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

StudyJournal of agricultural and food chemistry· Aug 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 & ImmunologyStudyQ1IF 6.9

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 … Zhenxing Li

Journal of agricultural and food chemistry · Aug 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.

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Results

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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.

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Conclusion

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

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

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

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