Influence of nonthermal extraction technique and allergenicity characteristics of tropomyosin from fish (Larimichthys crocea) in comparison with shrimp (Litopenaeus vannamei) and clam (Ruditapes philippinarum)

Xu, Lili; Lin, Hong; Li, Zhen Xing; Ahmed, Ifty; Pramod, Siddanakoppalu N.; Lin, Hang; Lv, Liang; Tian, Sheng Lan; Yu, Zhi Wen

doi:10.1016/j.foodchem.2019.125575

Cited by 20 publications

(17 citation statements)

References 31 publications

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“…Shrimps (Litopenaeus vannamei) were obtained from a local supermarket (Liqun supermarket, Qingdao, Shandong, China). Lit v 1 was purified from raw shrimp muscles as described . The anti-Lit v 1 IgG was obtained from Lit v 1-immunized mouse sera and purified by a Protein A Sepharose Column .…”

Section: Methodsmentioning

confidence: 99%

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Identification of the Dominant T-Cell Epitopes of Lit v 1 Shrimp Major Allergen and Their Functional Overlap with Known B-Cell Epitopes

Gasset

Lin

et al. 2021

J. Agric. Food Chem.

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Development of efficient peptide-based immunotherapy for shrimp allergy relies on the identification of the dominant T-cell epitopes of its major allergen, tropomyosin. In this study, immunoinformatic tools, T-cell proliferation, cytokine release, IgG/IgE binding, and degranulation assays were used to identify and characterize the T-cell epitopes in Lit v 1 in comparison with previously validated B-cell epitopes. The results showed that of the six in silico predicted T-cell epitopes only one (T2: VQESLLKANIQLVEK, 60–74) promoted T-cell proliferation, the release of IL-2, and upregulated secretion of Th2-associated cytokines in the absence of IgG/IgE binding and degranulation activities. These findings support T2 as a candidate for the development of an efficient peptide-based vaccine for the immunotherapy for shrimp-allergic patients.

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Section: Methodsmentioning

confidence: 99%

“…Lit v 1 was purified from raw shrimp muscles as described. 25 The anti-Lit v 1 IgG was obtained from Lit v 1-immunized mouse sera and purified by a Protein A Sepharose Column. 26 Goat anti-mouse IgG, goat anti-mouse IgE, and goat anti-human IgE antibodies were purchased from Zhongshan Jinqiao Co. (Beijing, China).…”

Section: ■ Introductionmentioning

confidence: 99%

Identification of the Dominant T-Cell Epitopes of Lit v 1 Shrimp Major Allergen and Their Functional Overlap with Known B-Cell Epitopes

Gasset

Lin

et al. 2021

J. Agric. Food Chem.

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“…Shrimp (L. vannamei) was obtained from a local supermarket (Liqun supermarket, Qingdao, Shandong, China), and raw muscles were used to obtain proteins based on our laboratory method. 12 Briefly, the minced muscle was homogenized in Buffer A (50 mM KCl containing 2 mM NaHCO 3 ). After the centrifugation, contents were washed by cold absolute.…”

Section: ■ Materials and Methodsmentioning

confidence: 99%

Natural Shrimp (Litopenaeus vannamei) Tropomyosin Shows Higher Allergic Properties than Recombinant Ones as Compared through SWATH-MS-Based Proteomics and Immunological Response

Zhang

et al. 2020

J. Agric. Food Chem.

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Tropomyosin (TM) is the major shrimp allergen that could trigger anaphylactic reactions. Recently, recombinant TM (rTM) has been accepted widely in the field of allergen-specific immunotherapy, but the allergenicity of rTM has not been compared with natural TM (nTM) based on an in vitro digestion profile. In this work, IgG-/IgE binding, allergen peptides, and degranulation ability of the digested samples in simulated gastric fluid/simulated intestinal fluid/gastrointestinal models from nTM and rTM were evaluated by immunoassays, proteomics, and basophil degranulation assay. Results showed that pepsin-digested and trypsin-digested samples of rTM exhibited lower IgG-/IgE binding and degranulation than those of nTM. More peptides of the digested samples from rTM (57.8%) matched shrimp allergic epitopes than those from nTM (33.3%). However, the peptide SITDELDQTF (269− 278) appeared most frequently. These findings would supply foundation data for epitope-based immunotherapy to shrimp allergic individuals.

