白念珠菌细胞壁蛋白Csp37抗原表位预测

中国真菌学杂志　 2018, Vol. 13 　Issue (6): 327-334.

白念珠菌细胞壁蛋白Csp37抗原表位预测

隋雪^1,2, 姜远英¹, 阎澜¹

1. 第二军医大学药学院新药研究中心, 上海 200433;
2. 大连医科大学医学科学研究院, 大连 116044

收稿日期:2018-01-19 出版日期:2018-12-28 发布日期:2018-12-28
通讯作者: 阎澜,E-mail:ylan20001228@sina.com E-mail:ylan20001228@sina.com
作者简介:隋雪,女(汉族),硕士,助理实验师.E-mail:suixue89@dmu.edu.cn
基金资助:
上海市自然科学基金（17ZR1437700），国家自然科学基金面上项目（81470158）

Prediction of the epitopes of the cell wall protein Csp37 in Candida albicans

SUI Xue^1,2, JIANG Yuan-ying¹, YAN Lan¹

1. Center for New Drug Research, School of Pharmacy, Second Military Medical University, 325 Guohe Road, Shanghai 200433;
2. Advanced Institute for Medical Sciences, Dalian Medical University, Dalian 116044

Received:2018-01-19 Online:2018-12-28 Published:2018-12-28

摘要/Abstract

摘要：

目的预测白念珠菌细胞壁蛋白Csp37的抗原表位，分析其作为疫苗靶点的免疫原性。方法采用生物信息学方法对Csp37蛋白的抗原表位进行预测，利用ProtParam网络服务器分析蛋白基本理化性质，SignaIP 3.0预测信号肽，TMHMM软件预测跨膜区，GOR4在线分析蛋白二级结构，DNAStar预测分析亲水性、可塑性、表面可及性和氨基酸抗原指数，使用在线工具ABCPred预测B细胞抗原表位，Syfpeithi预测T细胞抗原表位。最后，综合分析B细胞和T细胞共有抗原表位。结果预测白念珠菌细胞壁蛋白Csp37的B细胞表位9个和T细胞表位8个，以及共有的优势抗原表位5个，共同优势区域为：45-48，76-78，153-158，222-225，303-305位氨基酸。结论白念珠菌细胞壁蛋白Csp37含有丰富的抗原表位，具有诱导细胞免疫应答和体液免疫应答的潜能，可以作为疫苗研究的新靶点。

关键词: 白念珠菌, 抗原表位, 生物信息学, 疫苗

Abstract:

Objective To predict the antigenic epitopes of the cell wall protein Csp37 in Candida albicans, and analyze their immunogenicity as vaccine targets. Methods The epitopes of Csp37 were predicted by bioinformatics method; and the basic physical and chemical properties of Csp37 protein were analyzed by ProtParam network server; signal peptide was predicted by SignalP 3.0 server; transmembrane domain was predicted by TMHMM; secondary structure was predicted by GOR4; hydrophilicity, surface probability, flexible regions and antigenic index were predicted by DNAStar software. ABCPred and Syfpeithi were used to predict B and T cell epitopes, respectively. Finally, the prediction results of B and T cell epitopes were further analyzed to find the common ones. Results Prediction of B cell epitopes and T cell epitopes of the cell wall protein Csp37 of C. albicans were 9 and 8 respectively. The B&T cell common epitopes were 5, and the common dominant region were 45-48,76-78,153-158,222-225,303-305 aa. Conclusion Cell wall protein Csp37 of C. albicans is rich in antigenic epitopes, and has the potential to induce the cellular immune response and the humoral immune response, which could be used as a new target for vaccine against candidiasis.

Key words: Candida albicans, antigenic epitope, bioinformatics, vaccine

中图分类号:

R379.4

隋雪, 姜远英, 阎澜. 白念珠菌细胞壁蛋白Csp37抗原表位预测[J]. 中国真菌学杂志, 2018, 13(6): 327-334.

SUI Xue, JIANG Yuan-ying, YAN Lan. Prediction of the epitopes of the cell wall protein Csp37 in Candida albicans[J]. Chinese Journal of Mycology, 2018, 13(6): 327-334.

