A single mouse monoclonal antibody, E58 modulates multiple IgE epitopes on group 1 cedar pollen allergens

Randall M. Goldblum, Bo Ning, Barbara M. Judy, Luis Marcelo F. Holthauzen, Julius van Bavel, Atsushi Kamijo, Terumi Midoro-Horiuti

Research output: Contribution to journalArticle

2 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)106-112
Number of pages7
JournalMolecular Immunology
Volume74
DOIs
StatePublished - Jun 1 2016

Keywords

  • Allergen structure
  • Cedar pollen allergy
  • Conformational epitope
  • IgE epitope
  • Jun a 1
  • Monoclonal antibody

ASJC Scopus subject areas

  • Immunology
  • Molecular Biology

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