Please use this identifier to cite or link to this item: https://doi.org/10.1038/s41598-018-21792-1
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dc.titleConformational IgE Epitope Mapping of der p 2 and the Evaluations of Two Candidate Hypoallergens for Immunotherapy
dc.contributor.authorReginald, K
dc.contributor.authorChew, F.T
dc.date.accessioned2020-10-20T09:55:34Z
dc.date.available2020-10-20T09:55:34Z
dc.date.issued2018
dc.identifier.citationReginald, K, Chew, F.T (2018). Conformational IgE Epitope Mapping of der p 2 and the Evaluations of Two Candidate Hypoallergens for Immunotherapy. Scientific Reports 8 (1) : 3391. ScholarBank@NUS Repository. https://doi.org/10.1038/s41598-018-21792-1
dc.identifier.issn2045-2322
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/178428
dc.description.abstractEpitope mapping of Der p 2, a clinically important dust-mite allergen is the first step in designing immunotherapy hypoallergen vaccine candidates. Twenty-one single alanine mutants of Der p 2 were generated and their secondary structure was analysed using circular dichroism spectra. Only one mutant, K96A resulted in a misfolded protein. All mutants were tested for serum IgE reactivity using serum from dust mite allergic individuals by immuno dot-blots. Mutations to five residues, N10, E25, K77, K96 and E102 consistently showed reduced IgE reactions compared to wild-Type Der p 2, and therefore these residues constitute the major IgE epitopes of Der p 2. Two mutants with consistent low IgE binding, K96A and E102A, were subsequently evaluated as hypoallergen candidates. IgG antibodies raised in mice against both mutants could inhibit human IgE-binding to WT Der p 2. Both mutants had intact T-cell epitopes as they were able to stimulate peripheral blood mononuclear cell proliferation similar to WT Der p 2. However, a switch in Th1:Th2 cytokine profile was not observed. In summary, we have identified the major conformational epitopes of Der p 2, and evaluated two Der p 2 hypoallergen vaccine candidates for immunotherapy. © 2018 The Author(s).
dc.publisherNature Publishing Group
dc.rightsAttribution 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.sourceUnpaywall 20201031
dc.subjectallergen
dc.subjectarthropod protein
dc.subjectcytokine
dc.subjectDermatophagoides pteronyssinus antigen p 2
dc.subjectepitope
dc.subjecthouse dust allergen
dc.subjectimmunoglobulin E
dc.subjectimmunoglobulin G
dc.subjectvaccine
dc.subjectanimal
dc.subjectBagg albino mouse
dc.subjectepitope mapping
dc.subjectfemale
dc.subjecthuman
dc.subjectimmunology
dc.subjectimmunotherapy
dc.subjectmononuclear cell
dc.subjectmouse
dc.subjectprocedures
dc.subjectT lymphocyte
dc.subjectAllergens
dc.subjectAnimals
dc.subjectAntigens, Dermatophagoides
dc.subjectArthropod Proteins
dc.subjectCytokines
dc.subjectEpitope Mapping
dc.subjectEpitopes
dc.subjectFemale
dc.subjectHumans
dc.subjectImmunoglobulin E
dc.subjectImmunoglobulin G
dc.subjectImmunotherapy
dc.subjectLeukocytes, Mononuclear
dc.subjectMice
dc.subjectMice, Inbred BALB C
dc.subjectT-Lymphocytes
dc.subjectVaccines
dc.typeArticle
dc.contributor.departmentBIOLOGY (NU)
dc.description.doi10.1038/s41598-018-21792-1
dc.description.sourcetitleScientific Reports
dc.description.volume8
dc.description.issue1
dc.description.page3391
dc.published.statepublished
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