A novel IgE-binding epitope of cat major allergen, Fel d 1

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 an...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2016-02, Vol.470 (3), p.593-598
Main Authors: Tasaniyananda, Natt, Tungtrongchitr, Anchalee, Seesuay, Watee, Sakolvaree, Yuwaporn, Indrawattana, Nitaya, Chaicumpa, Wanpen, Sookrung, Nitat
Format: Article
Language:English
Subjects:
Adolescent
Adult
Aged
Allergenic epitope
allergenicity
allergens
Allergens - chemistry
Allergens - immunology
Allergy
Amino Acid Sequence
Binding Sites
blood serum
Cat allergen
Cells, Cultured
Computer Simulation
cross reaction
epitopes
Epitopes, B-Lymphocyte - chemistry
Epitopes, B-Lymphocyte - immunology
Fel d 1
Female
Glycoproteins - chemistry
Glycoproteins - immunology
Humans
hypersensitivity
Hypersensitivity, Immediate - immunology
IgE blocking
immunoglobulin E
Immunoglobulin E - chemistry
Immunoglobulin E - immunology
immunotherapy
Male
mice
Models, Chemical
Molecular Docking Simulation
Molecular Sequence Data
monoclonal antibodies
patients
Protein Binding
Protein Conformation
Young Adult
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Summary: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. [Display omitted] •A novel B cell epitope of the cat major allergen, Fel d 1, was identified.•The epitope is conformational and IgE-binding or allergenic.•The epitope contains surface exposed residues of the Fel d 1 chain 1.•They are L34, T37, T39, P40, E42, E45, R61, K64, N65, D68, E73 and K76.•The epitope is useful for designing component resolved diagnosis/immunotherapy.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2016.01.099