Publication: Effect of amino acid polymorphisms of house dust mite der p 2 variants on allergic sensitization
Issued Date
2016
Resource Type
Language
eng
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Mahidol University
Rights Holder(s)
Korean Academy of Asthma
Bibliographic Citation
Allergy Asthma Immunol Res. Vol.8, No.1 (2016), 55-62
Suggested Citation
Sasipa Tanyaratsrisakul, Orathai Jirapongsananuruk, Bhakkawarat Kulwanich, Hales, Belinda J., Thomas, Wayne R., Surapon Piboonpocanun Effect of amino acid polymorphisms of house dust mite der p 2 variants on allergic sensitization. Allergy Asthma Immunol Res. Vol.8, No.1 (2016), 55-62. doi:10.4168/aair.2016.8.1.55 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/1837
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Title
Effect of amino acid polymorphisms of house dust mite der p 2 variants on allergic sensitization
Abstract
PURPOSE:
The sequence variations of the Der p 2 allergen of Dermatophagoides pteronyssinus diverge along 2 pathways with particular amino acid substitutions at positions 40,47,111, and 114. The environmental prevalence and IgE binding to Der p 2 variants differ among regions. To compare IgE binding to Der p 2 variants between sera from Bangkok, Thailand and Perth, Western Australia with different variants and to determine the variant-specificity of antibodies induced by vaccination with recombinant variants.
METHODS:
The structures of recombinant variants produced in yeast were compared by circular dichroism and 1-anilinonaphthalene 8-sulfonic acid staining of their lipid-binding cavity. Sera from subjects in Bangkok and Perth where different variants are found were compared by the affinity (IC₅₀) of IgE cross-reactivity to different variants and by direct IgE binding. Mice were immunized with the variants Der p 2.0101 and Der p 2.0110, and their IgG binding to Der p 2.0103, 2.0104, and 2.0109 was measured.
RESULTS:
The secondary structures of the recombinant variants resembled the natural allergen but with differences in ANS binding. The IC₅₀ of Der p 2.0101 required 7-fold higher concentrations to inhibit IgE binding to the high-IgE-binding Der p 2.0104 than for homologous inhibition in sera from Bangkok where it is absent, while in sera from Perth that have both variants the IC₅₀ was the same and low. Reciprocal results were obtained for Der p 2.0110 not found in Perth. Direct binding revealed that Der p 2.0104 was best for detecting IgE in both regions, followed by Der p 2.0101 with binding to other variants showing larger differences. Mouse anti-Der p 2.0101 antibodies had a high affinity of cross-reactivity but bound poorly to other variants.
CONCLUSIONS:
The affinity of IgE antibody cross-reactivity, the direct IgE binding, and the specificities of antibodies induced by vaccination show that measures of allergic sensitization and therapeutic strategies could be optimized with knowledge of Der p 2 variants.