Abstract
In most parts of the world, house dust is the most important elicitor of allergic reactions, and more than 50 % of all allergic patients are sensitized to house dust mites. Specific immunotherapy of house dust mite allergy is performed routinely with allergen extracts. Due to the bad quality of house dust mite extracts, this treatment is less efficient than immunotherapy with pollen extracts. Therefore, it would be beneficial to perform diagnosis and immunotherapy of house dust mite allergy with pure natural or recombinant house dust mite allergens. Although more than 30 allergens have already been identified in house dust mites and most of them were produced as recombinant proteins, so far only few house dust mite allergens are available for routine diagnosis. This chapter describes aspects of diagnosis and therapy with recombinant house dust mite allergens.
This contribution is based on a publication by the authors that appeared in the Allergo Journal in 2013 (Vrtala S, Kleine-Tebbe J: Hausstaubmilbenallergene und ihre Bedeutung. Allergo J 2013; 22(8):546–9) and which has now been updated, expanded, and translated into English as a chapter for this book.
The authors gratefully thank Prof. Wayne Thomas, PhD, Telethon Kids Institute, West Perth, Western Australia, Australia, for reviewing the manuscript, editorial assistance, and many helpful suggestions regarding this chapter.
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References
Aki T, Kodama T, Fujikawa A, et al. Immunochemical characterization of recombinant and native tropomyosins as a new allergen from the house dust mite, Dermatophagoides farinae. J Allergy Clin Immunol. 1995;96:74–83.
An S, Chen L, Long C, et al. Dermatophagoides farinae allergens diversity identification by proteomics. Mol Cell Proteomics. 2013a;12:1818–28.
An S, Shen C, Liu X, et al. Alpha-actinin is a new type of house dust mite allergen. PLoS One. 2013b;8:e81377.
Arlian LG, Morgan MS, Neal JS. Dust mite allergens: ecology and distribution. Curr Allergy Asthma Rep. 2002;2:401–11.
Asokananthan N, Graham PT, Stewart DJ, et al. House dust mite allergens induce proinflammatory cytokines from respiratory epithelial cells: the cysteine protease allergen, Der p 1, activates protease-activated receptor (PAR)-2 and inactivates PAR-1. J Immunol. 2002;169:4572–8.
Asturias JA, Arilla MC, Gomez-Bayon N, et al. Sequencing and high level expression in Escherichia coli of the tropomyosin allergen (Der p 10) from Dermatophagoides pteronyssinus. Biochim Biophys Acta. 1998;1397:27–30.
Asturias JA, Ibarrola I, Arilla MC, et al. Engineering of major house dust mite allergens Der p 1 and Der p 2 for allergen-specific immunotherapy. Clin Exp Allergy. 2009;39:1088–98.
Banerjee S, Weber M, Blatt K, et al. Conversion of Der p 23, a new major house dust mite allergen, into a hypoallergenic vaccine. J Immunol. 2014;192:4867–75.
Batard T, Baron-Bodo V, Martelet A, et al. Patterns of IgE sensitization in house dust mite-allergic patients: implications for allergen immunotherapy. Allergy. 2016;71:220–9.
Boulet LP, Turcotte H, Laprise C, et al. Comparative degree and type of sensitization to common indoor and outdoor allergens in subjects with allergic rhinitis and/or asthma. Clin Exp Allergy. 1997;27:52–9.
Bousquet J, Michel FB. Specific immunotherapy in asthma. Allergy Proc. 1994;15:329–33.
Brunetto B, Tinghino R, Braschi MC, et al. Characterization and comparison of commercially available mite extracts for in vivo diagnosis. Allergy. 2010;65:184–90.
Casas L, Sunyer J, Tischer C, et al. Early-life house dust mite allergens, childhood mite sensitization, and respiratory outcomes. Allergy. 2015;70:820–7.
Casset A, Mari A, Purohit A, et al. Varying allergen composition and content affects the in vivo allergenic activity of commercial Dermatophagoides pteronyssinus extracts. Int Arch Allergy Immunol. 2012;159:253–62.
Chan SL, Ong ST, Ong SY, et al. Nuclear magnetic resonance structure-based epitope mapping and modulation of dust mite group 13 allergen as a hypoallergen. J Immunol. 2006;176:4852–60.
Chan TF, Ji KM, Yim AK, et al. The draft genome, transcriptome, and microbiome of Dermatophagoides farinae reveal a broad spectrum of dust mite allergens. J Allergy Clin Immunol. 2015;135:539–48.
Chen KW, Fuchs G, Sonneck K, et al. Reduction of the in vivo allergenicity of Der p 2, the major house-dust mite allergen, by genetic engineering. Mol Immunol. 2008;45:2486–98.
