Mapping IgE binding epitopes of major shrimp (Penaeus monodon) allergen with immunoinformatics tools

Zheng, Lei; Lin, Hong; Pawar, R. A.; Liu, Zhenxing; Li, Minghua

doi:10.1016/j.fct.2011.07.043

Cited by 101 publications

(84 citation statements)

References 28 publications

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“…The structure of alcohol dehydrogenase (ADH) and Cur I 3 from Curvularia lunata were in silico predicted, and it was shown that computational tools applied for 3-D structure determination provide ideal approximation and can be employed for epitope identification [15,32]. Recently, Per a 10 Allergen of Periplaneta Americana and Cur I 3 of Curvularia lunata were homology modelled, and their B and T-cell epitope regions were identified successfully by in silico tools [18,32]. In the present study, the lectin from black turtle beans (P. vulgaris L.), a homo-tetramer allergen protein, whose structure consisting of four identical or almost identical subunits, was modelled based on the template phytohemagglutinin from P. vulgaris (PHA-E) which has been solved experimentally by NMR [30], because of the highest sequence identity (98.43%) (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Thus, a large number of rapid, fairly accurate and cost effective in silico algorithms are being developed with an enormous expansion in protein structures [17]. In a recent study, combination strategy with Antigenic Peptides, BepiPred 1.0 Server and DNAStar analytical tools was accurately applied in the screen and recognition of B-cell epitopes of tropomyosin in Penaeus monodon [18]. Three B-cell epitopes and two T-cell epitopes from Per a 10 allergen of Periplaneta Americana, were successfully identified in conjunction with various B-cell prediction (ABCpred, Antigenic, BepiPred 1.0b, Bcepred, BCPREDS, DNASTAR, ElliPro and Epitopia) and T-cell prediction (MHCPred, SVRMHC and SMM-Alig, MULTIPRED, ProPred, RANKPEP and SVMHC) softwares, respectively [19].…”

Section: Introductionmentioning

confidence: 99%

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In Silico Identification and in Vitro Analysis of B and T-Cell Epitopes of the Black Turtle Bean (Phaseolus Vulgaris L.) Lectin

Zhao

Elfalleh

et al. 2018

Cell Physiol Biochem

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Background/Aims: The incidence of lectin allergic disease is increasing in recent decades, and definitive treatment is still lacking. Identification of B and T-cell epitopes of allergen will be useful in understanding the allergen antibody responses as well as aiding in the development of new diagnostics and therapy regimens for lectin poisoning. In the current study, we mainly addressed these questions. Methods: Three-dimensional structure of the lectin from black turtle bean (Phaseolus vulgaris L.) was modeled using the structural template of Phytohemagglutinin from P. vulgaris (PHA-E, PDB ID: 3wcs.1.A) with high identity. The B and T-cell epitopes were screened and identified by immunoinformatics and subsequently validated by ELISA, lymphocyte proliferation and cytokine profile analyses. Results: Seven potential B-cell epitopes (B1 to B7) were identified by sequence and structure based methods, while three T-cell epitopes (T1 to T3) were identified by the predictions of binding score and inhibitory concentration. The epitope peptides were synthesized. Significant IgE binding capability was found in B-cell epitopes (B2, B5, B6 and B7) and T2 (a cryptic B-cell epitope). T1 and T2 induced significant lymphoproliferation, and the release of IL-4 and IL-5 cytokine confirmed the validity of T-cell epitope prediction. Abundant hydrophobic amino acids were found in B-cell epitope and T-cell epitope regions by amino acid analysis. Positively charged amino acids, such as His residue, might be more favored for B-cell epitope. Conclusion: The present approach can be applied for the identification of epitopes in novel allergen proteins and thus for designing diagnostics and therapies in lectin allergy.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

In Silico Identification and in Vitro Analysis of B and T-Cell Epitopes of the Black Turtle Bean (Phaseolus Vulgaris L.) Lectin

Zhao

Elfalleh

et al. 2018

Cell Physiol Biochem

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“…The dot-blot assay Dot-blot assay was performed as previously described (Cai et al, 2010;Zheng, Lin, Pawar, Li, & Li, 2011) with some modifications. In brief, purified CPP was spotted onto nitrocellulose membranes (5 µl for each dot) and left to dry at room temperature 37°C.…”

Section: Sds-page Analysismentioning

confidence: 99%

Evaluation of the IgE reactivity of common pandora parvalbumin in a Moroccan population and action of heating and enzymatic treatments

Mejrhit

Azdad

Aarab

2017

Food and Agricultural Immunology

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The aim of this study was to evaluate the immunoglobulin E (IgE) sensitivity to common pandora (Pagellus erythrinus) parvalbumin (CPP) in a Moroccan population from the Fez region, and then to study the effect of temperature and enzymatic digestion on the allergenicity of CPP. This work was conducted with a questionnaire completed by a sera-bank, obtained from 500 patients recruited from Fez hospitals. Their sera were analyzed for specific IgE against CPP. Evaluation of specific IgE showed that 11.8% of patients present higher values (>150 IU/ml). Further indirect ELISA and dot-blot results indicated that CPP showed a decrease in the binding of anti-IgE under heating with an average diminution of 41.9%, while pepsin hydrolysis reduced IgE recognition by 22.9%. These results demonstrate that this population was sensitive to CPP and the sensitivity could be reduced by heating and pepsin hydrolysis with an action higher with temperature than enzymatic digestion processing. ARTICLE HISTORY

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“…The amino acid sequences of the Pen a1 epitopes were highly conserved, and some species of shrimp had identical amino acid sequences (Zheng et al, 2011). Most recent research to examine the desensitization of shrimp allergens focused on the whole tropomyosin protein of Pen a1.…”

Section: Introductionmentioning

confidence: 99%

Influence of Gamma Irradiation and Heat Treatment on the Immunogenicity of Five Epitopes of Pen a1

Mou

Gao

Zhao

et al. 2014

FSTR

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BACKGROUND: Pen a1 is a major allergen in shrimp. It is a 284 amino acid protein member of the tropomyosin family with a molecular weight of 36 kDa. Irradiation and heat treatments have been previously shown to reduce the immunoreactivity of Pen a1, but since anaphylaxis is not induced by the whole protein but by epitopes within the protein, studying of the influence of these treatments on the epitopes of Pen a1 is helpful for understanding the sensitization mechanism. In this study, the immunoreactivity of the five epitopes of Pen a1 exposed to heat and irradiation treatments was detected by Ci-ELISA and western blot, using specific anti-sera generated from 5 synthesized epitope peptides of Pen a1. We examined the function of each epitope in the sensitization process by analyzing the variations of their immunoreactivity following irradiation, heat treatment, or a combination of both. RESULTS

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Mapping IgE binding epitopes of major shrimp (Penaeus monodon) allergen with immunoinformatics tools

Cited by 101 publications

References 28 publications

In Silico Identification and in Vitro Analysis of B and T-Cell Epitopes of the Black Turtle Bean (Phaseolus Vulgaris L.) Lectin

In Silico Identification and in Vitro Analysis of B and T-Cell Epitopes of the Black Turtle Bean (Phaseolus Vulgaris L.) Lectin

Evaluation of the IgE reactivity of common pandora parvalbumin in a Moroccan population and action of heating and enzymatic treatments

Influence of Gamma Irradiation and Heat Treatment on the Immunogenicity of Five Epitopes of Pen a1

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