Journal Mobile Options
Table of Contents
Vol. 129, No. 1, 2002
Issue release date: September 2002
Int Arch Allergy Immunol 2002;129:1–18
(DOI:10.1159/000065179)

Characterization and Immunobiology of House Dust Mite Allergens

Thomas W.R. · Smith W.-A. · Hales B.J. · Mills K.L. · O’Brien R.M.
aCentre for Child Health Research, University of Western Australia, Telethon Institute for Child Health Research, West Perth, W.A. and bDepartment of Medicine, University of Melbourne, Western General Hospital, Footscray, Vic., Australia

Individual Users: Register with Karger Login Information

Please create your User ID & Password





Contact Information











I have read the Karger Terms and Conditions and agree.

To view the fulltext, please log in

To view the pdf, please log in

Abstract

The examination of house dust mite extracts has indicated that over 30 different proteins can induce IgE antibody in patients allergic to the house dust mite. There are however dominant specificities especially the group 1 and 2 allergens which can account for much of the allergenicity of extracts. Of the 19 denominated allergens, the major IgE binding has been reported for the group 1, 2, 3, 9, 11, 14 and 15 allergens. The high-molecular-weight group 11, 14 and 15 allergens have only recently been described and although high IgE binding has been anticipated from immunoblotting, there is a need for considerable corroboration. Similarly, the study of the group 3 and 9 serine protease allergens has been incomplete. The group 4, 5, 7 and 8 allergens have shown intermediate IgE binding and the group 10 tropomyosins are of interest because of their potential cross-reactivity with allergen from disparate species. Although the progress with the production of recombinant group 1 allergens has been recent, many of the allergens can be produced as high IgE-binding polypeptides. The tertiary structure of the group 2 allergens has been determined from recombinant proteins and they are an excellent model for the investigation of modified allergens. An unexpected property of the group 1, 2 and 3 allergens has been the high degree of polymorphism found by cDNA analysis. It has however been possible to identify sequences to represent the variation in the natural allergens. The group 7 and 14 allergens show secondary modifications which vary in different extracts creating batch variation. While some estimate of the importance of allergens can be obtained from IgE binding, few analyses of T-cell responses have been made and these regulate both the development of, and the protection from sensitization.



Copyright / Drug Dosage

Copyright: All rights reserved. No part of this publication may be translated into other languages, reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording, microcopying, or by any information storage and retrieval system, without permission in writing from the publisher or, in the case of photocopying, direct payment of a specified fee to the Copyright Clearance Center.
Drug Dosage: The authors and the publisher have exerted every effort to ensure that drug selection and dosage set forth in this text are in accord with current recommendations and practice at the time of publication. However, in view of ongoing research, changes in goverment regulations, and the constant flow of information relating to drug therapy and drug reactions, the reader is urged to check the package insert for each drug for any changes in indications and dosage and for added warnings and precautions. This is particularly important when the recommended agent is a new and/or infrequently employed drug.
Disclaimer: The statements, opinions and data contained in this publication are solely those of the individual authors and contributors and not of the publishers and the editor(s). The appearance of advertisements or/and product references in the publication is not a warranty, endorsement, or approval of the products or services advertised or of their effectiveness, quality or safety. The publisher and the editor(s) disclaim responsibility for any injury to persons or property resulting from any ideas, methods, instructions or products referred to in the content or advertisements.

References

  1. Chapman MD, Platts-Mills TAE: Purification and characterization of the major allergen from Dermatophagoides pteronyssinus-antigen P1. J Immunol 1980;125:587–592.
  2. Lind P, Lowenstein H: Identification of allergens in Dermatophagoides pteronyssinus mite body extract by crossed radioimmunoelectrophoresis with two different rabbit antibody pools. Scand J Immunol 1983;17:263–273.
  3. Platts-Mills TAE, Chapman MD: Dust mites: Immunology, allergic disease and environmental control. J Allergy Clin Immunol 1987;80:755–775.
  4. Custovic A, Taggart SC, Francis HC, Chapman MD, Woodcock A: Exposure to house dust mite allergens and the clinical activity of asthma. J Allergy Clin Immunol 1996;98:64–72.
  5. Tovey ER, Chapman MD, Platts-Mills TAE: Mite faeces are a major source of house dust allergens. Nature 1981;289:592–593.
  6. Platts-Mills TAE, Thomas WR, Aalberse RC, Vervloet D, Chapman MD: Dust mite allergens and asthma: Report of a second international workshop. J Allergy Clin Immunol 1992;89:1046–1060.
  7. Ford AW, Rawle FC, Lind P, Spieksma FT, Lowenstein H, Platts-Mills TAE: Standardization of Dermatophagoides pteronyssinus: Assessment of potency and allergen content in ten coded extracts. Int Arch Allergy Appl Immunol 1985;76:58–67.

    External Resources

  8. Tovey ER, Baldo BA: Comparison by electroblotting of IgE-binding components in extracts of house dust mite bodies and spent mite culture. J Allergy Clin Immunol 1987;79:93–102.
  9. Baldo BA, Ford SA, Tovey ER: Toward a definition of the complete spectrum and rank order of importance of allergens from the house dust mite: Dermatophagoides pteronyssinus. Adv Biosci 1989;74:13–31.
  10. Krilis S, Baldo BA, Basten A: Antigens and allergens from the common house dust mite Dermatophagoides pteronyssinus. II. Identification of the major IgE-binding antigens by crossed radioimmunoelectrophoresis. J Allergy Clin Immunol 1984;74:142–146.
  11. Stewart GA, Thompson PJ, Simpson RJ: Protease antigens from house dust mite. Lancet 1989;ii:154–155.
  12. Shen HD, Chua KY, Lin KL, Hsieh KH, Thomas WR: Molecular cloning of a house dust mite allergen with common antibody-binding specificities with multiple components in mite extracts. Clin Exp Allergy 1993;23:934–940.
  13. Fujikawa A, Uchida K, Yanagidani A, et al: Altered antigenicity of M-177, a 177-kDa allergen from house dust mite Dermatophagoides farinae, in stored extracts. Clin Exp Allergy 1998;28:1549–1558.

