文献类型: 外文期刊
作者: Zhang, Baotai 1 ; Guo, Rongli 1 ; Xiao, Li 1 ; Zhong, Chunyan 1 ; Yuan, Xuesong 1 ; Huang, Jin 1 ; Zhu, Xuejiao 1 ; Zhou, Jinzhu 1 ; Fan, Baochao 1 ; Xue, Tao 2 ; Liu, Chuanmin 1 ; Zhu, Xing 5 ; Li, Jizong 1 ; Li, Bin 1 ;
作者机构: 1.Jiangsu Acad Agr Sci, Key Lab Vet Biol Engn & Technol, Inst Vet Med, Minist Agr, Nanjing 210014, Peoples R China
2.Linyi Univ, Sch Pharm, Linyi 276000, Peoples R China
3.Jiangsu Univ, Inst Life Sci, Sch Food & Biol Engn, Zhenjiang 212013, Peoples R China
4.Nanjing Agr Univ, Coll Vet Med, Nanjing 210095, Peoples R China
5.Guizhou Univ, Coll Anim Sci, Guiyang 550025, Peoples R China
6.Yangzhou Univ, Jiangsu Co Innovat Ctr Prevent & Control Important, Yangzhou 225009, Peoples R China
7.Qianxinan Vocat & Tech Coll Nationalities, Dept Bioengn, Xingyi 562400, Peoples R China
8.Inst Vet Med, Jiangsu Acad Agr Sci, Key Lab Vet Biol Engn & Technol, Key Lab Vet Diag,Minist Educ, Nanjing 210014, Peoples R China
关键词: PTVs; High-throughput sequencing; VP1; Diarrhea; Phylogenetic analysis
期刊名称:HELIYON ( 影响因子:4.0; 五年影响因子:4.1 )
ISSN:
年卷期: 2023 年 9 卷 4 期
页码:
收录情况: SCI
摘要: Porcine Teschoviruses (PTVs) are associated with polioencephalomyelitis and various diseases, including reproductive and gastrointestinal disorders of pigs and wild boars, but rarely detected in the feces of pigs. In this study, a sample of swine diarrhea that tested positive for PTVs is subjected to high-throughput sequencing. The viral genome was 7221 nucleotides (nt) in length, which was consisted of twelve genes. Phylogenetic analysis showed and it was closely related to the PTV-HNMY(MG755212.1). The nucleotide homology of VP1 gene of PTVs JS2021 with PTV-1AF 296102.1 reached 82.97%, belonging to a branch of PTV-1 serotype. The nucleotide ho-mology of VP1 protein with other serotypes of PTV is quite different from that of other serotypes of PTV. Bioinformatics analysis showed that PTVs have four capsid proteins, namely VP1, VP2, VP3 and VP4. The VP1 encodes a 29 kDa protein, which is the main protective antigen, a theoretical isoelectric point of 6.73, no transmembrane domain, no signal peptide and potential phosphorylation site. The VP1 protein is an unstable hydrophilic intracellular protein, which contains four secondary structures: irregular curl (c), extended chain (e), alpha-helix (h) and beta-folded (t). The tertiary structure is heart-shaped and has multiple B cell epitopes. By analyzing the tertiary structure, we found that the amino acid at position 129 of VP1 mutated and reduction a larger alpha helix. This may lead to the main cause of piglet diarrhea. These findings enriched our knowledge of the viruses in the role of swine diarrhea, and help to develop an effective strategy for disease prevention and control.
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