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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #341002
Research Project: Reducing Peanut and Tree Nut Allergy

Location: Food Processing and Sensory Quality Research

Title: Triosephosphate isomerase and filamin C share common epitopes as novel allergens of Procambarus clarkii

Author
item YANG, YANG - Jimei University
item ZHANG, YONG-XIA - Jimei University
item LIU, MENG - Jimei University
item Maleki, Soheila
item ZHANG, MING-LI - Xiamen University
item LIU, QUING-MEI - Jimei University
item CAO, MING-JIE - Jimei University
item SU, WEN-JIN - Jimei University
item LIU, GUANG-MING - Jimei University

Submitted to: Journal of Agricultural and Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 1/10/2017
Publication Date: 1/10/2017
Citation: Yang, Y., Zhang, Y., Liu, M., Maleki, S.J., Zhang, M., Liu, Q., Cao, M., Su, W., Liu, G. 2017. Triosephosphate isomerase and filamin C share common epitopes as novel allergens of Procambarus clarkii. Journal of Agricultural and Food Chemistry. 65:950-963.

Interpretive Summary: Triosephosphate isomerase (TIM) is a key enzyme in glycolysis and has been identified as an allergen in saltwater products. In this study, TIM with a molecular mass of 28 kDa was purified from the freshwater crayfish (Procambarus clarkii) muscle. A 90-kDa protein that shared Immunoglobulin G/Immunoglobulin E antibody binding activity with TIM was purified and identified as filamin C (FLN c), which is an actin-binding protein. TIM showed similar thermal and pH stability with better digestion resistance compared with FLN c. Antibody binding experiments measured the strength of anti-TIM polyclonal antibody (pAb) binding to both TIM and FLN c. Five linear and 3 conformational antibody binding sites of TIM, as well as 9 linear and 10 on conformational epitopes of FLN c, were identified. Antibody binding sites of TIM and FLN c demonstrated the sharing of certain amino acid residues in the two allergens accounts for the antibody binding to both.

Technical Abstract: Triosephosphate isomerase (TIM) is a key enzyme in glycolysis and has been identified as an allergen in saltwater products. In this study, TIM with a molecular mass of 28 kDa was purified from the freshwater crayfish (Procambarus clarkii) muscle. A 90-kDa protein that showed IgG/IgE cross-reactivity with TIM was purified and identified as filamin C (FLN c), which is an actin-binding protein. TIM showed similar thermal and pH stability with better digestion resistance compared with FLN c. The result of the surface plasmon resonance (SPR) experiment demonstrated the affinity of anti-TIM polyclonal antibody (pAb) to both TIM and FLN c. Five linear and 3 conformational epitopes of TIM, as well as 9 linear and 10 conformational epitopes of FLN c, were mapped by phage display. Epitopes of TIM and FLN c demonstrated the sharing of certain residues; the occurrence of common epitopes in the two allergens accounts for their cross-reactivity.