    External Resources

  14. Breiteneder H, Pettenburger K, Bito A, et al: The gene coding for the major birch pollen allergen Bet v 1, is highly homologous to a pea disease resistance response gene. EMBO J 1989;8:1935–1938.
  15. Thomas WR, Chua KY, Stewart GA, et al: Analysis and expression of cDNA clones coding for house dust mite allergens. Adv Biosci 1989;74:139–147.
  16. Lind P: Purification and partial characterization of two major allergens from the house dust mite Dermatophagoides pteronyssinus. J Allergy Clin Immunol 1985;76:753–761.
  17. Van der Zee JS, van Swieten P, Jansen HM, Aalberse RC: Skin tests and histamine release with P1-depleted Dermatophagoides pteronyssinus body extracts and purified P1. J Allergy Clin Immunol 1988;81:884–895.
  18. Heymann PW, Chapman MD, Platts-Mills TAE: Antigen Der f I from the house dust mite Dermatophagoides farinae: In structural comparison with Der p I from Dermatophagoides pteronyssinus and epitope specificity of murine IgG and human IgE antibodies. J Immunol 1986;137:2841–2847.

    External Resources

  19. Lind P, Hansen OC, Horn N: The binding of mouse hybridoma and human IgE antibodies to the major fecal allergen, Der p I, of Dermatophagoides pteronyssinus. Relative binding site location and species specificity studied by solid-phase inhibition assays with radiolabeled antigen. J Immunol 1988;140:4256–4262.
  20. Ferrandiz R, Casas R, Dreborg S, Einarsson R, Bonachea I, Chapman M: Characterisation of allergenic components from house dust mite Dermatophagoides siboney. Purification of Der s 1 and Der s 2 allergens. Clin Exp Allergy 1995;25:922–928.

    External Resources

  21. Meyer CH, Bond JF, Chen MC, Kasaian MT: Comparison of the levels of the major allergens Der p I and Der p II in standardised extract of the house dust mite, Dermatophagoides pteronyssinus. Clin Exp Allergy 1994;24:1041–1048.

    External Resources

  22. Chapman MD, Heymann PW, Platts-Mills TAE: Epitope mapping of two major inhalant allergens, Der p I and Der f I, from mites of the genus Dermatophagoides. J Immunol 1987;139:1479–1484.
  23. Yaseuda H, Mia H, Yui Y, Shida T: Comparative analysis of physicochemical and immunochemical properties of the two major allergens from the Dermatophagoides pteronyssinus and the corresponding allergens from Dermatophagoides farinae. Int Arch Allergy Appl Immunol 1989;88:402–407.

    External Resources

  24. Lind P, Ingemann L, Brouvez M: Demonstration of species-specific sensitisation to major allergens of Dermatophagoides spp by solid-phase absorption of human IgE antibodies. Scand J Immunol 1987;25:1–10.

    External Resources

  25. O’Brien RM, Thomas WR: Immune reactivity to Der p I and Der p II in house dust mite-sensitive patients attending paediatric and adult allergy clinics. Clin Exp Allergy 1994;24:737–742.
  26. Shibasaki M, Isoyama S, Takita H: Influence of age on IgE responsiveness to Dermatophagoides farinae: An immunoblot study. Int Arch Allergy Immunol 1994;103:53–58.
  27. Van der Veen MJ, Jansen HM, Aalberse RC, van der Zee JS: Der p 1 and Der p 2 induce less severe late asthmatic responses than native Dermatophagoides pteronyssinus extract after a similar early asthmatic response. Clin Exp Allergy 2001;31:705–714.

    External Resources

  28. Mita H, Yasueda H, Akiyama K: Affinity of IgE antibody to antigen influences allergen-induced histamine release. Clin Exp Allergy 2000;30:1583–1589.

    External Resources

  29. Heymann PW, Chapman MD, Aalberse RC, Fox JW, Platts-Mills TAE: Antigenic and structural analysis of group II allergens (Der f II and Der p II) from house dust mites (Dermatophagoides spp). J Allergy Clin Immunol 1989;83:1055–1067.
  30. King C, Simpson RJ, Moritz RL, Reed GL, Thompson PJ, Stewart GA: The isolation and characterisation of a novel collagenolytic serine protease allergen (Der p 9) from the dust mite Dermatophagoides pteronyssinus. J Allergy Clin Immunol 1996;98:739–747.
  31. Yasueda H, Mita H, Shida T, Ando T, Sugiyama S, Yamakawa H: Allergens from Dermatophagoides with chymotryptic activity. Clin Exp Allergy 1993;23:384–390.

    External Resources

  32. Ando T, Homma R, Ino Y, et al: Trypsin-like protease of mites-purification and characterisation of trypsin-like protease from mite faecal extract Dermatophagoides farinae. Relationship between trypsin-like protease and Der f III. Clin Exp Allergy 1993;23:777–784.

    External Resources

  33. Ford SA, Tovey ER, Baldo BA: The spectrum of low molecular weight house dust mite (Dermatophagoides pteronyssinus) allergens with emphasis on Der p II. Clin Exp Allergy 1989;20:27–31.
  34. O’Neill GM, Baldo BA: Intra-species cross-reactivity of house dust mite allergens separated by protein blotting and detected by selective elution of mite components and IgE antibodies. Electrophoresis 1993;14:923–925.

    External Resources

  35. Lake FR, Ward LD, Simpson RJ, Thompson PJ, Stewart GA: House dust mite-derived amylase: Allergenicity and physicochemical characterization. J Allergy Clin Immunol 1991;87:1035–1042.

    External Resources

  36. Mills KL, Thomas WR, Smith W: Characterization of the group 4 allergens of the house dust mite. J Allergy Clin Immunol 2002;109:S180.
  37. Shen HD, Chua KY, Lin WL, Chen HL, Hsieh KH, Thomas WR: IgE and monoclonal antibody binding by the mite allergen Der p 7. Clin Exp Allergy 1996;26:308–315.

