Reference
Reference TypeLiterature
TitleTriosephosphate Isomerase and Filamin C Share Common Epitopes as Novel Allergens of Procambarus clarkii.
AuthorsYang Yang; Yong-Xia Zhang; Meng Liu; Soheila J Maleki; Ming-Li Zhang; Qing-Mei Liu; Min-Jie Cao; Wen-Jin Su; Guang-Ming Liu
AffiliationsCollege 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.
JournalJ Agric Food Chem
Year2017
AbstractTriosephosphate 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 Updated2023-08-18 22:48:58
Epitope
Epitope ID591382
Chemical TypeLinear peptide
Linear SequenceNGDRAGIDSIISFMK
Source Molecule Nametriosephosphate isomerase
Source OrganismProcambarus clarkii (red swamp crayfish)
Starting Position16
Ending Position30
Epitope Reference Details
Epitope Structure DefinesEpitope containing region/antigenic site
Epitope NameTIM 16-30 peptide 1
Location of Data in ReferenceTable 5
Immunization
Host OrganismOryctolagus cuniculus (rabbit)
1st In Vivo Process
In Vivo Process TypeAdministration in vivo
1st Immunogen
Epitope RelationSource Antigen
Chemical TypeProtein
Molecule Nametriosephosphate isomerase
OrganismProcambarus clarkii (red swamp crayfish)
Immunization Comments
Immunization CommentsThe details of the immunization procedure were not described.
B Cell Assay
Qualitative MeasurementPositive
Method/Techniqueinhibition by antigen
Measurement ofqualitative binding
Assayed Antibody
Assayed Antibody Source MaterialSerum
Assayed Antibody Immunoglobulin DomainEntire Antibody
Assayed Antibody Purification StatusPolyclonal
Assayed Antibody Heavy Chain TypeIgG
Antigen
Epitope RelationEpitope
Chemical TypeLinear peptide
Linear SequenceNGDRAGIDSIISFMK
Source Molecule Nametriosephosphate isomerase
Source OrganismProcambarus clarkii (red swamp crayfish)
Starting Position16
Ending Position30
Assay Reference Details
Assay Comments by IEDB CuratorRabbit 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 ReferenceFigure 6