IgE Epitope Analysis for Scy p 1 and Scy p 3, the Heat-Stable Myofibrillar Allergens in Mud Crab

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Scy p 8 (triosephosphate isomerase) as a crab allergen in inducing distinct T-helper (Th) cell differentiation and a linear epitope associated with allergenicity remain elusive. In this study, mice sensitized with Scy p 8 exhibited significantly upregulated levels of IgE, IgG1, and IL-4 release, inducing a Th2 immune response. Moreover, the release of IFN-γ (Th1) and the levels of Treg cells were downregulated, while IL-17A (Th17) was upregulated, indicating that Scy p 8 disrupted the Th1/Th2 balance and Th17/Treg balance in mice. Furthermore, bioinformatics prediction and serum samples from crab-allergic patients and mice enabled the discovery of 8 linear epitopes of Scy p 8. Meanwhile, the analysis of peptide similarity and tertiary superposition revealed that 8 epitopes of Scy p 8 exhibited conservation across various species, potentially resulting in cross-reactivity. These findings possess the potential to enhance the comprehension of crab allergens, thereby establishing a foundation for investigating cross-reactivity.

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Allergenicity and Linear Epitope Analysis of Scy p 8, an Allergen from Mud Crab

Xia,

Li,

Liu

et al. 2024

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“…Typical examples include atezolizumab, an antiprogrammed cell death 1 ligand 1 antibody identified by screening a human phage display library and approved by the FDA in 2016 for treating urothelial carcinoma and metastatic lung cancer. , Ecallantide, a peptide containing 60 amino acids screened by phage display, was approved by the FDA in 2009 for treating hereditary angioedema . In addition, food scientists have shown considerable interest in implementing this technique in food allergy diagnosis, biotoxin, and foodborne pathogenic bacterial detection. − More recently, Li et al screened a phage random linear 7-mer peptide library to identify two candidate peptides (MTLERPW and MNLHLSF) that bind to the umami receptor’s venus flytrap domain (T1R1-VFT) with high affinity ( K d = 790 and 630 nM, respectively). They further validated that these two peptides display an umami taste and significantly enhance the umami intensity in monosodium glutamate solution, suggesting that phage display is a promising tool for discovering taste peptides …”

Section: Strategies To Develop Rice Bran Lipase Inhibitorsmentioning

confidence: 99%

Developing Lipase Inhibitor as a Novel Approach to Address the Rice Bran Rancidity Issue─A Critical Review

Li,

Liu,

Cai

et al. 2024

Rice bran is a valuable byproduct from the food processing industry, which contains abundant protein, essential unsaturated fatty acids, and numerous bioactive compounds. However, its susceptibility to rancidity greatly restricts its wide utilization. Many strategies have been proposed to delay the rancidity of rice bran, but most of them have their respective limitations. Here, we proposed that developing rice ban lipase peptide inhibitors represents an alternative and promising prescription for impeding the rancidity of rice bran, in contrast to the conventional stabilization approaches for rice bran. For this reason, the rancidity mechanisms of rice bran and the research progress of rice bran lipases were discussed. In addition, the feasibility of utilizing in silico screening and phage display, two state-of-the-art technologies, in the design of the related peptide inhibitors was also highlighted. This knowledge is expected to provide a theoretical basis for opening a new avenue for stabilizing rice bran.

“…The emergence of phage display peptide libraries has revolutionized the screening process of millions of peptides with infinite combinations to effectively bind targets of interest by iterative biopanning . Phage display technology exhibits immense potential in drug development and disease diagnosis owing to its strong specificity, high affinity, ease of use, and efficiency. , It is also shining brilliantly in the field of food allergy diagnosis, bio-toxin, and food borne pathogenic bacterial detection, and appropriate target molecules are essential for phage display peptide screening. − …”

Section: Introductionmentioning

confidence: 99%

Identifying Umami Peptides Specific to the T1R1/T1R3 Receptor via Phage Display

Li,

Zhang,

Zhu

et al. 2023

Umami peptides are small molecular weight oligopeptides that play a role in umami taste attributes. However, the identification of umami peptides is easily limited by environmental conditions, and the abundant source and high chromatographic separation efficiency remain difficult. Herein, we report a robust strategy based on a phage random linear heptapeptide library that targets the T1R1-Venus flytrap domain (T1R1-VFT). Two candidate peptides (MTLERPW and MNLHLSF) were readily identified with high affinity for T1R1-VFT binding (K D of MW-7 and MF-7 were 790 and 630 nM, respectively). The two peptides exhibited umami taste and significantly enhanced the umami intensity when added to the monosodium glutamate solution. Overall, this strategy shows that umami peptides could be developed via phage display technology for the first time. The phage display platform has a promising application to discover other taste peptides with affinity for taste receptors of interest and has more room for improvement in the future.