    External Resources

  38. Lynch NR, Thomas WR, Garcia NM, et al: Biological activity of recombinant Der p 2, Der p 5 and Der p 7 allergens of the house dust mite Dermatophagoides pteronyssinus. Int Arch Allergy Immunol 1997;114:68–73.
  39. Tovey ER, Johnson MC, Roche AL, Cobon GS, Baldo BA: Cloning and sequencing of a cDNA expressing a recombinant house dust mite protein that binds human IgE and corresponds to an important low molecular weight allergen. J Exp Med 1989;170:1457–1462.
  40. O’Neill G, Donovan GR, Baldo BA: Identification of a major allergen of the house dust mite, Dermatophagoides pteronyssinus, homologous with glutathione-S-transferase. Biochim Biophys Acta 1994;1219:521–524.
  41. Aki T, Kodama T, Fujikawa A, et al: Immunochemical characterisation of recombinant and native tropomyosins as a new allergen from the house dust mite, D. farinae. J Allergy Clin Immunol 1995;96:74–83.
  42. Van Ree R, Akkerdaas AL, Garritani AL, Aalberse RC, Bonifazi F: Possible induction of food allergy during anti-mite immunotherapy. Allergy 1996;51:108–113.
  43. Westritschnig K, Sibanda E, Thomas W, et al: Analysis of the allergen profile in Central Africa. Clin Exp Allergy 2002, in press.
  44. Tsai LC, Chao PL, Shen HD, et al: Isolation and characterisation of a novel 98-kDa Dermatophagoides farinae allergen. J Allergy Clin Immunol 1998;102:295–303.
  45. Tsai L, Sun Y, Chao P, et al: Sequence analysis and expression of a cDNA clone encoding a 98-kDa allergen in Dermatophagoides farinae. Clin Exp Allergy 1999;29:1583–1587.

    External Resources

  46. Lin KL, Wang SY, Hsieh KH: Analysis of house dust mite-specific IgE, IgG4, and IgG antibodies during immunotherapy in asthmatic children. Ann Allergy 1991;67:63–69.
  47. Nakanishi K, Shimokata K: Immunoblot analysis of Dermatophagoides farinae antigen. Ann Allergy 1990;64:219–231.

    External Resources

  48. Aki T, Ono K, Soon-Young P, et al: Cloning and characterization of cDNA coding for a new allergen from the house dust mite, Dermatophagoides farinae. Int Arch Allergy Immunol 1994;103:349–356.

    External Resources

  49. Fujikawa A, Ishimaru N, Seto A, et al: Cloning and characterisation of a new allergen Mag 3 from the house dust mite Dermatophagoides farinae: Cross-reactivity with high-molecular-weight allergen. Mol Immunol 1996;33:311–319.

    External Resources

  50. Malainual N: Human immune responses to house dust mite allergens; PhD thesis, University of Western Australia, Perth 2002.
  51. McCall C, Hunter S, Stedman K, et al: Characterization and cloning of a major high molecular weight house dust mite allergen (Der f 15) for dogs. Vet Immunol Immunopathol 2001;78:231–247.

    External Resources

  52. Tategaki A, Kawamoto S, Ski T, et al: Newly described house dust mite allergens. ACI Int 2000;suppl 1:74–76.
  53. Epton MJ, Smith W, Hales BJ, Hazell LA, Thompson PJ, Thomas WR: Non-allergenic antigen in allergic sensitisation: Responses to the mite ferritin heavy chain by allergic and non-allergic subjects. Clin Exp Allergy 2002, in press.
  54. Rawle FC, Mitchell EB, Platts-Mills TAE: T-cell response to the major allergen from the house dust mite, Dermatophagoides pteronyssinus, antigen P1: Comparison of patients with asthma, atopic dermatitis and perennial rhinitis. J Immunol 1984;133:195–201.
  55. O’Brien RM, Thomas WR, Wootton AM: T-cell responses to the purified major allergens from the house dust mite Dermatophagoides pteronyssinus. J Allergy Clin Immunol 1992;89:1021–1031.

    External Resources

  56. Cavaillon JM, Fitting C, Guinnepain MT, Rassemont R, David B: Lymphocyte proliferative responses to the purified Dermatophagoides farinae major allergen in untreated and hyposensitized atopic patients. Allergy 1988;43:146–151.
  57. Upham JW, Holt BJ, Baron-Hay MJ, et al: Allergen-specific T-cell reactivity is detectable in close to 100% of atopic and normal individuals: Covert responses are unmasked by serum-free medium. Clin Exp Allergy 1995;25:634–642.

    External Resources

  58. Hales BJ, Thomas WR: T-cell sensitisation to epitopes from the house dust mites Dermatophagoides pteronyssinus and Euroglyphus maynei. Clin Exp Allergy 1997;27:868–875.

    External Resources

  59. Hales BJ, Shen HD, Thomas WR: Cytokine responses to Der p 1 and Der p 7: House dust mite allergens with different IgE-binding activities. Clin Exp Allergy 2000;30:934–943.
  60. Hales BJ, Shen HD, Thomas WR: Cross-reactivity of T-cell responses to Dermatophagoides pteonyssinus and Dermatophagoides farinae. Studies with group 1 and 7 allergens. Clin Exp Allergy 2000;30:927–933.
  61. Byron KA, O’Brien RM, Varigos GA, Wootton AM: Dermatophagoides pteronyssinus II-induced interleukin-4 and interferon-γ expression by freshly isolated lymphocytes of atopic individuals. Clin Exp Allergy 1994;24:878–883.
  62. O’Brien RM, Byron KA, Varigos GA, Thomas WR: House dust mite immunotherapy results in a decrease in Der p 2-specific IFN-γ and IL-4 expression by circulating T lymphocytes. Clin Exp Allergy 1997;27:46–51.
  63. O’Hehir RE, Verhoef A, Panagiotopoulou E, et al: Analysis of human T-cell responses to the group II allergen of Dermatophagoides species: Localisation of major antigenic sites. J Allergy Clin Immunol 1993;92:105–113.

    External Resources

  64. O’Brien RM, Xu H, Rolland RM, Byron KA, Thomas WR: Allergen-specific production of interferon-γ by PBMC and CD8 T cells in allergic disease and following immunotherapy. Clin Exp Allergy 2000;30:333–341.
  65. Epton MJ, Hales BJ, Thompson PJ, Thomas WR: T-cell cytokine responses to outer membrane proteins of Haemophilus influenzae and the house dust mite allergens Der p 1 in allergic and non-allergic subjects. Clin Exp Allergy 2002, in press.
  66. Hales BJ, Hazell LA, Smith W, Thomas WR: Genetic variations of Der p 2 allergens: Effects on T-cell responses and IgE binding. Clin Exp Allergy 2002, in press.
  67. Tsitoura DC, Verhoef A, Gelder CM, O’Hehir RE, Lamb JR: Altered T-cell ligands derived from a major house dust mite allergen enhance IFN-γ but not IL-4 production by human CD4+ T cells. J Immunol 1996;157:2160–2165.

