A single mouse monoclonal antibody, E58 modulates multiple IgE epitopes on group 1 cedar pollen allergens. (June 2016)

• Record Type: Journal Article
• Authors: Goldblum, Randall M.; Ning, Bo; Judy, Barbara M.; Holthauzen, Luis Marcelo F.; van Bavel, Julius; Kamijo, Atsushi; Midoro-Horiuti, Terumi
• Is Part Of: Molecular immunology. Volume 74(2016:Jun.)
• Page Start: 106
• Page End: 112
• Publication Date: 2016-06
• Subjects: Cry j 1 the major allergen of Japanese cedar (Cryptomeria japonica) -- Cup s 1 the major allergen of Italian cypress (Cupressus sempervirens) -- HRP horse radish peroxidase -- Jun a 1 the major allergen of mountain cedar (Juniperus ashei) -- pfam protein family; Allergen structure -- Cedar pollen allergy -- Conformational epitope -- IgE epitope -- Jun a 1 -- Monoclonal antibody; Immunochemistry -- Periodicals; Molecular biology -- Periodicals; Immunochemistry -- Periodicals; Allergy and Immunology -- Periodicals; Molecular Biology -- Periodicals; Immunochimie -- Périodiques; Biologie moléculaire -- Périodiques; Immunochemistry; Molecular biology; Periodicals; Electronic journals; 571.96
• DOI: 10.1016/j.molimm.2016.04.006
• Languages: English
• ISSNs: 0161-5890

Abstract

Highlights: We discovered a unique monoclonal antibody E58, which binds to the group 1 allergens of cedar pollens from three highly populated areas in the world. Upon binding to these allergens, E58 reduces the binding of patient's IgE antibodies to group 1 allergens of cedar pollen. The characteristic of E58 suggests a new opportunity to develop preventative or therapeutic molecules for cedar pollen hypersensitivity. Abstract: We recently described a dominant role for conformational epitopes on the group 1 allergen of the mountain cedar ( Juniperus ashei, Cupressaceae), Jun a 1, in pollen hypersensitivity in South Central U.S.A. Since these epitopes are surface exposed and are likely to be flexible, they may be susceptible to molecular or physical perturbations. This may make Jun a 1 a potential target for new forms of therapy for cedar pollinosis. Here, we describe a mouse monoclonal antibody, termed E58, which binds to the group 1 allergens of the cedar pollens from three highly populated regions of the world (central U.S.A., France and Japan). Upon binding to these allergens, E58 strongly reduces the binding of patient's IgE antibodies to these dominant allergens. This characteristic of E58, and potentially other similar antibodies, suggests an opportunity to develop preventative or therapeutic agents that may inhibit cedar pollen sensitization or prevent their allergic reactions.