非洲猪瘟病毒pI215L蛋白结构与功能的生物信息学分析

doi:10.12160/j.issn.1672-5190.2023.04.002

畜牧与饲料科学 ›› 2023, Vol. 44 ›› Issue (4): 10-16.doi: 10.12160/j.issn.1672-5190.2023.04.002

非洲猪瘟病毒pI215L蛋白结构与功能的生物信息学分析

赵金兵¹,王铁军²,王莫离¹,石建州¹,姚伦广¹

1.南阳师范学院，河南南阳 473061
2.南阳农业职业学院，河南南阳 473000

收稿日期:2023-02-14 出版日期:2023-07-30 发布日期:2023-08-30
通讯作者: 姚伦广（1974—），男，教授，博士，主要从事免疫学研究工作。
作者简介:赵金兵（1979—），男，馆员，主要从事猪病学研究工作。
基金资助:
南阳师范学院2023年理工科校级STP项目(2023STP006);河南省科技攻关项目(222102110260);河南省高等学校重点科研项目(22A180026);南阳市科技攻关项目(KJGG136)

Bioinformatics Analysis on the Structure and Function of African Swine Fever Virus pI215L Protein

ZHAO Jinbing¹,WANG Tiejun²,WANG Moli¹,SHI Jianzhou¹,YAO Lunguang¹

1. Nanyang Normal University，Nanyang 473061，China
2. Nanyang Vocational College of Agriculture，Nanyang 473000，China

Received:2023-02-14 Online:2023-07-30 Published:2023-08-30

摘要/Abstract

摘要：

[目的]研究非洲猪瘟病毒（African swine fever virus，ASFV）pI215L蛋白的结构与功能。[方法]从ASFV数据库（The African Swine Fever Virus Database，ASFVdb）下载29个不同ASFV毒株的pI215L基因序列，利用生物信息学工具分析不同毒株pI215L基因的同源性及遗传进化关系，预测pI215L蛋白的理化性质、二级结构、线性表位及三维空间位置。[结果]不同ASFV毒株的pI215L基因核苷酸序列同源性较高；pI215L蛋白性质不稳定，亲水性较高，二级结构主要含有α-螺旋、延伸链、β-转角、无规卷曲4种形式，含有1个E2泛素化结合酶结构域；共有16处肽段是潜在的线性表位；使用SWISS-MODEL对pI215L蛋白的三级结构完成同源建模，在PDB数据库中与6NYO.1（ubiquitin-conjugating enzyme E2 R2和ubiquitin）的同源性达46.06%；再使用PyMOL软件对pI215L蛋白进行构象表位预测，准确定位预测的表位三维空间位置在模型中的分布。[结论]该研究结果为解析pI215L蛋白的结构和功能以及研制ASFV疫苗和抗ASFV药物提供了参考。

关键词: 非洲猪瘟病毒, 生物信息学, pI215L蛋白, 结构与功能

Abstract:

[Objective] This study aimed to analyze the structure and function of African swine fever virus （ASFV） pI215L protein. [Method] A total of 29 pI215L gene sequences of different ASFV strains were downloaded from the African Swine Fever Virus Database （ASFVdb）. Bioinformatics tools were used to analyze the homology and genetic evolution of pI215L gene of different ASFV strains, and to predict the physicochemical properties, secondary structure, linear epitope, and three-dimensional spatial location of pI215L protein. [Result] The pI215L gene sequences had high homology among different ASFV strains. The pI215L protein was unstable and hydrophilic. Its secondary structure mainly contained four forms, including α-helix, extend strand, β-turn, and random coil, and had a domain of E2 Ubiqutin-conjugating enzyme. A total of 16 peptide fragments were potential linear epitopes. SWISS-MODEL was used to complete homology modeling of the tertiary structure of pI215L protein, and its homology with 6NYO.1 （ubiquitin-conjugating enzyme E2 R2 and ubiquitin） in the PDB database was 46.06%. The PyMOL software was used to predict the conformational epitopes of pI215L protein to accurately locate the distribution of the predicted three-dimensional spatial position of the epitopes in the model. [Conclusion] Our results provided references for unravelling the structure and function of pI215L protein, as well as developing vaccines and drugs for prevention and control of ASFV.

Key words: African swine fever virus, bioinformatics, pI215L protein, structure and function

中图分类号:

S858.282.651

赵金兵, 王铁军, 王莫离, 石建州, 姚伦广. 非洲猪瘟病毒pI215L蛋白结构与功能的生物信息学分析[J]. 畜牧与饲料科学, 2023, 44(4): 10-16.

ZHAO Jinbing, WANG Tiejun, WANG Moli, SHI Jianzhou, YAO Lunguang. Bioinformatics Analysis on the Structure and Function of African Swine Fever Virus pI215L Protein[J]. Animal Husbandry and Feed Science, 2023, 44(4): 10-16.

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非洲猪瘟病毒pI215L蛋白结构与功能的生物信息学分析

Bioinformatics Analysis on the Structure and Function of African Swine Fever Virus pI215L Protein

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