    External Resources

  68. Van Neerven RJJ, van de Pol MM, Wierenga EA, Aalberse RC, Jansen HM: Peptide specificity and HLA restriction do not dictate lymphokine production by allergen-specific T-lymphocyte clones. Immunology 1994;82:351–356.

    External Resources

  69. Van Neerven RJJ, van de Pol MM, van Milligen FJ, Jansen HM, Aalberse RC, Kapsenberg ML: Characterisation of cat dander-specific lymphocytes from atopic patients. J Immunol 1994;152:4203–4210.

    External Resources

  70. Chang JH, Chan H, Quirce S, et al: In vitro T-lymphocyte response and house dust mite bronchoconstriction. J Allergy Clin Immunol 1996;98:922–931.
  71. Till S, Dickason R, Huston D, et al: IL-5 secretion by allergen-stimulated CD4+ T cells in primary culture: Relationship to expression of allergic disease. J Allergy Clin Immunol 1997;99:563–569.
  72. Smart JM, Kemp AS: Increased Th1 and Th2 cytokine responses in children with allergic disease. Clin Exp Allergy 2002;32:796–802.
  73. Macaubas C, Sly PD, Burton P, et al: Regulation of T-helper cell responses to inhalant allergen during early childhood. Clin Exp Allergy 1999;29:1223–1231.
  74. Fujii S, Ono K, Shigeta S, Jyo T, Yamashita U: Human T cell responses to recombinant mite antigens of Dermatophagoides farinae. Clin Exp Immunol 1997;108:284–288.

    External Resources

  75. Epton MJ, Dilworth RJ, Smith W, Thomas WR: Sensitisation to the lipid-binding apolipophorin allergen Der p 14 and the peptide Mag-1. Int Arch Allergy Immunol 2001;124:57–60.
  76. Yasueda H, Mita H, Yui Y, Shida T: Isolation and characterization of two allergens from Dermatophagoides farinae. Int Arch Allergy Appl Immunol 1986;81:214–223.

    External Resources

  77. Thomas WR, Stewart GA, Simpson RJ, et al: Cloning and expression of DNA coding for the major house dust mite allergen Der p I in Escherichia coli. Int Arch Allergy Appl Immunol 1988;85:127–129.

    External Resources

  78. Chua KY, Stewart GA, Thomas WR, et al: Sequence analysis of cDNA coding for a major house dust mite allergen, Der p I. Homology with cysteine proteases. J Exp Med 1988;167:175–182.
  79. Dilworth RJ, Chua KY, Thomas WR: Sequence analysis of cDNA coding for a major house dust mite allergen, Der f I. Clin Exp Allergy 1991;21:25–32.
  80. Baker EN, Drenth J: The thiol proteases: Structure and mechanism. Biol Macromol Assembl 1987;3:313–368.
  81. Musil D, Zucic D, Turk D, et al: The refined 2.15 A X-ray crystal structure of human liver cathepsin B: The structural basis for its specificity. EMBO J 1991;10:2321–2330.
  82. Topham CM, Srinivasan N, Thorpe CJ, Overington H, Kalsheker NA: Comparative modelling of major house dust mite allergen Der p I: Structure validation using an extended environmental amino acid propensity table. Protein Eng 1994;7:869–894.

    External Resources

  83. Robinson C, Kalsheker NA, Srinivasan N, et al: On the potential significance of the enzymatic activity of mite allergens to immunogenicity. Clues to structure and function revealed by molecular characterisation. Clin Exp Allergy 1997;27:10–21.
  84. Greene WK, Chua KY, Stewart GA, Thomas WR: Antigenic analysis of group I house dust mite allergens using random fragments of Der p I expressed by recombinant DNA libraries. Int Arch Allergy Appl Immunol 1990;92:30–38.
  85. Kent NA, Hill MR, Keen JN, Holland PWH, Hart BJ: Molecular characterisation of group I allergen Eur m 1 from house dust mite Euroglyphus maynei. Int Arch Allergy Appl Immunol 1992;99:150–152.
  86. Smith W, Mills K, Hazell LA, Hart BJ, Thomas WR: Molecular analyses of the group 1 and 2 allergens from the house dust mite Euroglyphus maynei. Int Arch Allergy Immunol 1999;118:15–22.
  87. Higgins JE, Thorpe CJ, Hayball JD, Lamb JR, O’Hehir RE: Overlapping T-cell epitopes in the group I allergen of Dermatophagoides species restricted by HLA-DP and HLA-DR class II molecules. J Allergy Clin Immunol 1994;93:891–899.

    External Resources

  88. Kircher MF, Haeusler T, Nickel R, Lamb JR, Renz H, Beyer K: Vb 18.1 and Va 2.3+ T-cell subsets are associated with house dust mite allergy in human subjects. J Allergy Clin Immunol 2002;109:517–523.
  89. Chua KY, Kehal PK, Thomas WR: Sequence polymorphisms of cDNA clones encoding the mite allergen Der p I. Int Arch Allergy Immunol 1993;101:364–368.

    External Resources

  90. Stewart GA, Lake FR, Thompson PJ: Faecally derived hydrolytic enzymes from Dermatophagoides pteronyssinus: Physicochemical characterisation of potential allergens. Int Arch Allergy Appl Immunol 1991;95:248–256.

    External Resources

  91. Ando T, Ino Y, Haida M, et al: Isolation of cysteine protease in the crude extract Dermatophagoides farinae. Int Arch Allergy Appl Immunol 1991;96:199–205.
  92. Hewitt CRA, Horton H, Jones RM, Pritchard DI: Heterogeneous proteolytic specificity and activity of the house dust mite proteinase allergen Der p 1. Clin Exp Allergy 1997;27:201–207.

    External Resources

  93. Hewitt C, Brown A, Hart B, Prichard DI: A major house dust mite allergen disrupts the immunoglobulin network by selectively cleaving CD23: Innate protection by anti-proteases. J Exp Med 1995;182:1537–1544.
  94. Schulz O, Sutton BJ, Beavil RL, et al: Cleavage of the low-affinity receptor for human IgE (CD23) by a mite cysteine protease: Nature of the cleaved fragment in relation to the structure and function of CD23. Eur J Immunol 1997;27:584–588.

