In:
Food & Function, Royal Society of Chemistry (RSC), Vol. 12, No. 18 ( 2021), p. 8570-8582
Abstract:
Sarcoplasmic-calcium-binding protein (SCP) has been investigated as a novel allergen in Crassostrea angulata . Nevertheless, knowledge of its effector-cell-based allergic relevance and epitopes is limited. In this study, the heat-resistant allergen SCP was able to induce significant upregulation of CD63 and CD203c ( p 〈 0.05), which showed obvious allergenicity in a basophil activation test. Furthermore, immunoinformatic tools, a one-bead-one-compound peptide library, and phage display technology were combined to analyze the allergenic epitopes of SCP. Five linear epitopes named L-SCP-1 (AA 22–33 ), L-SCP-2 (AA 64–75 ), L-SCP-3 (AA 80–90 ), L-SCP-4 (AA 107–116 ), and L-SCP-5 (AA 144–159 ) were verified using serological tests. Additionally, two conformational epitopes (C-SCP-1 and C-SCP-2) were determined, and C-SCP-1 was located at one of the calcium-binding sites (AA 106–117 ). Moreover, SCP showed weaker typical α-helical features and higher hydrophobicity after Ca 2+ depletion, which reduced its IgE-binding capacity. Overall, these epitope data could enhance our understanding of oyster allergens, which could be used to develop hypoallergenic shellfish products.
Type of Medium:
Online Resource
ISSN:
2042-6496
,
2042-650X
Language:
English
Publisher:
Royal Society of Chemistry (RSC)
Publication Date:
2021
detail.hit.zdb_id:
2578152-2
SSG:
21
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