Tropomyosin Contains IgE‐Binding Epitopes Sensitive to Periodate but Not to Enzymatic Deglycosylation

Ruan, Wei-Wei; Cao, Min‐Jie; Chen, Feng; Cai, Qiu-Feng; Su, Wen‐Jin; Wang, You-Zhao

doi:10.1111/1750-3841.12169

Cited by 8 publications

(7 citation statements)

References 29 publications

(39 reference statements)

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“…17,29,30 Our previous studies also showed that the digestion products of TM still maintained the ability of sensitization. 35,36,43,44 This was the reason that TM had the ability to activate an allergic reaction after gastrointestinal digestion. In a similar manner, the peptides of Ara h 1 retained both their ability to sensitize and to elicit an allergic reaction after digestion.…”

Section: ■ Discussionmentioning

confidence: 99%

Analysis of the Allergenic Epitopes of Tropomyosin from Mud Crab Using Phage Display and Site-Directed Mutagenesis

Mei

et al. 2018

J. Agric. Food Chem.

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Mud crab ( Scylla serrata), which is widely consumed, can cause severe allergic symptoms. Eight linear epitopes and seven conformational epitopes of tropomyosin (TM) from S. serrata were identified using phage display. The conformational epitopes were formed based on the coiled-coil structure of TM. Most of the epitopes were located in the regions where primary structures were conserved among crustacean TM. Twelve synthetic peptides were designed according to the epitopes and trypsin-cutting sites of TM, among them, three synthetic peptides (including one linear epitope and two conformational epitopes) were recognized by all of the patient sera using inhibitory dot blotting. A triple-variant (R90A-E164A-Y267A) was constructed based on the critical amino acids of the TM epitope. The IgE-binding activity of the triple-variant was significantly reduced compared with that of native TM. The results of phage display and site-directed mutagenesis offered new information regarding conformational epitopes of TM.

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Section: ■ Discussionmentioning

confidence: 99%

Analysis of the Allergenic Epitopes of Tropomyosin from Mud Crab Using Phage Display and Site-Directed Mutagenesis

Mei

et al. 2018

J. Agric. Food Chem.

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“…When combined with heating (90 • C), the maximum reduction of IgG-binding ability was 85.1%. However, Ruan et al (2013) added glycosidase to cleave the O-linked disaccharides, and they found that enzymatic deglycosylation with this kind of enzyme did not affect the IgE-binding activity of TM.…”

Section: Enzymolysismentioning

confidence: 99%

“…However, Ruan et al. (2013) added glycosidase to cleave the O‐linked disaccharides, and they found that enzymatic deglycosylation with this kind of enzyme did not affect the IgE‐binding activity of TM.…”

Section: Modification On Tmmentioning

confidence: 99%

“…Among them, thermal treatments have been shown to markedly increase the IgE reactivity of TM in crab ( Portunus pelagicus ; Abramovitch et al., 2013). Enzymatic deglycosylation of TM was found to be inefficient for altering the IgE‐binding ability to bind to IgE (Ruan et al., 2013). Chemical treatment (such as glycation) can result in undesirable physicochemical changes in seafood products (Gavahian & Khaneghah, 2020; Lv et al., 2021).…”

Section: Introductionmentioning

confidence: 99%

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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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“…This is particularly true for allergens with shared epitopes (i.e., glycosylation) [ 40 ]. This issue has raised concerns over whether the group 10 proteins are bona fide HDM allergens, as it is known that tropomyosin has IgE-reactive glycosylation sites [ 41 ]. Aki et al [ 28 ], who discovered Der f 10, noted that the IgE-binding of recombinant Der f 10 was 25× less than the IgE-binding of the native protein, which could indicate differences in glycosylation as proteins synthesized in E. coli lack such modifications.…”

Section: Discovery Phasementioning

confidence: 99%

Consideration of methods for identifying mite allergens

Cui

Wang

Jia

2018

Clin Transl Allergy

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House dust mites are small arthropods that produce proteins—found in their feces, body parts, and eggs—that are major triggers of human allergies worldwide. The goal of this review is to describe the current methods used to identify these allergens. A literature search for allergen identification methods employed between 1995 and 2016 revealed multiple techniques that can be broadly grouped into discovery and confirmation phases. The discovery phase employs screening for mite proteins that can bind IgEs in sera from animals or patients allergic to dust mites. The confirmation phase employs biochemical methods to isolate either native or recombinant mite proteins, confirms the IgE binding of the purified allergens, and uses either in vitro or in vivo assays to demonstrate that the purified antigen can stimulate an immune response. The methods used in the two phases are defined and their strengths and weaknesses are discussed. The majority of HDM-allergic patients may respond to just a small subset of proteins, but new protein discovery methods are still warranted in order to develop a complete panel of HDM allergens for component resolved diagnosis and patient-tailored therapies.

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Tropomyosin Contains IgE‐Binding Epitopes Sensitive to Periodate but Not to Enzymatic Deglycosylation

Cited by 8 publications

References 29 publications

Analysis of the Allergenic Epitopes of Tropomyosin from Mud Crab Using Phage Display and Site-Directed Mutagenesis

Analysis of the Allergenic Epitopes of Tropomyosin from Mud Crab Using Phage Display and Site-Directed Mutagenesis

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

Consideration of methods for identifying mite allergens

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