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New research · Allergy & Immunology
Journal of agricultural and food chemistry · 23h
StudyJournal of agricultural and food chemistry · 2026

Identification and Key Amino Acid Analysis of Epitopes of Pin y 2, a Novel Allergen from Pinus yunnanensis .

Yuhao Huang, Yunying Sun, Lirui Sun … Zhenxing Li
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Allergy & ImmunologyStudy

Specific amino acids are crucial for Pin y 2 allergen binding.

Identification and Key Amino Acid Analysis of Epitopes of Pin y 2, a Novel Allergen from Pinus yunnanensis .

Yuhao Huang et al. · Journal of agricultural and food chemistry · 2026
Background

Pine nut allergy is a global food safety concern, yet the epitope of the major allergen from Pinus yunnanensis Pin y 2 remains unknown.

Methods

We identified linear B-cell epitopes of Pin y 2 using five bioinformatics tools, followed by indirect ELISA with rabbit anti-Pin y 2 IgG and sera from pine nut-allergic patients.

more than 50%
Results
substituting these amino acids reduced antibody binding to the allergen by over half
More results

Four IgE epitopes and three IgG epitopes were validated.

All epitopes are surface-located and predominantly in negatively charged electrostatic regions.

Comparative epitope mapping with other tree nut vicilin allergens showed the positional conservation but sequence divergence of the Pin y 2 epitope.

“
Conclusion

These findings reveal the epitope map and epitope key residues of Pin y 2, which provides rational targets for hypoallergenic design and diagnostics.

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