J. Dudley, and K. Tamura, “MEGA: a biologist-centric software for evolutionary analysis of DNA and protein sequences,” Briefings in Bioinformatics, vol. 9, no. 4, pp. 299–306, 2008. View at Publisher · View at Google Scholar · View at Scopus
  14. L. Zhang, Y. Huang, Z. Zou et al., “SORTALLER: predicting allergens using substantially optimized algorithm on allergen family featured peptides,” Bioinformatics, vol. 28, no. 16, pp. 2178–2179, 2012. View at Google Scholar
  15. K. Arnold, L. Bordoli, J. Kopp, and T. Schwede, “The SWISS-MODEL workspace: a web-based environment for protein structure homology modelling,” Bioinformatics, vol. 22, no. 2, pp. 195–201, 2006. View at Publisher · View at Google Scholar · View at Scopus
  16. T. Schwede, J. Kopp, N. Guex, and M. C. Peitsch, “SWISS-MODEL: an automated protein homology-modeling server,” Nucleic Acids Research, vol. 31, no. 13, pp. 3381–3385, 2003. View at Publisher · View at Google Scholar · View at Scopus
  17. E. Batanero, M. A. Gonzalez de la Peña, M. Villalba, R. I. Monsalve, M. Martin-Esteban, and R. Rodriguez, “Isolation, cDNA cloning and expression of Lig v 1, the major allergen from privet pollen,” Clinical and Experimental Allergy, vol. 26, no. 12, pp. 1401–1410, 1996. View at Publisher · View at Google Scholar · View at Scopus
  18. J. de Dios Alché, M. M'rani-Alaoui, A. J. Castro, and M. I. Rodríguez-García, “Ole e 1, the major allergen from olive (Olea europaea L.) pollen, increases its expression and is released to the culture medium during in vitro germination,” Plant and Cell Physiology, vol. 45, no. 9, pp. 1149–1157, 2004. View at Google Scholar · View at Scopus
  19. M. Schmidt, A. Zargari, P. Holt et al., “The complete cDNA sequence and expression of the first major allergenic protein of Malassezia furfur, Mal f 1,” European Journal of Biochemistry, vol. 246, no. 1, pp. 181–185, 1997. View at Google Scholar · View at Scopus
  20. M. L. Kennerson, G. A. Nicholson, S. G. Kaler et al., “Missense mutations in the copper transporter gene ATP7A cause X-linked distal hereditary motor neuropathy,” The American Journal of Human Genetics, vol. 86, no. 3, pp. 343–352, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. M. C. Good, A. E. Greenstein, T. A. Young, H.-L. Ng, and T. Alber, “Sensor domain of the Mycobacterium tuberculosis receptor Ser/Thr protein kinase, PknD, forms a highly symmetric β propeller,” Journal of Molecular Biology, vol. 339, no. 2, pp. 459–469, 2004. View at Publisher · View at Google Scholar · View at Scopus
  22. L. Kaiser, G. Gafvelin, E. Johansson, M. van Hage-Hamsten, and O. Rasool, “Lep d 2 polymorphisms in wild and cultured Lepidoglyphus destructor mites,” European Journal of Biochemistry, vol. 270, no. 4, pp. 646–653, 2003. View at Publisher · View at Google Scholar · View at Scopus
  23. S. Ichikawa, T. Takai, T. Inoue et al., “NMR study on the major mite allergen Der f 2: its refined tertiary structure, epitopes for monoclonal antibodies and characteristics shared by ML protein group members,” Journal of Biochemistry, vol. 137, no. 3, pp. 255–263, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. M. Yokoyama, M. Miyahara, K. Shimizu, K. Kino, and H. Tsunoo, “Purification, identification, and cDNA cloning of Jun a 2, the second major allergen of mountain cedar pollen,” Biochemical and Biophysical Research Communications, vol. 275, no. 1, pp. 195–202, 2000. View at Publisher · View at Google Scholar · View at Scopus
  25. M. Usui, A. Saito, N. Taniguchi, N. Nishijima, H. Azakami, and A. Kato, “Reduction of antigenicity of Cry j I, major allergen of Japanese cedar pollen, by the attachment of polysaccharides,” Bioscience, Biotechnology and Biochemistry, vol. 67, no. 11, pp. 2425–2430, 2003. View at Publisher · View at Google Scholar · View at Scopus
