Digestibility and Immunoreactivity of Shrimp Extracts Using an <i>In Vitro</i> Digestibility Model with Pepsin and Pancreatin

Toomer, Ondulla T.; Andrew, B.; Fu, Tong Jen; Williams, Kristina M.

doi:10.1111/1750-3841.12917

Cited by 17 publications

(9 citation statements)

References 16 publications

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“…Almost the same bands can be seen in all other extracts (except the high pressure steamed sample) although the intensities of the bands were reduced. Prominent protein bands in the extracts from processed samples include 200 kDa (myosin heavy chain), 100 kDa (α-actinin), a 75 kDa band, 42 kDa (arginine kinase), 36 kDa (tropomyosin) and 20 kDa (myosin light chain) (Liu, Huang, Cai, Weng, Su & Cao, 2011, Toomer, Do, Fu & Williams, 2015. In comparison with other bands however, the band intensities of tropomyosin and myosin light chain were enhanced (Fig 1).…”

Section: Sds-page Analysismentioning

confidence: 96%

Effects of buffer additives and thermal processing methods on the solubility of shrimp (Penaeus monodon) proteins and the immunoreactivity of its major allergen

Lasekan

Nayak

2016

Food Chemistry

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This study examines the potential of two buffer additives (Tween 20 and DTT) to improve the solubility of proteins from shrimp subjected to different heat treatments and the allergenicity of tropomyosin in the extracts. The concentration of soluble proteins extracted by all the buffers from processed shrimp was significantly reduced compared with untreated samples. The concentration of total soluble proteins from heat treated shrimp increased significantly when phosphate buffer containing both surfactant and reducing agent was used as the extraction buffer. However, the concentrations of heat-stable proteins in the buffers were mostly similar. The electrophoretic profile of extracted proteins showed that tropomyosin is very stable under the different heat treatment methods used in this study except for high pressure steaming where the intensity of tropomyosin band was reduced. Competitive inhibition ELISA showed that high pressure steaming reduced the allergenicity of tropomyosin compared with other heat treatments methods.

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Section: Sds-page Analysismentioning

confidence: 96%

Effects of buffer additives and thermal processing methods on the solubility of shrimp (Penaeus monodon) proteins and the immunoreactivity of its major allergen

Lasekan

Nayak

2016

Food Chemistry

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“…For example, peach lipid transfer protein, which is the main allergen in peach, is mainly hydrolyzed by trypsin and is resistant to pepsin and chymotrypsin; intact proteins and some high molecular weight peptides can be recognized by the patient's serum (Cavatorta et al, 2010). Toomer et al (2015) conducted a simulated gastric (0.8 U/μg pepsin; pH 2; 37 • C; 60 min), intestinal (32 U/μg pancreatin; pH 7.5; 37 • C; 60 min), and gastrointestinal digestion (60 min of gastric digestion and 30 min intestinal digestion) of total shrimp proteins, which found that only proteins that were stable to pepsin, trypsin, and chymosin simultaneously might trigger an immune response. Since both the stomach and intestine contain digestive enzymes that may hydrolyze allergens, it is also important to further study the changes in digestive characteristics and potential allergenicity of allergens during intestinal digestion.…”