Chua KY, Stewart GA, Thomas WR, et al. Sequence analysis of cDNA coding for a major house dust mite allergen, Der p 1. Homology with cysteine proteases. J Exp Med. 1988;167:175–82.
Chua KY, Cheong N, Kuo IC, et al. The Blomia tropicalis allergens. Protein Pept Lett. 2007;14:325–33.
Custovic A, Taggart SC, Francis HC, et al. Exposure to house dust mite allergens and the clinical activity of asthma. J Allergy Clin Immunol. 1996;98:64–72.
Derewenda U, Li J, Derewenda Z, et al. The crystal structure of a major dust mite allergen Der p 2, and its biological implications. J Mol Biol. 2002;318:189–97.
Epton MJ, Dilworth RJ, Smith W, et al. 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 peptide fragments Mag1 and Mag3. Int Arch Allergy Immunol. 1999;120:185–91.
Herman J, Thelen N, Smargiasso N, et al. Der p 1 is the primary activator of Der p 3, Der p 6 and Der p 9 the proteolytic allergens produced by the house dust mite Dermatophagoides pteronyssinus. Biochim Biophys Acta. 2014;1840:1117–24.
Huss K, Adkinson Jr NF, Eggleston PA, et al. House dust mite and cockroach exposure are strong risk factors for positive allergy skin test responses in the Childhood Asthma Management Program. J Allergy Clin Immunol. 2001;107:48–54.
Huss-Marp J, Gutermuth J, Schaffner I, et al. Comparison of molecular and extract-based allergy diagnostics with multiplex and singleplex analysis. Allergo J Int. 2015;24:46–53.
Inohara N, Nunez G. ML -- a conserved domain involved in innate immunity and lipid metabolism. Trends Biochem Sci. 2002;27:219–21.
King C, Simpson RJ, Moritz RL, et al. The isolation and characterization of a novel collagenolytic serine protease allergen (Der p 9) from the dust mite Dermatophagoides pteronyssinus. J Allergy Clin Immunol. 1996;98:739–47.
Maruo K, Akaike T, Ono T, et al. Generation of anaphylatoxins through proteolytic processing of C3 and C5 by house dust mite protease. J Allergy Clin Immunol. 1997;100:253–60.
Matricardi PM, Kleine-Tebbe J, Hoffmann HJ, et al. EAACI molecular allergology user’s guide. Pediatr Allergy Immunol. 2016;27(suppl23):1–250.
Mellerup MT, Hahn GW, Poulsen LK, et al. Safety of allergen-specific immunotherapy. Relation between dosage regimen, allergen extract, disease and systemic side-effects during induction treatment. Clin Exp Allergy. 2000;30:1423–9.
Mueller GA, Gosavi RA, Krahn JM, et al. Der p 5 crystal structure provides insight into the group 5 dust mite allergens. J Biol Chem. 2010a;285:25394–401.
Mueller GA, Edwards LL, Aloor JJ, et al. The structure of the dust mite allergen Der p 7 reveals similarities to innate immune proteins. J Allergy Clin Immunol. 2010b;125:909–17.
Niederberger V, Horak F, Vrtala S, et al. Vaccination with genetically engineered allergens prevents progression of allergic disease. Proc Natl Acad Sci U S A. 2004;101 Suppl 2:14677–82.
O’Neil SE, Heinrich TK, Hales BJ, et al. The chitinase allergens Der p 15 and Der p 18 from Dermatophagoides pteronyssinus. Clin Exp Allergy. 2006;36:831–9.
Pauli G, Larsen TH, Rak S, et al. Efficacy of recombinant birch pollen vaccine for the treatment of birch-allergic rhinoconjunctivitis. J Allergy Clin Immunol. 2008;122:951–60.
Platts-Mills TA, Rakes G, Heymann PW. The relevance of allergen exposure to the development of asthma in childhood. J Allergy Clin Immunol. 2000;105:S503–8.
Reese G, Ayuso R, Lehrer SB. Tropomyosin: an invertebrate pan-allergen. Int Arch Allergy Immunol. 1999;119:247–58.
Satinover SM, Reefer AJ, Pomes A, et al. Specific IgE and IgG antibody-binding patterns to recombinant cockroach allergens. J Allergy Clin Immunol. 2005;115:803–9.
Schmitz R, Ellert U, Kalcklosch M, et al. Patterns of sensitization to inhalant and food allergens - findings from the German Health Interview and Examination Survey for Children and Adolescents. Int Arch Allergy Immunol. 2013;162:263–70.
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.
