Mapping and characterization of antigenic epitopes of arginine kinase of Scylla paramamosain

Yang, Yang; Cao, Min‐Jie; Alcocer, Marcos; Liu, Qingmei; Fei, Dan-Xia; Mao, Haiyan

doi:10.1016/j.molimm.2015.02.010

Cited by 39 publications

(63 citation statements)

References 36 publications

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“…In AK-specific mimotopes, two peptides (NCSNSIPCAVKA and TLSLPGFTFVPT) were in the same linear epitope of S. paramamosain (amino acids 121-141 and 141-155) and in the same linear region of epitopes 4a and 4b (amino acids 121-141 and 142-159) of L. vannamei AK. 24,38 The conformational epitope was proved to be the predominant epitope type in AK in our previously research. 5 Using specific IgE from eight patients allergic to AK, a total of 36 mimotopes with eight conformational epitopes were obtained.…”

Section: Discussionmentioning

confidence: 74%

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A comprehensive analysis of the allergenicity and IgE epitopes of myosinogen allergens in Scylla paramamosain

Yang

Jin

et al. 2018

Clin Experimental Allergy

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Section: Discussionmentioning

confidence: 74%

“…Using specific IgE from eight patients allergic to AK, a total of 36 mimotopes with eight conformational epitopes were obtained. Epitopes 6 and 7 are the same as the IgG epitopes C‐AK‐3 and C‐AK‐4 reported by Yang et al …”

Section: Discussionmentioning

confidence: 79%

A comprehensive analysis of the allergenicity and IgE epitopes of myosinogen allergens in Scylla paramamosain

Yang

Jin

et al. 2018

Clin Experimental Allergy

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“…Tyrosinase is an oxidase, and acts mostly on tyrosyl residues leading to cross‐linking of proteins, polysaccharides, and proteins with polysaccharides . The epitopes of AK with IgE affinity were described previously . The amino acid residues of Y 134 , Y 145 , Y 211 , and Y323 in AK linear epitopes which reacted with tyrosine led to a reduction in IgE‐binding activity.…”

Section: Discussionmentioning

confidence: 99%

“…The destruction of a conformational epitope made decrease allergenicity. It was reported that AK contains six free cysteine thiols, and the intramolecular disulfide bond that forms between Cys201 and Cys271 is essential for the structural stability of AK . The reaction in the amino acid residues of Y 205 may affect the Cys201, resulting in low allergenicity.…”

Section: Discussionmentioning

confidence: 99%

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Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen

Fei

Liu

Chen

et al. 2016

Molecular Nutrition Food Res

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Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas

Zhao

Feng

et al. 2021

J Sci Food Agric

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BACKGROUND Molluscan shellfish, including oysters, often cause allergic reactions in sensitive people throughout the world. It has been demonstrated that arginine kinase (AK) is one of the major allergens of oyster. The present study aimed to evaluate the immunoreactivity and structure of oyster AK as affected by heat treatment, pH change, and in vitro digestion. What is more, the immunoglobulin E‐binding epitopes of this allergen were also predicted and validated. RESULTS Thermal and pH assays revealed that AK was unstable at temperature >40 °C or pH ≤5.0 by sodium dodecyl sulfate polyacrylamide gel electrophoresis and circular dichroism, and the digestibility assays suggested that AK was more easily digested by pepsin than by trypsin and chymotrypsin. The potential epitopes were predicted through immunoinformatics tools, and seven linear epitopes were identified by indirect competition enzyme‐linked immunosorbent assay with pooled sera and individual serum from oyster‐allergic patients. The critical amino acids in each epitope were also confirmed using mutant peptides. These linear epitopes and critical amino acids were apt to distribute on the outer surface of homology‐based AK model. Moreover, the three denaturants (sodium dodecyl sulfate, β‐mercaptoethanol, and urea) can destroy the spatial structure of AK and increase or reduce its allergenicity by denaturation treatments. CONCLUSION Processing conditions lay the foundation for the variation of allergenicity. Seven linear epitopes and their critical amino acids were identified by indirect competitive enzyme‐linked immunosorbent assay. These findings will be helpful in allergy diagnosis and development of hypoallergenic products in the near future. © 2021 Society of Chemical Industry.

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Mapping and characterization of antigenic epitopes of arginine kinase of Scylla paramamosain

Cited by 39 publications

References 36 publications

A comprehensive analysis of the allergenicity and IgE epitopes of myosinogen allergens in Scylla paramamosain

A comprehensive analysis of the allergenicity and IgE epitopes of myosinogen allergens in Scylla paramamosain

Assessment of the sensitizing capacity and allergenicity of enzymatic cross‐linked arginine kinase, the crab allergen

Physicochemical characterization and linear epitopes identification of arginine kinase allergen from Crassostrea gigas

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