Publication: A novel IgE-binding epitope of cat major allergen, Fel d 1
Issued Date
2016-02-12
Resource Type
ISSN
10902104
0006291X
0006291X
Other identifier(s)
2-s2.0-84957605254
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Mahidol University
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SCOPUS
Bibliographic Citation
Biochemical and Biophysical Research Communications. Vol.470, No.3 (2016), 593-598
Suggested Citation
Natt Tasaniyananda, Anchalee Tungtrongchitr, Watee Seesuay, Yuwaporn Sakolvaree, Nitaya Indrawattana, Wanpen Chaicumpa, Nitat Sookrung A novel IgE-binding epitope of cat major allergen, Fel d 1. Biochemical and Biophysical Research Communications. Vol.470, No.3 (2016), 593-598. doi:10.1016/j.bbrc.2016.01.099 Retrieved from: https://repository.li.mahidol.ac.th/handle/123456789/43095
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Title
A novel IgE-binding epitope of cat major allergen, Fel d 1
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Abstract
© 2016 Elsevier Inc. All rights reserved. Information on the antigenic repertoire, especially the IgE-binding epitopes of an allergen is important for understanding the allergen induced immune response and cross-reactivity, as well as for generating the hypoallergenic variants for specific component resolved immunotherapy/diagnosis (CRIT and CRD). Data on the IgE-binding epitopes of cat allergens are scarce. In this study, a novel IgE-binding epitope of the cat major allergen, Fel d 1, was identified. Mouse monoclonal antibody (MAb) specific to the Fel d 1 was produced. Computerized intermolecular docking was used for determining the residues of the Fel d 1 bound by the specific MAb. The presumptive surface exposed residues of the Fel d 1 intrigued by the MAb are located on the chain 1. They are: L34 and T37 (helix 1); T39 (between helices 1 and 2); P40, E42 and E45 (helix 2); R61, K64, N65 and D68 (helix 3); and E73 and K76 (helix 4). The MAb competed efficiently with the cat allergic patients' serum IgE for Fel d 1 binding in the competitive IgE binding assay, indicating allergenicity of the MAb epitope. The newly identified allergenic epitope of the Fel d 1 is useful in a design of the CRIT and CRD for cat allergy.