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人白细胞介素-38的特性分析及B细胞表位的预测 被引量:2

Characteristic Analysis of Human Interleukin- 38 and Prediction of Its B- Cell Epitope
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摘要 目的:为进一步了解人白细胞介素(IL)-38蛋白质的特性和B细胞表位,从GenBank中查得其序列,用生物信息学等方法预测人IL-38蛋白质的二级结构等特性,并对其B细胞表位进行预测。方法:应用ProtParam tool、ProtScale、Emini和Kolaskar等程序或方法,对IL-38的组成、理化特性、亲水性、柔韧性和可及性等进行分析,以进一步预测其二级结构和抗原表位。结果:IL-38的二级结构主要由无规则卷曲(44.08%)和β-折叠(39.47%)组成。其B细胞表位可能位于第26-36、45-55、78-98和124-143等氨基酸区段。结论:首次利用生物信息学方法对IL-38基因及其蛋白质结构进行了分析和预测,预测结果将有助于确定IL-38的B细胞表位,为IL-38基因功能的深入研究及研制IL-38单克隆抗体提供了理论依据。 Objective:Based on interleukin (IL) -38 amino acid sequence from GenBank,the secondary structure and B -Cell epitope were predicted by bioinformaties. Method :The ProtParam tool, ProtSeale, Emini and Kolaskar were applied to analyze human IL- 38 pro- tein' s composition, physical and chemical properties, hydrophileity ,flexibility, aeeessibility, and ordered to forecast seeondary structures, B -cell epitopes. Result:The secondary structure of human IL -38 eontented random coil (44. 08% ) and extended strand (39.47%). It showed that the most possible epitopes of IL - 38 were located in or adjacent to amino acid 26 - 36,45 - 55,78 - 98,124 - 143. Conclusion:The view was the first report to analysis the construction of protein IL - 38 by bioinformaties. These results would be helpful for the estimate of the epitopes, provided references for further research of human IL - 38 protein function and a theory basis for de- veloping monoclonal antibodies against human IL- 38.
出处 《生物技术》 CAS CSCD 北大核心 2014年第1期41-44,共4页 Biotechnology
基金 国家自然科学基金项目("阻抑IL-33/ST2信号对慢性阻塞性肺疾病气道炎症的作用及机制" No.81070034) 宁波市科技创新团队项目("宁波市消化系统恶性肿瘤诊治新技术创新团队" 2011B82014) 浙江省教育厅科研项目(Y201327689) 宁波大学学科项目(XKL11D2112 XKL11D2113)资助
关键词 人IL-38 二级结构 B细胞表位 Human IL - 38 Secondary structure B - cell epitope
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  • 1郭秀丽,代红星,李祥龙,周荣艳,王立泽.不同物种MHC-DQA1基因部分序列的生物信息分析[J].中国畜牧兽医,2007,34(1):65-67. 被引量:9
  • 2Blattman AW, Hulme DJ, Kinghorn BP, et al. A search for associations between major histocompatibility complex restriction fragment length polymorphism bands and resistances Haemonchus contours in- fection in sheep. Animal Genetics, 1993,24:277-282.
  • 3Escayg AP, Montgomery GW, Hickford JG, et al. A BgI II RFLP at the ovine M HC class II DRA locus. Anim Genet, 1993,24 (3) :217.
  • 4Escayg AP, Hickford JGH, Bullock DW, et al. Polymorphism at the ovine major histocompatibility complex class II loci. Anita Genet, 1996,27(5) :305-312.
  • 5Nakai K,Horton P. PSORT:a program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem Sci, 1999 (24) :34-36.
  • 6Jensen LJ, Gupta R, Blom N, et al. Ab initio prediction of human orphan protein function from post-translational modifications and localization features. J Mol Biol, 2002,319 : 1257-1265.
  • 7Jensen LJ, Strfeldt HH, Borunak S. Prediction of human protein function according to gene ontology categories. Bioinformatics, 2003,19(5) :635-642.
  • 8Walter J, High KA. Gene therapy for the hemophiliac. Adv Vet Med, 1997,23 ( 12 ) : 119-134.
  • 9Izard JW, Doughty MB, Kendall DA. Physical and eonformational properties of synthetic idealized signal sequences parallel their biologicalfunctior L. Biochemistry, 1995,34 ( 31 ) :9904-9906.
  • 10Antonio MR, Martinez A. Secretion of recombinant pro-and mature fungal-sarein ribo toxin by themethylotrophie yeast P/ch /apastoris:the Lys-arg motif is required for maturation. Protein Expr Purif, 1998,12(6) :315-322.

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