Molecular Basis of Plant Profilins’ Cross-Reactivity

Author:

Terán María1,García-Ramírez Benjamín1ORCID,Mares-Mejía Israel1,Ortega Enrique2ORCID,O’Malley Andrea34,Chruszcz Maksymilian34ORCID,Rodríguez-Romero Adela1ORCID

Affiliation:

1. Instituto de Química, Universidad Nacional Autónoma de México, Mexico City 04510, Mexico

2. Instituto de Investigaciones Biomédicas, Universidad Nacional Autónoma de México, Circuito Exterior, Ciudad. Universitaria, Coyoacán, Mexico City 04510, Mexico

3. Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29209, USA

4. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824, USA

Abstract

Profilins are ubiquitous allergens with conserved structural elements. Exposure to profilins from different sources leads to IgE-cross-reactivity and the pollen–latex–food syndrome. Monoclonal antibodies (mAbs) that cross-react with plant profilins and block IgE-profilin interactions are relevant for diagnosis, epitope mapping, and specific immunotherapy. We generated IgGs mAbs, 1B4, and 2D10, against latex profilin (anti-rHev b 8) that inhibit the interaction of IgE and IgG4 antibodies from sera of latex- and maize-allergic patients by 90% and 40%, respectively. In this study, we evaluated 1B4 and 2D10 recognition towards different plant profilins, and mAbs recognition of rZea m 12 mutants by ELISAs. Interestingly, 2D10 highly recognized rArt v 4.0101 and rAmb a 8.0101, and to a lesser extent rBet v 2.0101, and rFra e 2.2, while 1B4 showed recognition for rPhl p 12.0101 and rAmb a 8.0101. We demonstrated that residue D130 at the α-helix 3 in profilins, which is part of the Hev b 8 IgE epitope, is essential for the 2D10 recognition. The structural analysis suggests that the profilins containing E130 (rPhl p 12.0101, rFra e 2.2, and rZea m 12.0105) show less binding with 2D10. The distribution of negative charges on the profilins’ surfaces at the α-helices 1 and 3 is relevant for the 2D10 recognition, and that may be relevant to explain profilins’ IgE cross-reactivity.

Funder

Consejo Nacional de Ciencia y Tecnología

DGAPA-UNAM

National Institute of Allergy and Infectious Diseases

Publisher

MDPI AG

Subject

Molecular Biology,Biochemistry

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