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“…Furthermore, the cross‐reactivity among TMs might be due to similar epitopes within the eight epitopes in shrimp TM (Pen a 1), of which five are the same as cockroach TM (Per a 7), and four are the same as lobster TM (Hom a 1) and dust mite TM (Der p 10 and Der f 10; Hall & Liceaga, 2020; Tong et al., 2018). It was found that the cross‐reactivity was 97.6% for raw TM between shrimp ( L. vannamei ) and clam ( Ruditapes philippinarum; X. L. Li et al., 2020). Among seafood and other invertebrates, cross‐reactivity was also reported with 71% of mite‐allergic patients having a 55% chance of being allergic to shrimp TM (Matyushenko et al., 2020; Palmer et al., 2020).…”

Section: Tm: Molecular Characterization Epitopes and Cross‐reactivitymentioning

confidence: 99%

“…Certainly, its accuracy has been verified, and studies have shown that the accuracy of bioinformatics is over 90% when applied to obtain binding peptide chips for identifying epitopes biomarkers (C. Wang et al., 2020). To be specific, software or websites include DNAStar (DNAS‐TAR), AntheProt (Institute of Biology and Chemistry of Proteins, BepiPred 1.0 (http://www.cbs.dtu.dk/services/BepiPred/), Bioinformatics Predicted Antigenic Peptides system (http://immunax.dfci.harvard.edu/Tools/antigenic.html), ABCpred (http://www.imtech.res.in/raghava/abcpred/dataset.html), Immune Epitope Database Bank (IEDB) (http://www.immuneepitopes.org), and so on (X. L. Li et al., 2020).…”

Section: Tm: Molecular Characterization Epitopes and Cross‐reactivitymentioning

confidence: 99%

An overview of tropomyosin as an important seafood allergen: Structure, cross‐reactivity, epitopes, allergenicity, and processing modifications

Cheng

Wang

Sun

2021

Comp Rev Food Sci Food Safe

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Tropomyosin (TM) is a major allergen in crustaceans, which often causes allergy and is fatal to some consumers. Currently, the most effective treatment is to avoid ingesting TM, although most adverse events occur in accidental ingestion. In this review, the molecular characterization, epitopes, cross‐reactivity, and pathogenesis of TM are introduced and elucidated. Modification of TM by traditional processing methods such as heat treatment and enzymatic hydrolysis, and innovative processing technologies including high‐pressure treatment, cold plasma (CP), ultrasound, pulsed electric field (PEF), pulsed ultraviolet, microwave and irradiation are discussed in detail. Particularly, enzymolysis, PEF, and CP technologies show great potential for modifying TM and more studies are needed to verify their effectiveness for the seafood industry. Possible mechanisms and the advantages/disadvantages of these technologies for the mitigation of TM allergenicity are also highlighted. Further work should be conducted to investigate the allergenicity caused by protein segments such as epitopes, examine the interaction sites between the allergen and the processing techniques and reveal the reduction mechanism of allergenicity.

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Influence of nonthermal extraction technique and allergenicity characteristics of tropomyosin from fish (Larimichthys crocea) in comparison with shrimp (Litopenaeus vannamei) and clam (Ruditapes philippinarum)

Cited by 20 publications

References 31 publications

Identification of the Dominant T-Cell Epitopes of Lit v 1 Shrimp Major Allergen and Their Functional Overlap with Known B-Cell Epitopes

Identification of the Dominant T-Cell Epitopes of Lit v 1 Shrimp Major Allergen and Their Functional Overlap with Known B-Cell Epitopes

Natural Shrimp (Litopenaeus vannamei) Tropomyosin Shows Higher Allergic Properties than Recombinant Ones as Compared through SWATH-MS-Based Proteomics and Immunological Response

An overview of tropomyosin as an important seafood allergen: Structure, cross‐reactivity, epitopes, allergenicity, and processing modifications

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