4.7 Article

IgE-binding residues analysis of the house dust mite allergen Der p 23

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SCIENTIFIC REPORTS
卷 11, 期 1, 页码 -

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NATURE PORTFOLIO
DOI: 10.1038/s41598-020-79820-y

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  1. Ministry of Education Academic Research Fund
  2. National Medical Research Council
  3. Agency for Science, Technology and Research [R-154-000-404-112, R-154-000-553-112, R-154-000-565-112, R-154-000-630-112, R-154-000-A08-592, R-154-000-A27-597, NMRC/1150/2008, BMRC/01/1/21/18/077, BMRC/04/1/21/19/315, H17/01/a0/008]
  4. Biomedical Research Council, Singapore
  5. Universiti Kebangsaan Malaysia (UKM) [MI-2017-008]

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The study identified K44 and E46 residues as major IgE-binding residues of the Der p 23 allergen for HDM-sensitized individuals. Individuals sensitized only to HDM have a higher number of IgE-binding residues compared to polysensitized individuals. Those with allergic multimorbidity and moderate-to-severe allergic rhinitis also exhibit a higher number of IgE-binding residues.
House dust mites (HDMs) are one of the major causes of allergies in the world. The group 23 allergen, Der p 23, from Dermatophagoides pteronyssinus, is a major allergen amongst HDM-sensitized individuals. This study aims to determine the specific immunoglobulin E (sIgE) binding frequency and IgE-binding residues of recombinant Der p 23 (rDer p 23) allergen amongst a cohort of consecutive atopic individuals in a tropical region. We performed site-directed mutagenesis and carried out immuno-dot blot assays using 65 atopic sera. The immuno-dot blot assays results indicated that the two residues K44 and E46 which are located at the N-terminal region are the major IgE-binding residues. The rDerp-23 sIgE titers are strongly correlated to the number of IgE-binding residues for rDer p 23 (P < 0.001). Atopic individuals who were only sensitized to HDM have a significantly higher number of IgE-binding residues than the individuals who were polysensitized to HDM and other crude allergens (P < 0.05). Individuals with allergic multimorbidity and moderate-to-severe allergic rhinitis also have a higher number of IgE-binding residues compared to those with single allergic disease and mild allergic rhinitis. The results prompt us to hypothesize that the individuals who have a higher number of IgE-binding residues may face a bigger challenge to be treated through immunotherapy due to the complexity in designing an effective hypoallergen with a high number of IgE-binding residues. We propose that the development of a refined molecular diagnostic assay, which includes alanine substitution of surface-exposed residues could be a more precise diagnostic strategy to identify all the IgE-binding residues of a major allergen for an atopic individual and the development could be another new dimension in allergy diagnosis and allergen immunotherapy treatment.

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