Please use this identifier to cite or link to this item: https://doi.org/10.4049/jimmunol.181.4.2586
Title: Nuclear magnetic resonance structure and IgE epitopes of Blo t 5, a major dust mite allergen
Authors: Chan, Siew Leong 
Ong, Tan Ching 
Gao, Yun Feng 
Tiong, Yuen Sung
Wang, De Yun 
Chew, Fook Tim 
Mok, Yu Keung 
Keywords: Science & Technology
Life Sciences & Biomedicine
Immunology
GRASS-POLLEN ALLERGEN
BLOMIA-TROPICALIS
CRYSTAL-STRUCTURE
CROSS-REACTIVITY
IDENTIFICATION
DYNAMICS
FAUNA
SPECIFICITIES
SENSITIZATION
SENSITIVITY
Issue Date: 15-Aug-2008
Publisher: AMER ASSOC IMMUNOLOGISTS
Citation: Chan, 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
Abstract: A 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.
Source Title: JOURNAL OF IMMUNOLOGY
URI: https://scholarbank.nus.edu.sg/handle/10635/168653
ISSN: 00221767
15506606
DOI: 10.4049/jimmunol.181.4.2586
Appears in Collections:Staff Publications
Elements

Show full item record
Files in This Item:
File Description SizeFormatAccess SettingsVersion 
15248_1_merged_1211604265.pdfAccepted version2.02 MBAdobe PDF

OPEN

Post-printView/Download

SCOPUSTM   
Citations

39
checked on Sep 15, 2020

WEB OF SCIENCETM
Citations

41
checked on Sep 7, 2020

Page view(s)

38
checked on Sep 17, 2020

Download(s)

1
checked on Sep 17, 2020

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.