Structural and dynamical characteristics of tropomyosin epitopes as the major allergens in shrimp

Ozawa, Hideo; Umezawa, Koji; Takano, Mitsunori; Ishizaki, Shoichiro; Watabe, Shugo; Ochiai, Yoshihiro

doi:10.1016/j.bbrc.2018.02.172

Cited by 12 publications

(11 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This revealed that conformational epitopes of TM were also more likely to change with increased temperature, supporting the result of molecular dynamics simulation that the epitope region was more stable. 48 As shown in the results of ELISA, each crab-allergic patient's IgE binding capacity for TM corresponded with the results obtained using ImmunoCAP. For example, the serum from one crab-allergic patient (serum ID: 022) showed a higher OD 450 value than the other two crab-allergic patients, as well as higher specific IgE levels.…”

Section: ■ Discussionsupporting

confidence: 76%

See 1 more Smart Citation

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.

View full text Add to dashboard Cite

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.

show abstract

Section: ■ Discussionsupporting

confidence: 76%

“…When the temperature reached 55 °C, the α-helix of nTM was 89.7%, while mTM showed 57.2% reduction compared with it. This revealed that conformational epitopes of TM were also more likely to change with increased temperature, supporting the result of molecular dynamics simulation that the epitope region was more stable …”

Section: Discussionsupporting

confidence: 71%

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.

View full text Add to dashboard Cite

show abstract

“…However, recent studies described an allergenic risk that was related to the consumption of edible insects due to potential cross-reactivity with other arthropods, especially crustaceans [4][5][6]. Tropomyosin, arginine-kinase, but also other insect proteins, such as larval cuticle protein, myosin light, and heavy chain, as well as troponin, are potentially involved in allergenic reactions in cross-reactivity with other allergenic species (shrimp, prawn, and crab) [5,7,8]. Consequently, particularly for consumers with a food allergy to crustaceans, it is necessary to consider the risk of an allergic reaction after consuming edible insects.…”

Section: Introductionmentioning

confidence: 99%

High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis Affect Mealworm Allergenic Proteins

et al. 2020

View full text Add to dashboard Cite

Edible insects have garnered increased interest as alternative protein sources due to the world’s growing population. However, the allergenicity of specific insect proteins is a major concern for both industry and consumers. This preliminary study investigated the capacity of high hydrostatic pressure (HHP) coupled to enzymatic hydrolysis by Alcalase® or pepsin in order to improve the in vitro digestion of mealworm proteins, specifically allergenic proteins. Pressurization was applied as pretreatment before in vitro digestion or, simultaneously, during hydrolysis. The degree of hydrolysis was compared between the different treatments and a mass spectrometry-based proteomic method was used to determine the efficiency of allergenic protein hydrolysis. Only the Alcalase® hydrolysis under pressure improved the degree of hydrolysis of mealworm proteins. Moreover, the in vitro digestion of the main allergenic proteins was increased by pressurization conditions that were specifically coupled to pepsin hydrolysis. Consequently, HHP-assisted enzymatic hydrolysis represents an alternative strategy to conventional hydrolysis for generating a large amount of peptide originating from allergenic mealworm proteins, and for lowering their immunoreactivity, for food, nutraceutical, and pharmaceutical applications.

show abstract

“…An allergic reaction is caused by the binding of immunoglobulin E (IgE) to epitope regions of proteins, which should be resistant to digestion in the stomach. By MD simulations, the epitope regions of prawn tropomyosin were found to have higher α-helical contents and lower flexibility of dihedral angles, in other words, rigid and much less subject to unfolding and digestion, when compared to the non-epitope regions (Ozawa et al 2018).…”

Section: Allergenicitymentioning

confidence: 93%

“…RLC and ELC stand for the regulatory light chain and essential light chain, respectively. b Kuruma prawn Marsupenaeus japonicus tropomyosin (after 10 ns of molecular dynamics simulation using 1C1G as a template) (Ozawa et al 2018). c Japanese flying squid Todarodes pacificus actin (modeled structure based on rabbit actin ADP form, 1J6Z, Ochiai et al 2013).…”

Section: Molecular Structurementioning

confidence: 99%

Biochemical and physicochemical characteristics of the major muscle proteins from fish and shellfish

Ochiai

Ozawa

2020

Fish Sci

Self Cite

View full text Add to dashboard Cite

Fish and marine invertebrates constitute an important part of the human diet worldwide, and their muscles are the major edible parts. The muscles are a rich source of proteins, which in other terms determines the nutritional value and the quality of seafood products. Though the fish skeletal muscle proteins share many similarities with their mammalian counterparts, there exist great differences in their biological activity and structural stability. While the muscles of shellfish or aquatic invertebrates share many properties and general structural features with their vertebrate counterparts, they have unique characteristics. Therefore, understanding the biochemical and physicochemical properties of their major protein components is needed from the viewpoint of effective utilization of aquatic bioresources. Thus, in this review, we aimed to assemble the basis of such differences and also to understand the benefits of these proteins as the targets for studies on the structure–stability relationship of proteins.

show abstract

Structural and dynamical characteristics of tropomyosin epitopes as the major allergens in shrimp

Cited by 12 publications

References 44 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

High Hydrostatic Pressure-Assisted Enzymatic Hydrolysis Affect Mealworm Allergenic Proteins

Biochemical and physicochemical characteristics of the major muscle proteins from fish and shellfish

Contact Info

Product

Resources

About