Publication: Proteome, Allergenome, and Novel Allergens of House Dust Mite, Dermatophagoides farinae
Issued Date
2016-02-05
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ISSN
15353907
15353893
15353893
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2-s2.0-84957610659
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Mahidol University
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SCOPUS
Bibliographic Citation
Journal of Proteome Research. Vol.15, No.2 (2016), 422-430
Suggested Citation
Jintarat Choopong, Onrapak Reamtong, Nitat Sookrung, Watee Seesuay, Nitaya Indrawattana, Yuwaporn Sakolvaree, Wanpen Chaicumpa, Anchalee Tungtrongchitr Proteome, Allergenome, and Novel Allergens of House Dust Mite, Dermatophagoides farinae. Journal of Proteome Research. Vol.15, No.2 (2016), 422-430. doi:10.1021/acs.jproteome.5b00663 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/43026
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Title
Proteome, Allergenome, and Novel Allergens of House Dust Mite, Dermatophagoides farinae
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Abstract
© 2016 American Chemical Society. Dermatophagoides farinae mite is a predominant source of indoor allergens causing high incidence of allergy worldwide. People with different genetic background respond differently to the mite components, and thus the component-resolved diagnosis (CRD) is preferred to the conventional allergy test based on crude mite extract. In this study, proteome and culprit components in the D. farinae whole body extract that sensitized the allergic patients were studied by using SDS-PAGE (1DE) and 2DE-IgE immunoblotting followed by LC-MS/MS and database search for protein identification. From the 1DE, the mite extract revealed 105 proteins that could be classified into seven functionally different groups: allergens, structural components, enzymes, enzyme inhibitor, receptor proteins, transporters, and binding/regulatory/cell signaling proteins. From the 2DE, the mite extract produced 94 spots; 63 were bound by IgE in sera of 20 D. farinae allergic patients. One more protein that was not revealed by the 2DE and protein staining reacted with IgE in 2 allergic patients. Proteins in 40 spots could be identified as 35 different types. Three of them reacted to IgE of >50% of the allergic patients, and hence they are major allergens: tropomyosin or Der f 10 (75%), aconitate hydratase (70%), and one uncharacterized protein (55%). Aconitate hydratase is a novel D. farinae major allergen unraveled in this study. Several mite minor allergens that have never been previously reported are also identified. The data have clinical applications in the component-resolved diagnosis for tailor-designed allergen-specific immunotherapy.