B-cell and T-cell epitope identification with stability analysis of AI-2 import ATP-binding cassette LsrA from S. typhi In silico approach

2018 ◽  
Vol 123 ◽  
pp. 487-495 ◽  
Author(s):  
Princy Vijayababu ◽  
Gopinath Samykannu ◽  
Christian Bharathi Antonyraj ◽  
SundaraBaalaji Narayanan ◽  
Syed Ibrahim Basheer Ahamed ◽  
...  
2020 ◽  
Author(s):  
Muhammad Saqib Sohail ◽  
Syed Faraz Ahmed ◽  
Ahmed Abdul Quadeer ◽  
Matthew McKay

2021 ◽  
Vol 171 ◽  
pp. 29-47 ◽  
Author(s):  
Muhammad Saqib Sohail ◽  
Syed Faraz Ahmed ◽  
Ahmed Abdul Quadeer ◽  
Matthew R. McKay

2016 ◽  
Vol 2016 ◽  
pp. 1-11 ◽  
Author(s):  
Lenka Potocnakova ◽  
Mangesh Bhide ◽  
Lucia Borszekova Pulzova

Identification of B-cell epitopes is a fundamental step for development of epitope-based vaccines, therapeutic antibodies, and diagnostic tools. Epitope-based antibodies are currently the most promising class of biopharmaceuticals. In the last decade, in-depth in silico analysis and categorization of the experimentally identified epitopes stimulated development of algorithms for epitope prediction. Recently, various in silico tools are employed in attempts to predict B-cell epitopes based on sequence and/or structural data. The main objective of epitope identification is to replace an antigen in the immunization, antibody production, and serodiagnosis. The accurate identification of B-cell epitopes still presents major challenges for immunologists. Advances in B-cell epitope mapping and computational prediction have yielded molecular insights into the process of biorecognition and formation of antigen-antibody complex, which may help to localize B-cell epitopes more precisely. In this paper, we have comprehensively reviewed state-of-the-art experimental methods for B-cell epitope identification, existing databases for epitopes, and novel in silico resources and prediction tools available online. We have also elaborated new trends in the antibody-based epitope prediction. The aim of this review is to assist researchers in identification of B-cell epitopes.


2018 ◽  
Vol 49 (4) ◽  
pp. 1600-1614 ◽  
Author(s):  
Shudong He ◽  
Jinlong Zhao ◽  
Walid Elfalleh ◽  
Mohamed Jemaà ◽  
Hanju  Sun ◽  
...  

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.


2020 ◽  
Vol 16 (3) ◽  
pp. e1008243 ◽  
Author(s):  
Ayat Zawawi ◽  
Ruth Forman ◽  
Hannah Smith ◽  
Iris Mair ◽  
Murtala Jibril ◽  
...  

2004 ◽  
Vol 25 ◽  
pp. S584
Author(s):  
Michael G. Agadjanyan ◽  
Irina Petrushina ◽  
Anahit Ghochikyan ◽  
Vitaly Vasilevko ◽  
Nina Movsesyan ◽  
...  

2013 ◽  
Vol 2013 ◽  
pp. 1-7 ◽  
Author(s):  
Yu-Min Lin ◽  
Guey-Mei Jow ◽  
Shu-Chi Mu ◽  
Bing-Fang Chen

To control hepatitis B virus (HBV) infection, a universal HBV vaccination program for infants was launched in Taiwan in 1984. The aim of this study was to investigate the role of B-cell and T-cell epitope variations of HBsAg and polymerase in HBV infection in vaccinated children. One hundred sixty-three sera from vaccinated children were enrolled randomly. HBV serum markers, including hepatitis B surface antigen (HBsAg) and antibodies to HBsAg (anti-HBs) and core antigen (anti-HBc), were detected by ELISA. Nucleotide sequences encoding the S and the pre-S regions of HBsAg were analyzed in all HBsAg positive sera. Five children were HBsAg positive. Sequence analysis of S, pre-S, and overlapped polymerase (P) genes showed that HBV isolates of HBsAg-positive vaccinees were variants; no G145R but G145A and other substitutions were found in the “a” determinant. Fifteen, six, and eight amino acid substitutions within B-cell and T-cell epitopes of S, pre-S, and P regions were detected, respectively. Several immune-epitope mutants, such as S45T/A, N131T, I194V, and S207N in S, were detected in all isolates. In conclusion, our results suggested that these naturally occurring immunoepitope mutants, which changed their immunogenicity leading to escape from immune response, might cause HBV infection.


2013 ◽  
Vol 2013 ◽  
pp. 1-9 ◽  
Author(s):  
Esther Blanco ◽  
Carolina Cubillos ◽  
Noelia Moreno ◽  
Juan Bárcena ◽  
Beatriz G. de la Torre ◽  
...  

Synthetic peptides incorporating protective B- and T-cell epitopes are candidates for new safer foot-and-mouth disease (FMD) vaccines. We have reported that dendrimeric peptides including four copies of a B-cell epitope (VP1 136 to 154) linked to a T-cell epitope (3A 21 to 35) of FMD virus (FMDV) elicit potent B- and T-cell specific responses and confer protection to viral challenge, while juxtaposition of these epitopes in a linear peptide induces less efficient responses. To assess the relevance of B-cell epitope multivalency, dendrimers bearing two (B2T) or four (B4T) copies of the B-cell epitope from type O FMDV (a widespread circulating serotype) were tested in CD1 mice and showed that multivalency is advantageous over simple B-T-epitope juxtaposition, resulting in efficient induction of neutralizing antibodies and optimal release of IFNγ. Interestingly, the bivalent B2T construction elicited similar or even better B- and T-cell specific responses than tetravalent B4T. In addition, the presence of the T-cell epitope and its orientation were shown to be critical for the immunogenicity of the linear juxtaposed monovalent peptides analyzed in parallel. Taken together, our results provide useful insights for a more accurate design of FMD subunit vaccines.


Vaccine ◽  
1997 ◽  
Vol 15 (16) ◽  
pp. 1761-1766 ◽  
Author(s):  
Patricia A. O'Hern ◽  
Zhi-Guo Liang ◽  
Charanjit S. Bambra ◽  
Erwin Goldberg

1997 ◽  
Vol 10 (3) ◽  
pp. 129-136 ◽  
Author(s):  
SOFIA CASARES ◽  
TEODOR-DORU BRUMEANU ◽  
ADRIAN BOT ◽  
CONSTANTIN A. BONA

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