Pollen-Food Allergy Syndrome: From Food Avoidance to Deciphering the Potential Cross-Reactivity between Pru p 3 and Ole e 7

Author:

Álvarez Paula12ORCID,Aguado Rocío12ORCID,Molina Juan123,Trujillo-Aguilera Antonio12,Villalba Mayte34,Díaz-Perales Araceli35ORCID,Oeo-Santos Carmen6,Chicano Eduardo27ORCID,Blanco Nadine12ORCID,Navas Ana123,Ruiz-León Berta123,Jurado Aurora123ORCID

Affiliation:

1. Department of Immunology and Allergy, Reina Sofía University Hospital, 14004 Córdoba, Spain

2. Maimonides Biomedical Research Institute of Córdoba (IMIBIC)/Reina Sofía University Hospital, University of Córdoba, 14004 Córdoba, Spain

3. Allergy Network ARADyAL, Instituto de Salud Carlos III, 28029 Madrid, Spain

4. Department of Biochemistry and Molecular Biology, Faculty of Chemical Sciences, Complutense University of Madrid, 28040 Madrid, Spain

5. Centre for Plant Biotechnology and Genomics (CBGP, UPM-INIA), Polytechnic University of Madrid, 28223 Madrid, Spain

6. Department of Physiology, Biochemistry and Human Genetics, Faculty of Health Science, Rey Juan Carlos University, 28922 Madrid, Spain

7. IMIBIC Mass Spectrometry and Molecular Imaging Unit (IMSMI), 14004 Córdoba, Spain

Abstract

Background: Cross-reactivity between nonspecific lipid transfer proteins could cause anaphylaxis, further influencing food avoidance and nutrient deficiencies. The one affecting olive pollen (Ole e 7) and peach (Pru p 3) may underlie a variety of pollen-food syndromes, though a deep molecular analysis is necessary. Methods: Three Ole e 7-monosensitised patients (MON_OLE), three Pru p 3-monosensitised patients (MON_PRU) and three bisensitised patients (BI) were selected. For epitope mapping, both digested proteins were incubated with patient sera, and the captured IgE-bound peptides were characterised by LC-MS. Results: The analysis revealed two Ole e 7 epitopes and the three Pru p 3 epitopes previously described. Interestingly, the “KSALALVGNKV” Ole e 7 peptide was recognised by MON_OLE, BI and MON_PRU patients. Conversely, all patients recognised the “ISASTNCATVK” Pru p 3 peptide. Although complete sequence alignment between both proteins revealed 32.6% identity, local alignment considering seven residue fragments showed 50 and 57% identity when comparing “ISASTNCATVK” with Ole e 7 and “KSALALVGNKV” with Pru p 3. Conclusions: This study mapped sIgE-Ole e 7-binding epitopes, paving the way for more precise diagnostic tools. Assuming non-significant sequence similarity, structural homology and shared key residues may underlie the potential cross-reactivity between Ole e 7 and Pru p 3 nsLTPs.

Funder

Fundación Progreso y Salud, Consejería de Salud, Junta de Andalucía

Spanish Society of Allergy and Clinical Immunology

Publisher

MDPI AG

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