Identification and Allergenicity Analysis of Tropomyosin: A Heat-Stable Allergen in .

, a prevalent aquatic delicacy, is known to elicit allergic reactions in certain individuals. Nevertheless, the investigation into its allergenic components has remained notably inadequate. In the research, an approximately 35 kDa heat-stable protein of raw/steamed extracts was verified as tropomyosin (TM) by LC-MS/MS.

A Crystal Structure of Pro c 2 Provides Insights into Cross-Reactivity of Aquatic Allergens from the Phosphagen Kinase Family.

Arginine kinase (AK) from the phosphagen kinase family is a cross-reactive shellfish allergen. Structurally related cross-reactive allergens are involved in the pathogenesis of allergic symptoms. This study aimed to unravel the cross-reactivity of AK from a structural perspective.

Optimized carbonylation treatment of Litopenaeus vannamei matrix decreased its immunoreactivity and improved edible quality, simultaneously.

The study aimed to investigate how carbonylation affects the immunoreactivity and edible quality of the Litopenaeus vannamei matrix. The carbonylation treatment conditions of the shrimp matrix were optimized. Firstly, the treatment condition is optimized with 1.

Effects of Glycosylation Combined with Phosphate Treatment on the Allergenicity and Structure of Tropomyosin in .

Tropomyosin (TM) is the main allergen in shrimp (). In this study, the effects of allergenicity and structure of TM by glycosylation (GOS-TM), phosphate treatment (SP-TM), and glycosylation combined with phosphate treatment (GOS-SP-TM) were investigated. Compared to GOS-TM and SP-TM, the IgG/IgE binding capacity of GOS-SP-TM was significantly decreased with 63.

Immunoglobulin E Epitope Mapping and Structure-Allergenicity Relationship Analysis of Crab Allergen Scy p 9.

Filamin C is an allergen of (Scy p 9), and six IgE linear epitopes of the allergenic predominant region had previously been validated. However, the IgE epitope and structure-allergenicity relationship of Scy p 9 are unclear. In this study, a hydrophobic bond was found to be an important factor of conformation maintaining.

IgE Epitope Analysis and Hypo-Immunoreactivity Derivative of Arginine Kinase in Mantis Shrimp ().

As the main allergenic food, shrimp can trigger allergic reactions in various degrees. In this study, arginine kinase (AK) was identified as an allergen in by LC-MS/MS. The open reading frame of AK was obtained, which included 356 amino acids, and recombinant AK (rAK) was expressed in .

Hypoallergenic derivatives of heat-stable allergens alleviated food allergy symptoms in Balb/c mice.

The design of hypoallergenic derivatives is a new strategy for allergen-specific immunotherapy. Although hypoallergenic derivatives of (mud crab) heat-stable tropomyosin (TM) and myosin light chain (MLC) have been preliminarily explored, their allergenicity needs to be further studied. In this work, recombinant allergens (wtTM, wtMLC) and hypoallergenic derivatives (mtTM, mtMLC) were purified.

IgE Epitope Analysis for Scy p 1 and Scy p 3, the Heat-Stable Myofibrillar Allergens in Mud Crab.

Tropomyosin (Scy p 1) and myosin light chain (Scy p 3) are investigated to be important heat-stable allergens in . However, the epitopes of Scy p 1 and Scy p 3 are limited. In this study, recombinant Scy p 1 and Scy p 3 had similar IgE-binding capacity to natural proteins.

Identification of linear epitopes and their major role in the immunoglobulin E-binding capacity of tropomyosin from .

Tropomyosin (TM) is an important allergen in molluscans. However, there was a lack of information about TM as an allergen in oysters. TM was purified and identified from (ATM), and its primary sequence was cloned and encoded with 284 amino acids (AAs).

Characterization, Epitope Identification, and Cross-reactivity Analysis of Tropomyosin: An Important Allergen of .

Oyster is a common shellfish product in China, which is associated with food allergy. However, there is still lack of research on allergens in oysters. In this study, tropomyosin (TM), an important allergen of , was purified and identified by mass spectrometry.

Crystal Structure Analysis and IgE Epitope Mapping of Allergic Predominant Region in Filamin C, Scy p 9.

Filamin C (FLN c) is a novel allergen in shellfish. In this study, FLN c from was divided into three regions for recombinant expression based on the number of domains and amino acids. Using dot blot and basophil activation tests, the allergic predominant region of FLN c was determined to be 336-531 amino acid positions (named FLN c-M).

Linear Epitopes Play an Important Role in the Immunoglobulin G (IgG)/Immunoglobulin E (IgE)-Binding Capacity of Scy p 4.

Sarcoplasmic calcium-binding protein is a stable allergen in and named Scy p 4. To explore the importance of linear epitopes in the immunoglobulin G (IgG)/immunoglobulin E (IgE)-binding capacity of Scy p 4, chemical denaturants were used to destroy the structure. Scy p 4 was reduced with dithiothreitol and subsequently alkylated with iodoacetamide (IAA).

IgE epitope analysis of sarcoplasmic-calcium-binding protein, a heat-resistant allergen in .