参考文献

[1] Horn DL, Neofytos D, Anaissie EJ, et al. Epidemiology and outcomes of candidemia in 2019 patients:data from the prospective antifungal therapy alliance registry[J]. Clin Infect Dis, 2009, 48(12):1695-1703.
[2] Hsu FC, Lin PC, Chi CY, et al. Prognostic factors for patients with culture-positive Candida infection undergoing abdominal surgery[J]. J Microbiol Immunol Infect, 2009, 42(5):378-384.
[3] Nanjappa SG, Klein B S. Vaccine immunity against fungal infections[J]. Curr Opin Immunol, 2014, 28:27-33.
[4] Pfaller MA, Diekema DJ, Andes D, et al. Clinical breakpoints for the echinocandins and Candida revisited:integration of molecular, clinical, and microbiological data to arrive at species-specific interpretive criteria[J]. Drug Resist Updat, 2011, 14(3):164-176.
[5] Odds FC, Brown AJ, Gow N A. Antifungal agents:mechanisms of action[J]. Trends Microbiol, 2003, 11(6):272-279.
[6] Li YY, Chen WY, Li X, et al. Asymptomatic oral yeast carriage and antifungal susceptibility profile of HIV-infected patients in Kunming, Yunnan Province of China[J]. BMC Infect Dis, 2013, 13:46.
[7] Habib AG, Yakasai AM, Owolabi LF, et al. Neurocognitive impairment in HIV-1-infected adults in Sub-Saharan Africa:a systematic review and meta-analysis[J]. Int J Infect Dis, 2013, 17(10):e820-831.
[8] Free SJ. Fungal cell wall organization and biosynthesis[J]. Adv Genet, 2013, 81:33-82.
[9] Sentandreu M, Nieto A, Iborra A, et al. Cloning and characterization of CSP37, a novel gene encoding a putative membrane protein of Candida albicans[J]. J Bacteriol, 1997, 179(15):4654-4663.
[10] Gasteiger E, Gattiker A, Hoogland C, et al. ExPASy:The proteomics server for in-depth protein knowledge and analysis[J]. Nucleic Acids Res, 2003, 31(13):3784-3788.
[11] Li L, Miao W, Liu W, et al. The signal peptide-like segment of hpaXm is required for its association to the cell wall in transgenic tobacco plants[J]. PLoS One, 2017, 12(1):e0170931.
[12] Melen K, Krogh A, Von Heijne G. Reliability measures for membrane protein topology prediction algorithms[J]. J Mol Biol, 2003, 327(3):735-744.
[13] Kouza M, Faraggi E, Kolinski A, et al. The GOR Method of Protein Secondary Structure Prediction and Its Application as a Protein Aggregation Prediction Tool[J]. Methods Mol Biol, 2017, 1484:7-24.
[14] Garnier J, Gibrat JF, Robson B. GOR method for predicting protein secondary structure from amino acid sequence[J]. Methods Enzymol, 1996, 266:540-553.
[15] Burland TG. DNASTAR's Lasergene sequence analysis software[J]. Methods Mol Biol, 2000, 132:71-91.
[16] Costa JG, Faccendini PL, Sferco SJ, et al. Evaluation and comparison of the ability of online available prediction programs to predict true linear B-cell epitopes[J]. Protein Pept Lett, 2013, 20(6):724-730.
[17] Rammensee H, Bachmann J, Emmerich N P, et al. SYFPEITHI:database for MHC ligands and peptide motifs[J]. Immunogenetics, 1999, 50(3-4):213-219.
[18] Konstantinou G N. T-Cell Epitope Prediction[J]. Methods Mol Biol, 2017, 1592:211-222.
[19] Welling GW, Weijer WJ, Van Der Zee R, et al. Prediction of sequential antigenic regions in proteins[J]. FEBS Lett, 1985, 188(2):215-218.
[20] Barlow DJ, Edwards MS, Thornton J M. Continuous and discontinuous protein antigenic determinants[J]. Nature, 1986, 322(6081):747-748.
[21] Schwede T, Kopp J, Guex N, et al. SWISS-MODEL:An automated protein homology-modeling server[J]. Nucleic Acids Res, 2003, 31(13):3381-3385.