  26. A. Petersen, G. Schramm, A. Bufe, M. Schlaak, and W.-M. Becker, “Structural investigations of the major allergen Phl p I on the complementary DNA and protein level,” Journal of Allergy and Clinical Immunology, vol. 95, no. 5, part 1, pp. 987–994, 1995. View at Publisher · View at Google Scholar · View at Scopus
  27. G. López-Torrejón, G. Salcedo, M. Martín-Esteban, A. Díaz-Perales, C. Y. Pascual, and R. Sánchez-Monge, “Len c 1, a major allergen and vicilin from lentil seeds: protein isolation and cDNA cloning,” Journal of Allergy and Clinical Immunology, vol. 112, no. 6, pp. 1208–1215, 2003. View at Publisher · View at Google Scholar · View at Scopus
  28. K. Fischer, D. C. Holt, P. Harumal, B. J. Currie, S. F. Walton, and D. J. Kemp, “Generation and characterization of cDNA clones from Sarcoptes scabiei var. hominis for an expressed sequence tag library: identification of homologues of house dust mite allergens,” The American Journal of Tropical Medicine and Hygiene, vol. 68, no. 1, pp. 61–64, 2003. View at Google Scholar · View at Scopus
  29. A. Immonen, T. Kinnunen, P. Sirven et al., “The major horse allergen Equ c 1 contains one immunodominant region of T cell epitopes,” Clinical and Experimental Allergy, vol. 37, no. 6, pp. 939–947, 2007. View at Publisher · View at Google Scholar · View at Scopus
  30. A. Gieras, P. Cejka, K. Blatt et al., “Mapping of conformational IgE epitopes with peptide-specific monoclonal antibodies reveals simultaneous binding of different IgE antibodies to a surface patch on the major birch pollen allergen, Bet v 1,” Journal of Immunology, vol. 186, no. 9, pp. 5333–5344, 2011. View at Publisher · View at Google Scholar · View at Scopus
  31. E. Adam, K. K. Hansen, O. F. Astudillo et al., “The house dust mite allergen Der p 1, unlike Der p 3, stimulates the expression of interleukin-8 in human airway epithelial cells via a proteinase-activated receptor-2-independent mechanism,” The Journal of Biological Chemistry, vol. 281, no. 11, pp. 6910–6923, 2006. View at Publisher · View at Google Scholar · View at Scopus
  32. Y. Xia, H. J. Spence, J. Moore et al., “The ABA-1 allergen of Ascaris lumbricoides: sequence polymorphism, stage and tissue-specific expression, lipid binding function, and protein biophysical properties,” Parasitology, vol. 120, no. 2, pp. 211–224, 2000. View at Publisher · View at Google Scholar · View at Scopus
  33. M. Perez-Gordo, J. Cuesta-Herranz, A. S. Maroto et al., “Identification of sole parvalbumin as a major allergen: study of cross-reactivity between parvalbumins in a Spanish fish-allergic population,” Clinical and Experimental Allergy, vol. 41, no. 5, pp. 750–758, 2011. View at Publisher · View at Google Scholar · View at Scopus
  34. E. K. Ong, I. J. Griffith, R. B. Knox, and M. B. Singh, “Cloning of a cDNA encoding a group-V (group-IX) allergen isoform from rye-grass pollen that demonstrates specific antigenic immunoreactivity,” Gene, vol. 134, no. 2, pp. 235–240, 1993. View at Publisher · View at Google Scholar · View at Scopus
  35. R. González-Rioja, J. A. Asturias, A. Martínez, F. M. Goñi, and A. R. Viguera, “Par j 1 and Par j 2, the two major allergens in Parietaria judaica, bind preferentially to monoacylated negative lipids,” FEBS Journal, vol. 276, no. 6, pp. 1762–1775, 2009. View at Publisher · View at Google Scholar · View at Scopus
  36. M. Mena, R. Sanchez-Monge, L. Gomez, G. Salcedo, and P. Carbonero, “A major barley allergen associated with baker's asthma disease is a glycosylated monomeric inhibitor of insect α-amylase: cDNA cloning and chromosomal location of the gene,” Plant Molecular Biology, vol. 20, no. 3, pp. 451–458, 1992. View at Publisher · View at Google Scholar · View at Scopus
