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Pollen-Food Allergy Syndrome: From Food Avoidance to Deciphering the Potential Cross-Reactivity between Pru p 3 and
Paula Álvarez1,2, Rocío Aguado1,2, Juan Molina1,2,3
1Department of Immunology and Allergy, Reina Sofía University Hospital, 14004 Córdoba, Spain.
Nutrients
|September 14, 2024
Summary
Cross-reactivity between olive (Ole e 7) and peach (Pru p 3) allergens can cause anaphylaxis. This study identified shared epitopes, suggesting structural similarities underlie this pollen-food syndrome.
Area of Science:
- Immunology
- Allergology
- Molecular Biology
Background:
- Nonspecific lipid transfer proteins (nsLTPs) like Ole e 7 (olive pollen) and Pru p 3 (peach) can cause cross-reactive anaphylaxis.
- This cross-reactivity contributes to pollen-food syndromes, necessitating detailed molecular investigation.
Purpose of the Study:
- To map specific IgE (sIgE)-binding epitopes of Ole e 7 and Pru p 3.
- To investigate the molecular basis of cross-reactivity between Ole e 7 and Pru p 3.
Main Methods:
- Epitope mapping using LC-MS on IgE-bound peptides from Ole e 7 and Pru p 3.
- Analysis of sera from patients monosensitized to Ole e 7, Pru p 3, or bisensitized.
Main Results:
- Previously described epitopes for Ole e 7 and Pru p 3 were confirmed.
- A specific Ole e 7 peptide (KSALALVGNKV) and a Pru p 3 peptide (ISASTNCATVK) were recognized by all patient groups.
- High local sequence identity (50-57%) was observed between cross-reactive peptide fragments, despite low overall sequence identity (32.6%).
Conclusions:
- Specific sIgE-binding epitopes for Ole e 7 were mapped, enabling improved diagnostic strategies.
- Structural homology and shared key residues, rather than significant sequence similarity, likely drive the cross-reactivity between Ole e 7 and Pru p 3 nsLTPs.
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