摘要: |
对三种隐孢子虫(C. parvum Iowa II、 C. hominis TU502和C. muris RN66)钙依赖蛋白激酶(Calcium-dependent protein kinases, CDPKs)进行生物信息学分析,探索该蛋白的结构并预测其功能,为其基因功能的研究提供一定的理论基础。通过隐孢子虫基因组数据库收集数据,获得三种隐孢子虫CDPKs蛋白的序列信息,通过生物信息学软件进行分析,预测该蛋白的理化性质、翻译后修饰位点、功能域、亚细胞定位、二级结构、亲/疏水性、抗原表位等。隐孢子虫CDPKs的蛋白性质不稳定,理论分子量从59.76 kDa到76.63 kDa,pI值为5.33~6.09,CDPKs不具有跨膜区和信号肽,不是跨膜分泌性蛋白,都具有蛋白激酶C 磷酸化位点、酪氨酸激酶Ⅱ磷酸化位点、酪氨酸激酶磷酸化位点、cAMP和cGMP依赖蛋白激酶磷酸化位点、N-端糖基化位点、N-端肉豆蔻酰化位点和EF-hand钙结合域,二级结构主要以α螺旋和无规卷曲为主;CDPKs主要存在虫体细胞内,均有20多个潜在的抗原表位。在隐孢子虫中,CDPKs蛋白不仅可单独发挥作用,而且还能通过相互结合发挥其生物学效应;同时,CDPKs有望成为候选疫苗及潜在药物靶点。 |
关键词: 隐孢子虫 钙依赖蛋白激酶 生物信息学 蛋白结构 功能预测 |
DOI:10.3969/j.issn.1672-5565.2016.02.03 |
分类号:Q51 |
文献标识码:A |
基金项目:国家外专局“外专千人计划”专项基金项目(No.WQ20136300172)。 |
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Function analysis of Calcium-dependent protein kinases in Cryptosporidiumbased on bioinformatics |
ZHANG Xueyong1,2, JIAN Yingna1,2, MA Liqing1,2
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(1. The Academy of Animal and Veterinary Sciences, Qinghai University, Xining 810016, China;2. Qinghai Academy of Animal Sciences and Veterinary Medicine, Xining 810016, China)
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Abstract: |
HJ1.6mm]The propose of this study is to conduct bioinformatics analysis about the calcium-dependent protein kinases of Cryptosporidium(C.parvum Iowa II,C.hominis TU502and C.murisRN66),and to explore the structures and predict the functions of the protein family for the studies of genetic function of Cryptosporidiumoffering theoretical basis. The protein sequences of CryptosporidiumCDPKs were obtained from the Genome Database and then the bioinformatics softwares were used to analyze and predict the physico-chemical properties of the proteins, such as post-translational modification sites, functional domains, subcellular localization, secondary structure, hydrophilicity/hydrophobicity and epitopes.The proteins had unstable physico-chemical characteristics. The theoretical molecular weight of the deduced proteins were from 59.76 to 59.76 kDa, theoretical pI from 5.33 to 6.09,no transmembrane regions and signal peptides, all had N-glycosylation sites, protein kinase C phosphorylation sites, casein kinase II phosphorylation sites, Tyrosine kinase phosphorylation sites,N-myristoylation sites,cAMP-and cGMP-dependent protein kinase phosphorylation sites and EF-hand calcium-binding domains; Secondary structure mainly were alpha helix and random coil;CDPKs mainly exist in body cells,had more than 20 potential antigen epitopes.In Cryptosporidium,CDPKs were able to work alone, but also through mutual supports exert biological effects,meanwhile CDPKs will promise to be vaccine candidates and potential drug targets. |
Key words: Cryptosporidium Calcium-dependent protein kinases Bioinformatics Protein structure Function prediction |