Immunogenic peptides: B &amp; T Cell Epitopes of Per a 10 Allergen of Periplaneta americana

Govindaraj, Dhanapal; Sharma, Swati; Gaur, Shailendra Nath; Lavasa, Shakuntala; Prasad, Nagendra; Arora, Naveen

doi:10.1016/j.molimm.2016.10.007

Cited by 19 publications

(20 citation statements)

References 39 publications

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“…4c). The epitope peptides identified by specific IgE binding and PBMC proliferations from Per a 10 allergen of Periplaneta Americana were also found to be of high hydrophobicity [19].…”

Section: Discussionmentioning

confidence: 91%

“…The online tools are fast, precise and extremely efficient means of structure identification and mapping of epitope regions [35,36]. Since the prediction accuracy of combined methods for B and T-cell epitope prediction is far higher than any single in silico tool, consensus method was used as it combined the strengths of different prediction algorithms [19,35]. Nevertheless, due to a wide range of predictions for epitopes was obtained, further structural screenings were absolutely essential.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, high average flexibility and surface accessibility of sequence could also be employed as the indicators for B-cell epitope identification, as the suggested sequence would be more flexible and easily exposed outside [19,39]. Higher average flexibility and surface accessibility are found in epitopes B5 and B6, which displayed higher IgE binding capacity (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…The amino acid composition analysis of ADH from Curvularia lunata showed that Pro and Lys residues had high propensities to lie in B-cell epitope regions [15]. Recently, Gly, Pro, Cys and Glu residues were found to be rich in IgE binding epitope peptides (Per a 10) of Periplaneta americanao [19]. Amino acids in lectin B-cell epitopes were further analyzed by QSAR method, which indicated that the identified lectin B-cell epitopes tend to consist of hydrophobic residues, but positively charged residues such as His residue seemed to have a more important role in B-cell epitopes activity (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…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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“…4c). The epitope peptides identified by specific IgE binding and PBMC proliferations from Per a 10 allergen of Periplaneta Americana were also found to be of high hydrophobicity [19].…”

Section: Discussionmentioning

confidence: 91%