Stewart GA, Ward LD, Simpson RJ, et al. The group III allergen from the house dust mite Dermatophagoides pteronyssinus is a trypsin-like enzyme. Immunology. 1992;75:29–35.
Sun G, Stacey MA, Schmidt M, et al. Interaction of mite allergens Der p3 and Der p9 with protease-activated receptor-2 expressed by lung epithelial cells. J Immunol. 2001;167:1014–21.
Sunyer J, Jarvis D, Pekkanen J, et al. Geographic variations in the effect of atopy on asthma in the European Community Respiratory Health Study. J Allergy Clin Immunol. 2004;114:1033–9.
Takai T, Yokota T, Yasue M, et al. Engineering of the major house dust mite allergen Der f 2 for allergen-specific immunotherapy. Nat Biotechnol. 1997;15:754–8.
Takai T, Mori A, Yuuki T, et al. Non-anaphylactic combination of partially deleted fragments of the major house dust mite allergen Der f 2 for allergen-specific immunotherapy. Mol Immunol. 1999;36:1055–65.
Takai T, Hatanaka H, Ichikawa S, et al. Effects of double mutation at two distant IgE-binding sites in the three-dimensional structure of the major house dust mite allergen Der f 2 on IgE-binding and histamine-releasing activity. Biosci Biotechnol Biochem. 2001;65:1601–9.
Thomas WR. Hierarchy and molecular properties of house dust mite allergens. Allergol Int Off J Japanese Soc Allergol. 2015;64:304–11.
Thomas WR, Smith WA, Hales BJ, et al. Characterization and immunobiology of house dust mite allergens. Int Arch Allergy Immunol. 2002;129:1–18.
Thomas WR, Hales BJ, Smith WA. Structural biology of allergens. Curr Allergy Asthma Rep. 2005;5:388–93.
Tovey ER, Chapman MD, Platts-Mills TA. Mite faeces are a major source of house dust allergens. Nature. 1981;289:592–3.
Trompette A, Divanovic S, Visintin A, et al. Allergenicity resulting from functional mimicry of a Toll-like receptor complex protein. Nature. 2009;457:585–8.
Tsai LC, Chao PL, Shen HD, et al. Isolation and characterization of a novel 98-kd Dermatophagoides farinae mite allergen. J Allergy Clin Immunol. 1998;102:295–303.
Van Hage-Hamsten M, Johansson SG, Hoglund S, et al. Storage mite allergy is common in a farming population. Clin Allergy. 1985;15:555–64.
Van Hage-Hamsten M, Johansson SG, Johansson E, et al. Lack of allergenic cross-reactivity between storage mites and Dermatophagoides pteronyssinus. Clin Allergy. 1987;17:23–31.
Voorhorst R, Spieksma-Boezeman MI, Spieksma FT. Is a mite (Dermatophagoides Sp.) the producer of the house-dust allergen? Allerg Asthma (Leipz). 1964;10:329–34.
Wahn U, Lau S, Bergmann R, et al. Indoor allergen exposure is a risk factor for sensitization during the first three years of life. J Allergy Clin Immunol. 1997;99:763–9.
Walton SF, Slender A, Pizutto S, et al. Analysis of IgE binding patterns to house dust mite allergens in scabies-endemic communities: insights for both diseases. Clin Exp Allergy. 2016;46:508.
Wan H, Winton HL, Soeller C, et al. Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions. J Clin Invest. 1999;104:123–33.
Weghofer M, Dall’antonia Y, Grote M, et al. Characterization of Der p 21, a new important allergen derived from the gut of house dust mites. Allergy. 2008a;63:758–67.
Weghofer M, Thomas WR, Kronqvist M, et al. Variability of IgE reactivity profiles among European mite allergic patients. Eur J Clin Invest. 2008b;38:959–65.
Weghofer M, Grote M, Resch Y, et al. Identification of Der p 23, a peritrophin-like protein, as a new major Dermatophagoides pteronyssinus allergen associated with the peritrophic matrix of mite fecal pellets. J Immunol. 2013;190:3059–67.
Wraith DG, Cunnington AM, Seymour WM. The role and allergenic importance of storage mites in house dust and other environments. Clin Allergy. 1979;9:545–61.
Yasueda H, Mita H, Akiyama K, et al. Allergens from Dermatophagoides mites with chymotryptic activity. Clin Exp Allergy. 1993;23:384–90.
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Vrtala, S., Kull, S., Kleine-Tebbe, J. (2017). Allergens, Diagnostics, and Therapeutic Aspects in House Dust Mite Allergy. In: Kleine-Tebbe, J., Jakob, T. (eds) Molecular Allergy Diagnostics. Springer, Cham. https://doi.org/10.1007/978-3-319-42499-6_22
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