    External Resources

  95. Schulz O, Sewell HF, Shakib F: Proteolytic cleavage of CD25, the α subunit of the human T cell interleukin-2 receptor, by Der p 1, a major mite allergen with cysteine protease activity. J Exp Med 1998;187:271–275.
  96. Gough L, Schulz O, Sewell HF, Shakib F: The cysteine protease activity of the major dust mite allergen Der p 1 selectively enhances the immunoglobulin E antibody response. J Exp Med 1999;190:1897–1902.
  97. Gough L, Sewell HF, Shakib F: The proteolytic activity of the major dust mite allergen Der p 1 enhances the IgE antibody response to a bystander antigen. Clin Exp Allergy 2001;31:1594–1598.

    External Resources

  98. Ghaemmaghami AM, Robins A, Gough L, Sewell HF, Shakib F: Human T-cell subset commitment determined by the intrinsic property of antigen: The proteolytic activity of the major mite allergen Der p 1 conditions T cells to produce more IL-4 and less IFN-γ. Eur J Immunol 2001;31:1211–1216.
  99. Wan H, Winton HL, Soeller C, et al: Quantitative structural and biochemical analyses of tight junction dynamics following exposure of epithelial cells to house dust mite allergen Der p 1. Clin Exp Allergy 2000;30:685–698.

    External Resources

  100. King C, Brennan S, Thompson PJ, Stewart GA: Dust mite proteolytic allergens induce cytokine release from cultured airway epithelium. J Immunol 1998;161:3645–3651.
  101. Nuttall TJ, Pemberton AD, Lamb JR, Hill PB: Peripheral blood mononuclear cell responses to major and minor Dermatophagoides allergens in canine atopic dermatitis. Vet Immunol Immunopathol 2002;84:143–150.

    External Resources

  102. Masuda K, Tsujimoto H, Fujiwara S, et al: IgE sensitivity and cross-reactivity to crude and purified mite allergens (Der f 1, Der f 2, Der p 1, Der p 2) in atopic dogs sensitive to Dermatophagoides mite allergens. Vet Immunol Immunopathol 1999;72:303–313.

    External Resources

  103. Smith WA, Hales BJ, Jarnicki AG, Thomas WR: Allergens of wild house dust mites: Environmental Der p 1 and Der p 2 sequence polymorphisms. J Allergy Clin Immunol 2001;107:985–992.
  104. Jarnicki AG, Thomas WR: Stimulatory and inhibitory epitopes in T-cell responses of mice to Der p 1. Clin Exp Allergy 2002;32:942–950.
  105. Wahn U, Lau S, Bergmann R, et al: Indoor allergen exposure is a risk factor for sensitisation during the first three years of life. J Allergy Clin Immunol 1997;99:763–769.
  106. De Luca S, Sporick R, O’Meara TJ, Tovey ER: Mite allergen (Der p 1) is not only carried on mite feces. J Allergy Clin Immunol 1999;103:174–175.
  107. Lind P, Weeke B, Lowenstein H: A reference allergen preparation of the house dust mite D. pteronyssinus, produced from whole mite culture – A part of the DAS 76 study. Comparison with allergen preparations from other raw materials. Allergy 1984;39:259–274.
  108. Abe T, Ishii A: Comparison of Dermatophagoides pteronyssinus allergens from culture medium extract and whole body extract by using the same probe of pooled human serum. Allergy 1987;42:352–358.
  109. Chua KY, Doyle CR, Simpson RJ, Turner KJ, Stewart GA, Thomas WR: Isolation of cDNA coding for the major mite allergen Der p II by IgE plaque immunoassay. Int Arch Allergy Appl Immunol 1990;91:118–123.

    External Resources

  110. Yuuki T, Okumura Y, Ando T, et al: Cloning and sequencing of cDNAs corresponding to mite major allergen Der f II. Arerugi 1990;39:557–561.
  111. Trudinger M, Chua KY, Thomas WR: cDNA encoding the major mite allergen Der f II. Clin Exp Allergy 1991;21:33–37.

    External Resources

  112. Hakkaart GAJ, Aalberse RC, van Ree R: Lack of lysozyme activity of natural and yeast-derived recombinant Der p 2. Int Arch Allergy Immunol 1997;114:202–204.

    External Resources

  113. Mueller GA, Smith AM, Williams DC, et al: Expression and secondary structure determination by NMR methods of the major house dust mite allergen Der p 2. J Biol Chem 1997;272:26893–26898.
  114. Ichikawa S, Hatanaka H, Yuuki T, et al: Solution structure of Der f 2, the major mite allergen for atopic diseases. J Biol Chem 1998;273:356–360.
  115. Van Hage-Hamsten M, Olsson S, Emilson A, Härfast B, Svensson A, Scheynius A: Localisation of major allergens in the house dust mite Lepidoglyphus destructor with confocal laser scanning microscopy. Clin Exp Allergy 1995;25:536–542.
  116. Park GM, Lee SM, Lee IY, et al: Localization of a major allergen, Der p 2, in the gut and faecal pellets of Dermatophagoides pteronyssinus. Clin Exp Allergy 2000;30:1293–1297.

    External Resources

  117. Thomas WR, Chua KY: The major mite allergen Der p 2 – A secretion of the male mite reproductive tract. Clin Exp Allergy 1995;25:667–669.
  118. Kirchhoff C, Osterhoff C, Young L: Molecular cloning and characterisation of HE1, a major secretory protein of the human epididymis. Biol Reprod 1996;54:847–856.

    External Resources

  119. Frohlich O, Young LG: Molecular cloning and characterisation of EPI-1, the major protein in chimpanzee (Pan troglodytes) cauda epididymal fluid. Biol Reprod 1996;54:857–864.

    External Resources

  120. Nishiyama C, Yuuki T, Takai T, Okumura Y, Okudaira H: Determination of three disulfide bonds in a major house dust mite allergen, Der f II. Int Arch Allergy Immunol 1993;101:159–166.

