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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 #323539
Research Project: Reducing Peanut and Tree Nut Allergy

Location: Food Processing and Sensory Quality Research

Title: Identification of triosephosphate isomerase as a novel allergen in octopus fangsiao

Author
item YANG, YANG - Jimei University
item CHEN, ZHONG-WEI - Jimei University
item Hurlburt, Barry
item GUI-LING, LI - Jimei University
item YONG-XIA, ZHANG - Jimei University
item DAN-XIA, FEI - Jimei University
item HAI-WANG, SHEN - Jimei University
item MIN-JIE, CAO - Jimei University
item GUANG-MING, LIU - Jimei University

Submitted to: Molecular Immunology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 2/7/2017
Publication Date: 2/14/2017
Citation: Yang, Y., Chen, Z., Hurlburt, B.K., Gui-Ling, L., Yong-Xia, Z., Dan-Xia, F., Hai-Wang, S., Min-Jie, C., Guang-Ming, L. 2017. Identification of triosephosphate isomerase as a novel allergen in octopus fangsiao. Molecular Immunology. 85:35-46.

Interpretive Summary: Shellfish are one catagory of the "Big Eight" food allergies, however very little is known about the proteins that cause the allergic reactions. In this paper, a major allergen from octopus has been characterized. The allergen was identified in a previous study using sera from shellfish allergic patients. In this study the protein was purified and characterized for temperature and pH stability as well as digestibility. The gene was also cloned. Several epitopes that bind IgE antibodies were also determined.

Technical Abstract: A 28 kDa-protein was purified from octopus (Octopus fangsiao) and identified to be triosephosphate isomerase (TIM). The purified TIM is a glycoprotein with 1.7% carbohydrates and the isoelectric point is 7.6. TIM aggregated after heating above 45 °C, and the secondary structure was altered in extreme conditions (> 80°C, pH< 4.0) which affected the IgE-binding activity of natural TIM. TIM could be degraded into small fragments in the simulated gastric fluid digestion, but the digested fragments retained over 80% of the IgE-binding activity. The full length of octopus TIM (1140 bp, 247 amino acid residues) was cloned, which shares over 60% of sequence identity with the other four known TIM allergens. Furthermore, eight linear epitopes were predicted and one conformational epitope was identified by phage display technology. In summary, the study formed a valuable asset for its significance in allergy diagnosis of octopus-allergic disorders and cross-reactivity of TIM.