Please use this identifier to cite or link to this item: https://doi.org/10.1016/j.str.2007.10.022
Title: Roles of Structure and Structural Dynamics in the Antibody Recognition of the Allergen Proteins: An NMR Study on Blomia tropicalis Major Allergen
Authors: Naik, M.T.
Kung, C.C.-H.
Huang, T.-H.
Chang, C.-F.
Kuo, I.-C.
Yi, F.-C.
Chua, K.-Y. 
Keywords: MOLIMMUNO
PROTEINS
Issue Date: 2008
Source: Naik, M.T., Kung, C.C.-H., Huang, T.-H., Chang, C.-F., Kuo, I.-C., Yi, F.-C., Chua, K.-Y. (2008). Roles of Structure and Structural Dynamics in the Antibody Recognition of the Allergen Proteins: An NMR Study on Blomia tropicalis Major Allergen. Structure 16 (1) : 125-136. ScholarBank@NUS Repository. https://doi.org/10.1016/j.str.2007.10.022
Abstract: Blo t 5 is the major allergen from Blomia tropicalis mites and shows strong IgE reactivity with up to 90% of asthmatic and rhinitis patients' sera. The NMR solution structure of Blo t 5 comprises three long α helices, forming a coiled-coil, triple-helical bundle with a left-handed twist. TROSY-NMR experiments were used to study Blo t 5 interaction with the Fab′ of a specific monoclonal antibody, mAb 4A7. The mAb epitope comprises two closely spaced surfaces, I and II, connected by a sharp turn and bearing critical residues Asn46 and Lys47 on one surface, and Lys54 and Arg57 on the other. This discontinuous epitope overlaps with the human IgE epitope(s) of Blo t 5. Epitope surface II is further predicted to undergo conformational exchange in the millisecond to microsecond range. The results presented are critical for the design of a hypoallergenic Blo t 5 for efficacious immunotherapy of allergic diseases. © 2008 Elsevier Ltd. All rights reserved.
Source Title: Structure
URI: http://scholarbank.nus.edu.sg/handle/10635/25625
ISSN: 09692126
DOI: 10.1016/j.str.2007.10.022
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