    External Resources

  121. Larsen LB, Ravn P, Boisen A, Berglund L, Peterson TE: Primary structure of EPV20, a secretory glycoprotein containing a previously uncharacterised type of domain. Eur J Biochem 1997;243:437–441.

    External Resources

  122. Mészáros M, Morton DB: Identification of a developmentally regulated gene ers16, in the human tracheal epithelium of Manduca sexta, with homology to a protein from human epididymis. Insect Biochem Mol Biol 1996;26:7–11.
  123. Mészáros M, Morton DB: Comparison of the expression patterns of five developmentally regulated genes in Manduca sexta and their regulation by 20-hyroxyecdysone in vitro. J Exp Biol 1996;199:1555–1561.

    External Resources

  124. Naureckiene S, Sleat DE, Lackland H, et al: Identification of HE1 as the second gene of Niemann-Pick C disease. Identification of HE1 as the second gene of Niemann-Pick C disease 2000;290:2298–2301.
  125. Okamura N, Kiuchi S, Tamba M, et al: A porcine homolog of the major secretory protein of human epididymis, HE1, specifically binds cholesterol. Biochim Biophys Acta 1999;1438:377–387.
  126. Tovey ER, Ford SA, Baldo BA: Enhanced immunodetection of blotted house dust mite protein allergens on nitrocellulose following blocking with Tween-20. Electrophoresis 1989;10:243–249.

    External Resources

  127. Thomas WR, Chua KY, Smith WA: Molecular polymorphisms of house dust mite allergens. Exp Appl Acarol 1992;16:153–164.
  128. Yuuki T, Okumura Y, Okudairo H: Genomic organisation and polymorphism of the major house dust mite allergen Der f 2. Int Arch Allergy Immunol 1997;112:44–48.
  129. Nishiyama C, Yuuki T, Usui Y, Iwamoto N, Okumura Y, Okudaira H: Effects of amino acid variations in recombinant Der f II on its human IgE and mouse IgG recognition. Int Arch Allergy Immunol 1994;105:62–69.

    External Resources

  130. Chua KY, Huang CH, Shen HD, Thomas WR: Analysis of sequence polymorphisms of a mite allergen Der p 2. Clin Exp Allergy 1996;26:829–837.

    External Resources

  131. Mueller GA, Smith AM, Chapman MD, Rule G, Benjamin DC: Hydrogen exchange nuclear magnetic resonance spectroscopy mapping of antibody epitopes on the house dust mite allergen Der p 2. J Biol Chem 2001;276:9359–9365.
  132. Smith AM, Benjamin DC, Hozic NDU, et al: The molecular basis of antigenic cross-reactivity between the group 2 mite allergens. J Allergy Clin Immunol 2001;107:977–984.
  133. O’Brien RM, Thomas WR, Nicholson I, Lamb JR, Tait BD: An immunogenetic analysis of the T-cell recognition of the major house dust mite allergen Der p 2. Identification of high and low responder HLA-DQ alleles and localisation of T-cell epitopes. Immunology 1995;86:176–182.
  134. Varela J, Ventas P, Carreira J, Barbas JA, Gimenez-Gallego G, Polo F: Primary structure of Lep d I, the main Lepidoglyphus destructor allergen. Eur J Biochem 1994;225:93–98.
  135. Schmidt M, Olsson S, van der Ploeg I, van Hage-Hamsten M: cDNA analysis of the mite allergen Lep d 1 identifies two different isoallergens and variants. FEBS Lett 1995;370:11–14.

    External Resources

  136. Gafvelin G, Johansson E, Lundin A, et al: Cross-reactivity studies of a new group 2 allergen from the dust mite Glycophagus domesticus, Gly d 2, and group 2 allergens from Dermatophagoides pteronyssinus, Lepidoglyphus destructor and Tyrophagus putrescentiae with recombinant allergens. J Allergy Clin Immunol 2001;107:511–518.
  137. Johansson E, Schmidt M, Johansson SGO, Machado L, Olsson S, van Hage-Hamsten M: Allergenic cross-reactivity between Leptidoglyphus destructor and Blomia tropicalis. Clin Exp Allergy 1997;27:691–699.

    External Resources

  138. Yaseuda H, Saito A, Yanagihara Y, Akiyama K, Takaoka M: Species-specific measurement of the second group of Dermatophagoides mite allergens, Der p 2 and Der f 2, using a monoclonal antibody-based ELISA. Clin Exp Allergy 1996;26:171–177.

    External Resources

  139. Witteman AM, Voorneman R, van den Oudenrijn S, et al: Silverfish protein in house dust in relation to mite and total arthropod protein. Clin Exp Allergy 1996;26:1171–1176.

    External Resources

  140. Stewart GA, Ward LD, Simpson RJ, Thompson PJ: The group III allergen from the house dust mite Dermatophagoides pteronyssinus is a trypsin-like enzyme. Immunology 1992;75:29–35.
  141. Smith WA, Chua KY, Kuo MC, Rogers BL, Thomas WR: Cloning and sequencing of Dermatophagoides pteronyssinus group III allergen Der p III. Clin Exp Allergy 1994;24:220–228.
  142. Smith W, Thomas WR: Comparative analysis of the genes encoding the group 3 allergens for Dermatophagoides pteronyssinus and Dermatophagoides farinae. Int Arch Allergy Immunol 1996;109:133–140.

    External Resources

  143. Nishiyama C, Yasuhara T, Yuuki T, Okumura Y: Cloning and expression in Escherichia coli of cDNA encoding house dust mite allergen Der f 3, serine protease from Dermatophagoides farinae. FEBS Lett 1995;377:62–66.

    External Resources

  144. Greer J: Comparative model-building of the mammalian serine proteases. Mol Biol 1981;153:1027–1042.
  145. Jurasek L, Olafson RW, Johnson P, Smillie LB: Relationships between the structures and activities of some microbial serine proteases. I. Purification, enzymic properties and primary structures of Streptomyces griseus proteases A, B and trypsin; in Ribbons DW, Brew KD (eds): Proteolysis and Physiological Regulation. New York, Academic Press, 1976, pp 93–123.
  146. Ferrandiz R, Casas R, Dreborg S: Purification and IgE-binding capacity of Der s 3, a major allergen from Dermatophagoides siboney. Clin Exp Allergy 1997;27:700–704.