  37. M. Emara, P.-J. Royer, Z. Abbas et al., “Recognition of the major cat allergen fel d 1 through the cysteine-rich domain of the mannose receptor determines its allergenicity,” The Journal of Biological Chemistry, vol. 286, no. 15, pp. 13033–13040, 2011. View at Publisher · View at Google Scholar · View at Scopus
  38. T. Grunwald, B. Bockisch, E. Spillner, J. Ring, R. Bredehorst, and M. W. Ollert, “Molecular cloning and expression in insect cells of honeybee venom allergen acid phosphatase (Api m 3),” Journal of Allergy and Clinical Immunology, vol. 117, no. 4, pp. 848–854, 2006. View at Publisher · View at Google Scholar · View at Scopus
  39. P. S. C. Leung and K. H. Chu, “cDNA cloning and molecular identification of the major oyster allergen from the Pacific oyster Crassostrea gigas,” Clinical and Experimental Allergy, vol. 31, no. 8, pp. 1287–1294, 2001. View at Publisher · View at Google Scholar · View at Scopus
  40. C. Nilsson, G. Lilja, M. Nordlund, M. Berthold, and M. P. Borres, “Phadiatop Infant detects IgE-mediated diseases among pre-school children: a prospective study,” Pediatric Allergy and Immunology, vol. 23, no. 2, pp. 160–166, 2012. View at Publisher · View at Google Scholar · View at Scopus
  41. R. W. Weber, “Cross-reactivity of pollen allergens: recommendations for immunotherapy vaccines,” Current Opinion in Allergy and Clinical Immunology, vol. 5, no. 6, pp. 563–569, 2005. View at Google Scholar · View at Scopus
  42. M. B. Stadler and B. M. Stadler, “Allergenicity prediction by protein sequence,” The FASEB Journal, vol. 17, no. 9, pp. 1141–1143, 2003. View at Google Scholar · View at Scopus
  43. J. L. Mueller, D. R. Ripoll, C. F. Aquadro, and M. F. Wolfner, “Comparative structural modeling and inference of conserved protein classes in Drosophila seminal fluid,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 37, pp. 13542–13547, 2004. View at Publisher · View at Google Scholar · View at Scopus
  44. J. Peng and J. Xu, “Low-homology protein threading,” Bioinformatics, vol. 26, no. 12, pp. i294–i300, 2010. View at Publisher · View at Google Scholar · View at Scopus
  45. R. Barderas, M. Villalba, C. Y. Pascual, E. Batanero, and R. Rodríguez, “Profilin (Che a 2) and polcalcin (Che a 3) are relevant allergens of Chenopodium album pollen: isolation, amino acid sequences, and immunologic properties,” Journal of Allergy and Clinical Immunology, vol. 113, no. 6, pp. 1192–1198, 2004. View at Publisher · View at Google Scholar · View at Scopus
  46. M. Nielsen, C. Lundegaard, O. Lund, and T. N. Petersen, “CPHmodels-3.0-remote homology modeling using structure-guided sequence profiles,” Nucleic Acids Research, vol. 38, supplement 2, pp. W576–W581, 2010. View at Publisher · View at Google Scholar · View at Scopus
  47. Y. Wang, R. I. Sadreyev, and N. V. Grishin, “PROCAIN: protein profile comparison with assisting information,” Nucleic Acids Research, vol. 37, no. 11, pp. 3522–3530, 2009. View at Publisher · View at Google Scholar · View at Scopus
  48. C. Möbs, C. Slotosch, H. Löffler, T. Jakob, M. Hertl, and W. Pfützner, “Birch pollen immunotherapy leads to differential induction of regulatory T cells and delayed helper T cell immune deviation,” Journal of Immunology, vol. 184, no. 4, pp. 2194–2203, 2010. View at Publisher · View at Google Scholar · View at Scopus
  49. M. Bublin, M. Pfister, C. Radauer et al., “Component-resolved diagnosis of kiwifruit allergy with purified natural and recombinant kiwifruit allergens,” Journal of Allergy and Clinical Immunology, vol. 125, no. 3, pp. 687–694, 2010. View at Publisher · View at Google Scholar · View at Scopus
  50. M. Pifferi, G. Baldini, G. Marrazzini et al., “Benefits of immunotherapy with a standardized Dermatophagoides pteronyssinus extract in asthmatic children: a three-year prospective study,” Allergy, vol. 57, no. 9, pp. 785–790, 2002. View at Publisher · View at Google Scholar · View at Scopus