Section: Duodenum Digestionmentioning

confidence: 99%

Gastrointestinal fate of food allergens and its relationship with allergenicity

Sun

Liu

et al. 2022

Comp Rev Food Sci Food Safe

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Food allergens are closely related to their gastrointestinal digestion fate, but the changes in food allergens during digestion and related mechanisms are quite complicated. This review presents in detail digestion models for predicting allergenicity, the fates of food allergens in oral, gastric and duodenal digestion, and the applications of digestomics in mapping IgE-binding epitopes of digestion-resistant peptides. Moreover, this review highlights the structure-activity relationships of food allergens during gastrointestinal digestion. Digestion-labile allergens may share common structural characteristics, such as high flexibility, rendering them easier to be hydrolyzed into small fragments with decreased or eliminated allergenicity. In contrast, the presence of disulfide bonds, tightly wound α-helical structures, or hydrophobic domains in food allergens helps them resist gastrointestinal digestion, stabilizing IgEbinding epitopes, thus maintaining their sensitization. In rare cases, digestion leads to increased allergenicity due to exposure of new epitopes. Finally, the action of the food matrix and processing on the digestion and allergenicity of food allergens as well as the underlying mechanisms was overviewed. The food matrix can directly act on the allergen by forming complexes or new epitopes to affect its gastrointestinal digestibility and thereby alter its allergenicity or indirectly affect the allergenicity by competing for enzymatic cleavage or influencing gastrointestinal pH and microbial flora. Several processing techniques attenuate the allergenicity of food proteins by altering their conformation to improve susceptibility to degradation by digestive enzymes. Given the complexity of food components, the food itself rather than a single allergen should be used to obtain more accurate data for allergenicity assessment.

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“…Tropomyosins are alpha-helical coiled-coil proteins that generally exist as a dimer, and show high heat stability and resistance to pepsin digestion. 9,10 Recent studies have demonstrated that structural and fold stability of allergenic proteins have a direct impact on their allergenicity through differential endolysosomal degradation and subsequent generation of allergen-derived peptides for MHC Class II presentation on antigen presenting cells, as shown in the case of Bet v 1, a major birch pollen allergen. 11 Whether structural differences influence allergenicity and cross-reactivity of the various tropomyosins, remains unclear.…”

Section: Introductionmentioning

confidence: 99%

Effect of structural stability on endolysosomal degradation and T-cell reactivity of major shrimp allergen tropomyosin

Kamath

Scheiblhofer

Johnson

et al. 2020

Preprint

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Background: Tropomyosins are highly conserved proteins, an attribute that forms the molecular basis for their IgE antibody cross-reactivity. Despite structural similarities, their allergenicity varies greatly between ingested and inhaled invertebrate sources. In this study, we investigated the relationship between the structural stability of different tropomyosins, their endolysosomal degradation patterns and T-cell reactivity. Methods:We investigated the differences between four tropomyosins -the major shrimp allergen Pen m 1 and the minor allergens Der p 10 (dust mite), Bla g 7 (cockroach) and Ani s 3 (fish parasite) -in terms of IgE binding, structural stability, endolysosomal degradation and subsequent peptide generation,and T-cell cross-reactivity in a BALB/c murine model. Results:Despite their conserved primary structure and consequent IgE co-reactivity, the invertebrate tropomyosins displayed different protein stabilities. Pen m 1 and Ani s 3, but not Der p 10 and Bla g 7 elicited differential melting temperatures that were pH-dependent. Endolysosomal experiments demonstrated differential degradation, as a function of stability, generating different peptide repertoires.Pen m 1 T-cell clones, with specificity for sequences highly conserved in all four tropomyosins, did not proliferate with Der p 10, Bla g 7 and Ani s 3, indicating that these peptides were not naturally produced for other invertebrate tropomyosins. Conclusions:Our data suggest that, although invertebrate tropomyosins exhibit a high degree of IgE cross-reactivity due to conserved B-cell epitopes, they do not necessarily share identical cross-reactive T-cell epitopes. This is likely due to differential endolysosomal processing as a function of different structural stabilities. Word Count: 3619 14.Kavan D, Man P. MSTools-Web based application for visualization and presentation of HXMS data. Int J Mass Spectrom. 2011;302(1):53-58. 15.Reese G, Viebranz J, Leong-Kee SM, et al. Reduced allergenic potency of VR9-1, a mutant of the major shrimp allergen Pen a 1 (tropomyosin).

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Digestibility and Immunoreactivity of Shrimp Extracts Using an In Vitro Digestibility Model with Pepsin and Pancreatin

Cited by 17 publications

References 16 publications

Effects of buffer additives and thermal processing methods on the solubility of shrimp (Penaeus monodon) proteins and the immunoreactivity of its major allergen

Effects of buffer additives and thermal processing methods on the solubility of shrimp (Penaeus monodon) proteins and the immunoreactivity of its major allergen

Gastrointestinal fate of food allergens and its relationship with allergenicity

Effect of structural stability on endolysosomal degradation and T-cell reactivity of major shrimp allergen tropomyosin

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