    External Resources

  147. Smith W, Thomas WR: Sequence polymorphisms of the Der p 3 house dust mite allergen. Clin Exp Allergy 1996;26:571–579.

    External Resources

  148. Maruo K, Akaike T, Ono T, Okamoto T, Maeda H: Generation of anaphylatoxins through proteolytic processing of C3 and C5 by house dust mite protease. J Allergy Clin Immunol 1997;100:253–260.
  149. Sun G, Stacey MA, Schmidt M, Mori L, Mattoli S: Interaction of mite allergens Der p 3 and Der p 9 with protease-activated receptor-2 expressed by lung epithelial cells. J Immunol 2001;167:1014–1021.

    External Resources

  150. Stewart GA, Kollinger MR, King CM, Thompson PJ: A comparative study of three serine proteases from Dermatophagoides pteronyssinus and Dermatophagoides farinae. Allergy 1994;49:553–560.
  151. Mills KLH, Lynch BJ, Thomas NR, Smith W: Molecular characterization of the group 4 house dust mite allergen from Dermatophagoides pteronyssinus and its amylase homologue from Euroglyphus maynei. Int Arch Allergy Immunol 1999;120:100–107.

    External Resources

  152. Lin KL, Chua KY, Thomas WR, Chiang BL, Hsieh KH: Characterisation of Der p V allergen. cDNA analysis and IgE-mediated reactivity to the recombinant protein. J Allergy Clin Immunol 1994;94:989–996.

    External Resources

  153. O’Neill GM, Donovan GR, Baldo BA: Sequence analyses of the native form of a major house dust mite allergen and its nascent polypeptide. Mol Immunol 1994;31:1447–1448.
  154. Arruda LK, Fernandez-Caldas E, Naspitz CK, Montealegre F, Chapman MD: Molecular cloning of Blomia tropicalis allergen Blo t 5 and its sequence homology to D. pteronyssinus Der p 5. J Allergy Clin Immunol 1994;93:205.
  155. Arruda LK, Vailes LD, Platts-Mills TAE, et al: Sensitisation to Blomia tropicalis in patients with asthma and identification of allergen Blo t 5. Am J Respir Crit Care Med 1997;155:343–350.
  156. Eriksson TL, Rasool O, Huecas S, et al: Cloning of three new allergens from the dust mite Lepidoglyphus destructor using phage surface display technology. Eur J Biochem 2001;268:287–294.

    External Resources

  157. Li CS, Hsu CW, Chua KY, Hsieh KH, Lin RH: Environmental distribution of house dust mite allergen Der p 5. J Allergy Clin Immunol 1996;97:857–859.
  158. Bennett BJ, Thomas WR: Cloning and sequencing of the group 6 allergen of Dermatophagoides pteronyssinus. Clin Exp Allergy 1996;26:1150–1154.

    External Resources

  159. Kawamoto S, Mizuguchi Y, Morimoto K, et al: Cloning and expression of Der f 6, a serine protease allergen from the house dust mite, Dermatophagoides farinae. Biochim Biophys Acta 1999;1454:201–207.
  160. Shen HD, Lin WL, Tsai LC, et al: Characterisation of the allergen Der f 7 from house dust mite extracts by species-specific and cross-reactive monoclonal antibodies. Clin Exp Allergy 1997;27:824–832.

    External Resources

  161. Shen HD, Chua KY, Lin NL, Hsieh KH, Thomas WR: Characterisation of the house dust mite allergen Der p 7 by monoclonal antibodies. Clin Exp Allergy 1995;25:416–422.
  162. Shen HD, Chua KY, Lin WL, Hsieh KH, Thomas WR: Molecular cloning and immunological characterisation of the house dust mite allergen Der f 7. Clin Exp Allergy 1995;25:1000–1006.

    External Resources

  163. Arruda LK, Vailes LD, Platts-Mills TAE, Hayden ML, Chapman MD: Induction of IgE antibody responses by glutathione-S-transferase from the German cockroach (Blattella germanica). J Biol Chem 1997;272:20907–20912.
  164. Asturias JA, Arrilla MC, Gomez-Bayon N, Martinez J, Martinez A, Palacios R: Sequencing and high level expression in E. coli of the tropomyosin allergen (Der p 10) from Dermatophagoides pteronyssinus. Biochim Biophys Acta 1998;1397:27–30.
  165. Ramos JD, Nge C, Wah LB, Yan CK: cDNA cloning and expression of Blo t 11, the Blomia tropicalis allergen homologous to paramyosin. Int Arch Allergy Immunol 2001;126:286–293.
  166. Puerta L, Caraballo L, Fernándas-Calda E, et al: Nucleotide sequence analysis of a complementary DNA coding for a Blomia tropicalis allergen. J Allergy Clin Immunol 1997;98:932–937.
  167. Caraballo L, Puerta L, Jiménez S, et al: Cloning and IgE binding of a recombinant allergen from the mite Blomia tropicalis, homologous with fatty acid-binding proteins. Int Arch Allergy Immunol 1997;112:341–347.
  168. Eriksson T, Whitley P, Johansson E, van Hage-Hamsten M, Gafvelin G: Identification and characterisation of two allergens from the dust mite Acarus siro, homologous with fatty acid-binding proteins. Int Arch Allergy Immunol 1999;119:275–281.
  169. Epton MJ, Dilworth RJ, Smith W, Hart BJ, Thomas WR: High-molecular-weight allergens of the house dust mite. An apolipophorin-like cDNA has sequence identity with the major M-177 allergen and the IgE-binding polypeptide fragments Mag 1 and Mag 3. Int Arch Allergy Immunol 1999;120:185–191.
  170. Epton MJ, Malainual N, Smith W, Thomas WR: Vitellogenin-apolipophorin like allergen Der p 14 is a major specificity in house dust mite sensitisation. J Allergy Clin Immunol 2001;107:S107.

    External Resources

  171. Greene WK, Cyster JG, Chua KY, O’Brien RM, Thomas WR: IgE and IgG binding of peptides expressed from fragments of cDNA encoding the major house dust mite allergen Der p I. J Immunol 1991;147:3768–3773.

