Please use this identifier to cite or link to this item: https://doi.org/10.4049/jimmunol.181.4.2586
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dc.titleNuclear magnetic resonance structure and IgE epitopes of Blo t 5, a major dust mite allergen
dc.contributor.authorChan, Siew Leong
dc.contributor.authorOng, Tan Ching
dc.contributor.authorGao, Yun Feng
dc.contributor.authorTiong, Yuen Sung
dc.contributor.authorWang, De Yun
dc.contributor.authorChew, Fook Tim
dc.contributor.authorMok, Yu Keung
dc.date.accessioned2020-05-29T04:02:58Z
dc.date.available2020-05-29T04:02:58Z
dc.date.issued2008-08-15
dc.identifier.citationChan, Siew Leong, Ong, Tan Ching, Gao, Yun Feng, Tiong, Yuen Sung, Wang, De Yun, Chew, Fook Tim, Mok, Yu Keung (2008-08-15). Nuclear magnetic resonance structure and IgE epitopes of Blo t 5, a major dust mite allergen. JOURNAL OF IMMUNOLOGY 181 (4) : 2586-2596. ScholarBank@NUS Repository. https://doi.org/10.4049/jimmunol.181.4.2586
dc.identifier.issn00221767
dc.identifier.issn15506606
dc.identifier.urihttps://scholarbank.nus.edu.sg/handle/10635/168653
dc.description.abstractA high incidence of sensitization to Blomia tropicalis, the predominant house dust mite species in tropical regions, is strongly associated with allergic diseases in Singapore, Malaysia, and Brazil. IgE binding to the group 5 allergen, Blo t 5, is found to be the most prevalent among all B. tropicalis allergens. The NMR structure of Blo t 5 determined represents a novel helical bundle structure consisting of three antiparallel α-helices. Based on the structure and sequence alignment with other known group 5 dust mite allergens, surface-exposed charged residues have been identified for site-directed mutagenesis and IgE binding assays. Four charged residues, Glu76, Asp81, Glu86, and Glu91 at around the turn region connecting helices α2 and α3 have been identified to be involved in the IgE binding. Using overlapping peptides, we have confirmed that these charged residues are located on a major putative linear IgE epitope of Blo t 5 from residues 76-91 comprising the sequence ELKRTDLNILERFNYE. Triple and quadruple mutants have been generated and found to exhibit significantly lower IgE binding and reduced responses in skin prick tests. The mutants induced similar PBMC proliferation as the wild-type protein but with reduced Th2:Th1 cytokines ratio. Mass screening on a quadruple mutant showed a 40% reduction in IgE binding in 35 of 42 sera of atopic individuals. Findings in this study further stressed the importance of surface-charged residues on IgE binding and have implications in the cross-reactivity and use of Blo t 5 mutants as a hypoallergen for immunotherapy. Copyright © 2008 by The American Association of Immunologists, Inc.
dc.language.isoen
dc.publisherAMER ASSOC IMMUNOLOGISTS
dc.sourceElements
dc.subjectScience & Technology
dc.subjectLife Sciences & Biomedicine
dc.subjectImmunology
dc.subjectGRASS-POLLEN ALLERGEN
dc.subjectBLOMIA-TROPICALIS
dc.subjectCRYSTAL-STRUCTURE
dc.subjectCROSS-REACTIVITY
dc.subjectIDENTIFICATION
dc.subjectDYNAMICS
dc.subjectFAUNA
dc.subjectSPECIFICITIES
dc.subjectSENSITIZATION
dc.subjectSENSITIVITY
dc.typeArticle
dc.date.updated2020-05-28T08:22:58Z
dc.contributor.departmentDEPT OF BIOLOGICAL SCIENCES
dc.contributor.departmentDEPT OF OTOLARYNGOLOGY
dc.contributor.departmentMECHANOBIOLOGY INSTITUTE
dc.description.doi10.4049/jimmunol.181.4.2586
dc.description.sourcetitleJOURNAL OF IMMUNOLOGY
dc.description.volume181
dc.description.issue4
dc.description.page2586-2596
dc.description.codenJOIMA
dc.identifier.isiut000258345300038
dc.description.placeUnited States
dc.published.statePublished
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