The enzymatic cross-linking of an allergen by food processing may alter its sensitization potential. In this study, the IgE-binding activity and allergenicity cross-linked thermal polymerized arginine kinase (CL-pAK) were investigated.The stability CL-pAK analyzed immunological proteomics methods. potency to induce oral tolerance tested using in vivo assays a cell model. According results inhibition ELISA, half inhibitory concentration AK after changed from 1.13 228.36 μg/mL. vitro digestion...

<italic>Chlamys nobilis</italic>is a commercially important shellfish cultured bivalve in the South China Sea, which causes an IgE-mediated food allergy. However, studies on allergens its musculus are not comprehensive enough.

Oyster is a common food that causes allergy. However, little information available about its allergens and cross-reactivity. In this study, arginine kinase (AK) was identified as novel allergen in Crassostrea angulata. The primary sequence of AK cloned which encoded 350 amino acids, recombinant (rAK) obtained. immunodot results, secondary structure digestive stability showed native rAK had similar IgG/IgE-binding activity physicochemical properties. Serological analysis 14 oyster-sensitive...

Pro c 2 (arginine kinase) is a major allergen in crayfish (Procambarus clarkii). Shark-derived variable domains of new antigen receptors (VNARs) have advantages developing detection and immunotherapy. This study constructed VNAR domain library from Chiloscyllium plagiosum immunized with 2. Three VNARs (VNAR-11, VNAR-20, VNAR-29) against obtained by screening the were expressed HEK293F cells, fusing immunoglobulin (Ig) G1 Fc fragment (VNAR-Fc-11, VNAR-Fc-29, VNAR-Fc-20). The VNAR-Fc fusions...

Triosephosphate isomerase (TIM) is a key enzyme in glycolysis and has been identified as an allergen saltwater products. In this study, TIM with molecular mass of 28 kDa was purified from the freshwater crayfish (Procambarus clarkii) muscle. A 90-kDa protein that showed IgG/IgE cross-reactivity filamin C (FLN c), which actin-binding protein. similar thermal pH stability better digestion resistance compared FLN c. The result surface plasmon resonance (SPR) experiment demonstrated infinity...

Shellfish allergy is a prevalent, long-lasting disorder usually persisting throughout life. However, the allergen information incomprehensive in crab. This study aimed to identify novel crab, show its potential diagnosis and reduce allergenicity by food processing. A 21-kDa protein was purified from Scylla paramamosain confirmed as sarcoplasmic calcium binding (SCP) matrix-assisted laser desorption ionization-time-of-flight/time-of-flight mass spectrometry (MALDI-TOF/TOF-MS). Total RNA...

Mud crab (Scylla serrata), which is widely consumed, can cause severe allergic symptoms. Eight linear epitopes and seven conformational of tropomyosin (TM) from S. serrata were identified using phage display. The formed based on the coiled-coil structure TM. Most located in regions where primary structures conserved among crustacean Twelve synthetic peptides designed according to trypsin-cutting sites TM, them, three (including one epitope two epitopes) recognized by all patient sera...

Scylla paramamosain is one of the most common and serious food allergens in Asia. Therefore, research on its prevalence, accurate diagnosis, IgE-binding pattern crucial.To identify IgE epitopes myosinogen S. using phage peptide library.The prevalence allergy to crabs (AC) sensitization was analysed a questionnaire serological assay. BAT performed by flow cytometry, diagnostic performance evaluated relation purified from crab myosinogen. were identified display patients with AC. Sequence-...

Allergic reactions occur after the whole food is ingested, rather than purified allergen. The present study explores low-allergenic processing for Litopenaeus vannamei by analysis of macrostructure, digestibility, and immunoreactivity. Furthermore, presence modified amino acids on reported IgE epitopes was analyzed mass spectrometry. Results showed that combination Maillard reaction (shrimp meat with galactose) high temperature–pressure at 115 °C obviously changed macrostructure increased...

Food processing can change the structure and immunoreactivity of purified allergens, but effect food on processed allergen is still poorly understood.

The triosephosphate isomerase (TIM), Scy p 8, is a crab allergen and shows cross-reactivity in the shellfish. Here, recombinant 8 was expressed, its crystal structure determined at resolution of 1.8 Å. three-dimensional primarily composed (β/α)8-barrel motif prototype. Additionally, showed with high sequential secondary structural identity among TIMs from shellfish species. site-directed mutagenesis critical amino acids conformational epitopes carried out, mutants Trp 168 Lys 237 to Ala...

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 SCP was able to induce significant upregulation CD63 CD203c (p < 0.05), which showed obvious allergenicity basophil activation test. Furthermore, immunoinformatic tools, one-bead-one-compound peptide library, phage display technology were combined analyze...

Filamin C (FLN c) is a novel allergen in shellfish. In this study, FLN c from Scylla paramamosain was divided into three regions for recombinant expression based on the number of domains and amino acids. Using dot blot basophil activation tests, allergic predominant region determined to be 336-531 acid positions (named c-M). It confirmed that by X-ray diffraction, crystal structure c-M with immunoglobulin-like folding at resolution 1.7 Å obtained. The monomer barrel composed 16 β-strands 2...

The mud crab (Scylla paramamosain) is widely consumed but can cause a severe food allergic reaction. To reduce allergenicity to arginine kinase (AK), site-directed mutagenesis was used destroy disulfide bonds or mutate critical amino acids of conformational epitopes. Three hypoallergenic mutant AKs (mAK1, mAK2, and mAK3) were generated, with the immunoreactivity decreasing by 54.2, 40.1, 71.4%, respectively. In comparison recombinant AK (rAK), structure mAKs clearly changed. Additionally,...

Filamin C is an allergen of Scylla paramamosain (Scy p 9), and six IgE linear epitopes the allergenic predominant region had previously been validated. However, epitope structure-allergenicity relationship Scy 9 are unclear. In this study, a hydrophobic bond was found to be important factor conformation maintaining. The critical amino acids in predicted conformational were mutated, IgE-binding capacity surface hydrophobicity four mutants (E216A, T270A, Y699A, V704A) reduced compared 9. Ten...

This study investigated the properties of Scy p 9 in mud crab (<italic>Scylla paramamosain</italic>).

Arginine kinase (AK) was identified as an allergen in Crassostrea angulata. However, little information is available about its epitopes. In this study, AK from C. angulata registered to the World Health Organization/International Union of Immunological Societies nomenclature committee be named Cra a 2. The immunoglobulin G/immunoglobulin E-binding capacity 2 significantly reduced after chemical denaturation treatment. Further, eight linear mimotopes and five conformational were obtained...