    External Resources

  172. Greene WK, Thomas WR: IgE-binding structures of the major house dust mite allergen Der p I. Mol Immunol 1992;29:257–262.
  173. Chua KY, Kehal PK, Thomas WR, Vaughan PR, Macreadie IG: High-frequency binding of IgE to the Der p allergen expressed in yeast. J Allergy Clin Immunol 1992;89:95–102.
  174. Takahashi K, Takai T, Yasuhara T, Yokota T, Okumura Y: Effects of site-directed mutagenesis in the cysteine residues and the N-glycosylation motif in recombinant Der f 1 on secretion and protease activity. Int Arch Allergy Immunol 2001;124:454–460.
  175. Takahashi K, Takai T, Yasuhara T, et al: Production of enzymatically and immunologically active Der f 1 in Escherichia coli. Int Arch Allergy Immunol 2000;122:108–114.
  176. Best EA, Stedman KE, Bozic CM, et al: A recombinant group 1 house dust mite allergen, rDer f 1, with biological activities similar to those of the native allergen. Protein Express Purif 2000;20:462–471.

    External Resources

  177. Yasuhara T, Takai T, Yuuki T, Okudaira H, Okumura Y: Biologically active recombinant forms of a major house dust mite group 1 allergen Der f 1 with full activities of both cysteine protease and IgE binding. Clin Exp Allergy 2001;31:116–124.

    External Resources

  178. Shoji H, Horiuchi H, Takagi M: Production of recombinant Der f I (a major mite allergen) by Aspergillus oryzae. Biosci Biotechnol Biochem 1999;63:703–709.

    External Resources

  179. Jacquet A, Haumont M, Massaer M, et al: Biochemical and immunological characterization of a recombinant precursor form of the house dust mite allergen Der p 1 produced by Drosophila cells. Clin Exp Allergy 2000;30:677–684.

    External Resources

  180. Van Oort E, de Heer PG, van Leeuwen WA, et al: Maturation of Pichia pastoris-derived recombinant pro-Der p 1 induced by deglycosylation and by the natural cysteine protease Der p 1 from house dust mite. Eur J Biochem 2002;269:671–679.

    External Resources

  181. Chua KY, Greene WK, Kehal P, Thomas WR: IgE-binding studies with large peptides expressed from Der p II cDNA constructs. Clin Exp Allergy 1991;21:161–166.
  182. Tame A, Sakiyama Y, Kobayashi I, Terai I, Kobayashi K: Differences in the titres of IgE, IgG4 and other IgG subclass anti-Der p 2 antibodies measured with a recombinant allergen. Clin Exp Allergy 1996;26:43–49.
  183. Iwamoto N, Nishiyama C, Yasuhara T, et al: Direct expression of Der f 2, a major house dust mite allergen, in Escherichia coli. Int Arch Allergy Immunol 1996;109:356–361.
  184. Hakkaart GA, Harmsen MM, Chua KY, Thomas WR, Aalberse RC, van Ree R: Expression of the house dust mite allergen Der p 2 in the baker’s yeast Saccharomyces cerevisiae. Clin Exp Allergy 1998;28:45–52.
  185. Smith AM, Chapman MD: Reduction in IgE binding to allergen variants generated by site-directed mutagenesis: Contribution of disulfide bonds to the antigenic structure of the major house dust mite allergen Der p 2. Mol Immunol 1996;33:399–405.
  186. Hakkaart GA, Aalberse RC, van Ree R: Epitope mapping of the house-dust-mite allergen Der p 2 by means of site-directed mutagenesis. Allergy 1998;53:165–172.
  187. Smith AM, Chapman MD: Localization of antigenic sites on Der p 2 using oligonucleotide-directed mutagenesis targeted to predicted surface residues. Clin Exp Allergy 1997;27:593–599.

    External Resources

  188. Smith AM, Chapman MD, Taketomi EA, Platts-Mills TA, Sung SS: Recombinant allergens for immunotherapy: A Der p 2 variant with reduced IgE reactivity retains T-cell epitopes. J Allergy Clin Immunol 1998;101:423–425.
  189. Takai T, Ichikawa S, Yokota T, Hatanaka H, Inagaki F, Okumura Y: Unlocking the allergenic structure of the major house dust mite allergen Der f 2 by elimination of key intramolecular interactions. FEBS Lett 2000;484:102–107.
  190. Takai T, Yokota T, Yasue M, et al: Engineering of the major house dust mite allergen Der f 2 for allergen-specific immunotherapy. Nat Biotech 1997;1997:754–754.
  191. Takai T, Ichikawa S, Hatanaka H, Inagaki F, Okumura Y: Effects of proline mutations in the major house dust mite allergen Der f 2 on IgE-binding and histamine-releasing activity. Eur J Biochem 2000;267:6650–6656.

    External Resources

  192. Van’t Hof W, Driedijk PC, Van den Berg M, Beck-Sickinger AG, Jung G, Aalberse RC: Epitope mapping of the Dermatophagoides pteronyssinus house dust mite major allergen Der p II using overlapping synthetic peptides. Mol Immunol 1991;28:1225–1232.
  193. Takai T, Yuuki T, Okumura Y, Mori A, Okudaira H: Determination of the N- and C-terminal sequences required to bind human IgE of the major house dust mite allergen Der f 2 and epitope mapping for monoclonal antibodies. Mol Immunol 1997;34:255–261.

    External Resources

  194. Takai T, Mori A, Yuuki T, Okudaira H, Okumura Y: Non-anaphylactic combination of partially deleted fragments of the major house dust mite allergen Der f 2 for allergen-specific immunotherapy. Mol Immunol 1999;36:1055–1065.
  195. Smith W: Molecular analysis of the group 3 allergens from the Dermatophagoides pteronyssinus house dust mite; PhD thesis, University of Western Australia, Perth 1995.
  196. Liaw SH, Chen HZ, Kuo IC, Chua KY: Crystallization and preliminary X-ray diffraction analysis of group 5 mite allergen from Dermatophagoides pteronyssinus. J Struct Biol 1998;123:265–268.
  197. Monteiro BP, Lataro RC, Ferro JA, de Castro Reinach F: Functional α-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute for the amino-terminal acetyl group. J Biol Chem 1994;269:10461–10466.


Pay-per-View Options
Direct payment This item at the regular price: USD 38.00
Payment from account With a Karger Pay-per-View account (down payment USD 150) you profit from a special rate for this and other single items.
This item at the discounted price: USD 26.50