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 ORIGINAL ARTICLE
Year : 2017  |  Volume : 35  |  Issue : 4  |  Page : 522-528

The bioinformatics analyses reveal novel antigen epitopes in major outer membrane protein of Chlamydia trachomatis


1 State Key Laboratory Incubation Base of Xinjiang Major Diseases Research (2010DS890294) and Xinjiang Key Laboratory of Echinococcosis, First Affiliated Hospital of Xinjiang Medical University, Urumqi, Xinjiang 830011, P.R. China
2 State Key Laboratory Incubation Base of Xinjiang Major Diseases Research (2010DS890294) and Xinjiang Key Laboratory of Echinococcosis, First Affiliated Hospital of Xinjiang Medical University; Shenzhen Hospital of Southern Medical University, Urumqi, Xinjiang 830011, P.R. China
3 College of Basic Medicine of Xinjiang Medical University, Urumqi, Xinjiang 830011, P.R. China
4 Department of Microbiology and Immunologya and Pathology, University of Texas Health Science Center at San Antonio, San Antonio, Texas, USA
5 State Key Laboratory Incubation Base of Xinjiang Major Diseases Research (2010DS890294) and Xinjiang Key Laboratory of Echinococcosis, First Affiliated Hospital of Xinjiang Medical University; College of Basic Medicine of Xinjiang Medical University, Urumqi, Xinjiang 830011, P.R. China

Correspondence Address:
Ms. Amanguli· Yasheng
NO.137 South Road of carp mountain, Urumqi
P.R. China
Dr. Xiumin Ma
College of Basic Medicine of Xinjiang Medical University, Urumqi, Xinjiang 830011
P.R. China
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Source of Support: None, Conflict of Interest: None


DOI: 10.4103/ijmm.IJMM_17_251

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Purpose: The aim of this study was to predict the T-cell and B-cell epitopes in major outer membrane protein (MOMP) of Chlamydia trachomatis (CT) by using online software and also to analyse the secondary structure of MOMP through bioinformatics tools. Materials and Methods: The predictions of secondary structure of MOMP protein were carried out using SOPMA software, and the prediction of B-cell epitopes in MOMP protein was carried out using IEDB and LEPS software, while the T-cell epitopes were predicted by the software of IEBD and SYFPEITHI. The predictions from the software were combined with MOMP protein characteristics, including surface features, hydrophilicity, flexibility, accessibility and plasticity, to analyse the common epitope areas' response by T-cells and B-cells. Results: In the secondary structure of CT MOMP, the alpha-helices accounted for 41.62% of total amino acid, while the beta sheets and random coil accounted for 19.80% and 32.49%, respectively. Predictions combined with MOMP protein surface features, hydrophilicity, flexibility, accessibility and plasticity were further characterised, and three high-score B-cell epitope areas were found as located in 24–31, 307–311 and 318–327 amino acids of MOMP protein, respectively; in the meanwhile, three high-score T-cell epitope areas were found in 234–236, 323–329 and 338–343 amino acids of MOMP using major histocompatibility complex (MHC) class I HLA-A 0201 restrictive T-cell epitope analyser. Conclusion: We established the methods by using the biological information network technologies for looking the T-cell antigen epitopes and B-cell antigen epitopes in MOMP of CT, and three novel T-cell epitopes as well as three novel B-cell epitopes were identified in the current study. It provides important information for further studying the antigenicity of CT MOMP protein and also provides useful information for developing highly efficient subunit vaccines for CT.






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