Reference | ||
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Reference Type | Literature | IEDB_Reference:1031214 |
Title | Triosephosphate Isomerase and Filamin C Share Common Epitopes as Novel Allergens of Procambarus clarkii. | |
Authors | Yang Yang; Yong-Xia Zhang; Meng Liu; Soheila J Maleki; Ming-Li Zhang; Qing-Mei Liu; Min-Jie Cao; Wen-Jin Su; Guang-Ming Liu | |
Affiliations | College of Food and Biological Engineering, Xiamen Key Laboratory of Marine Functional Food, Fujian Provincial Engineering Technology Research Center of Marine Functional Food, Fujian Collaborative Innovation Center for Exploitation and Utilization of Marine Biological Resources, Jimei University , Xiamen, Fujian 361021, China; Agricultural Research Service, Southern Regional Research Center, U. S. Department of Agriculture , New Orleans, Louisiana 70124, United States; Xiamen Second Hospital , Xiamen, Fujian 361021, China. | |
Journal | J Agric Food Chem | |
Year | 2017 | |
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 infinity 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. | |
Curation Last Updated | 2023-08-18 22:48:58 |
Epitope | ||
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Epitope ID | 591382 | IEDB_epitope:591382 |
Chemical Type | Linear peptide | |
Linear Sequence | NGDRAGIDSIISFMK | |
Source Molecule Name | triosephosphate isomerase | |
Source Organism | Procambarus clarkii (red swamp crayfish) | |
Starting Position | 16 | |
Ending Position | 30 |
Epitope Reference Details | ||
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Epitope Structure Defines | Epitope containing region/antigenic site | |
Epitope Name | TIM 16-30 peptide 1 | |
Location of Data in Reference | Table 5 |
Immunization | ||
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Host Organism | Oryctolagus cuniculus (rabbit) |
1st In Vivo Process | ||
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In Vivo Process Type | Administration in vivo |
1st Immunogen | ||
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Epitope Relation | Source Antigen | |
Chemical Type | Protein | |
Molecule Name | triosephosphate isomerase | |
Organism | Procambarus clarkii (red swamp crayfish) |
Immunization Comments | ||
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Immunization Comments | The details of the immunization procedure were not described. |
B Cell Assay | ||
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Qualitative Measurement | Positive | |
Method/Technique | inhibition by antigen | |
Measurement of | qualitative binding |
Assayed Antibody | ||
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Assayed Antibody Source Material | Serum | |
Assayed Antibody Immunoglobulin Domain | Entire Antibody | |
Assayed Antibody Purification Status | Polyclonal | |
Assayed Antibody Heavy Chain Type | IgG |
Antigen | ||
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Epitope Relation | Epitope | |
Chemical Type | Linear peptide | |
Linear Sequence | NGDRAGIDSIISFMK | |
Source Molecule Name | triosephosphate isomerase | |
Source Organism | Procambarus clarkii (red swamp crayfish) | |
Starting Position | 16 | |
Ending Position | 30 |
Assay Reference Details | ||
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Assay Comments by IEDB Curator | Rabbit antibody to triosephosphate isomerase (TIM) bound TIM as well as filamin C (FLN), and the epitope was able to inhibit this binding as seen by dot blot. Direct binding by dot blot was also demonstrated. | |
Location of Assay Data in Reference | Figure 6 |