Sarcoplasmic-calcium-binding protein (SCP) has been investigated as a novel allergen in . Nevertheless, knowledge of its effector-cell-based allergic relevance and epitopes is limited. In this study, the heat-resistant allergen SCP was able to induce significant upregulation of CD63 and CD203c ( < 0.

Combination Processing Method Reduced IgE-Binding Activity of by Modifying Lysine, Arginine, and Cysteine on Multiple Allergen Epitopes.

Allergic reactions occur after the whole food is ingested, rather than the purified allergen. The present study explores the low-allergenic food processing for by analysis of macrostructure, digestibility, and immunoreactivity. Furthermore, the presence of modified amino acids on the reported IgE epitopes was analyzed by mass spectrometry.

Effects of thermal processing on the allergenicity, structure, and critical epitope amino acids of crab tropomyosin.

Food processing can change the structure and immunoreactivity of purified allergens, but the effect of food processing on the immunoreactivity of the processed and purified allergen is still poorly understood. In this study, tropomyosin (TM) was obtained from Scylla paramamosain and purified after different treatments. A basophil activation test was employed to detect the allergenicity of allergens.

Identification and Cross-reactivity Analysis of Sarcoplasmic-Calcium-Binding Protein: A Novel Allergen in .

Oysters are an important shellfish group known to cause food allergy; however, knowledge of their sensitization components and cross-reactivity is limited. This study aimed to identify a novel allergen in and investigate its cross-reactivity. To this end, a 20 kDa protein was purified from oyster and confirmed to be a sarcoplasmic-calcium-binding protein (SCP) by LC-MS/MS.

Cloning, expression and comparison of the properties of Scy p 9, a Scylla paramamosain allergen.

This study investigated the properties of Scy p 9 in mud crab (Scylla paramamosain). The gene sequence of filamin C obtained from crabs, which was denoted as Scy p 9, contains a 2544 bp open reading frame and encodes 848 amino acid residues. Recombinant Scy p 9 (rScy p 9) is expressed in Escherichia coli, which exhibits tertiary structure changes, and the IgE binding activity of rScy p 9 is higher than that of native Scy p 9 (nScy p 9).

Delayed in toilet training association with pediatric lower urinary tract dysfunction: A systematic review and meta-analysis.

Background: Globally, attitudes and practices towards toilet training have changed several decades ago and children are completing toilet training at a later age compared to previous generations. Concurrently, there has been an increase in the incidence of pediatric bladder bowel dysfunction (BBD), including lower urinary tract dysfunction (LUTD). Whether the fact of delayed toilet training may negatively impact the ability of children to obtain bladder and bowel control and cause LUT dysfunction remains controversial.

Crystal Structure Analysis and Conformational Epitope Mutation of Triosephosphate Isomerase, a Mud Crab Allergen.

The triosephosphate isomerase (TIM), Scy p 8, is a crab allergen and shows cross-reactivity in the shellfish. Here, recombinant Scy p 8 was expressed, and its crystal structure was determined at a resolution of 1.8 Å.

Cloning, Expression, and Epitope Identification of Myosin Light Chain 1: An Allergen in Mud Crab.

Mud crab () is a commonly consumed seafood as a result of its high nutritional value; however, it is associated with food allergy. The current understanding of crab allergens remains insufficient. In the present study, an 18 kDa protein was purified from crab muscle and confirmed to be myosin light chain 1 (MLC1) by matrix-assisted laser desorption/ionization-tandem time-of-flight mass spectrometry.

Effects of thermal processing on digestion stability and immunoreactivity of the Litopenaeus vannamei matrix.

Many types of shellfish, including shrimp, are sometimes cooked before ingestion. Hence, it is necessary to investigate how cooking (boiling, pressure treatment or none (raw)) affects the structure, digestibility and immunoreactivity of multi-component shrimp muscle. Protein extraction, simulated gastrointestinal digestion, immunoreactivity, immunoglobulin E (IgE)-mediated human mast cell degranulation, morphology, particle size and UV absorbance scanning were used to investigate changes in the shrimp muscle upon treatment.

[Influencing factors and mechanism of arsenic removal during the aluminum coagulation process].

Aluminum coagulants are widely used in arsenic (As) removal during the drinking water treatment process. Aluminium chloride (AlCl3) and polyaluminium chloride (PACl) which contains high content of Al13 were used as coagulants. The effects of aluminum species, pH, humic acid (HA) and coexisting anions on arsenic removal were investigated.

[Treatment of landfill leachate using sequential anaerobic/aerobic moving-bed biofilm reactor].

A sequential anaerobic-aerobic moving-bed biofilm reactor (MBBR) was employed to treat landfill leachate produced from disposal of municipal solid waste. The affecting operation conditions were investigated, and the affecting mechanism was also analyzed. The results showed that the HRT and organic loading rate (OLR) could greatly influence the treat efficiency.

[Correlations of blood lead levels in infant, in maternal blood and in breast milk].

Objective: To understand the correlation of blood lead levels in infant, in maternal blood and in breast milk as to providing evidence for prevention of potential infant hazard from lead.

Methods: Lead levels were measured by using graphite stove atom absorption spectrographic methods in maternal breast milk, maternal blood and infant blood in infants aged 0 to 11 months and their mothers between November and December 2002 in Xiamen City. Blood samples were collected from both mother and infant's fingertips.