Conserved Domains in Variable Surface Lipoproteins A-G of Mycoplasma hyorhinis May Serve as Probable Multi-Epitope Candidate Vaccine: Computational Reverse Vaccinology Approach
文献类型: 外文期刊
作者: Zubair, Muhammad 1 ; Wang, Jia 1 ; Yu, Yanfei 1 ; Rasheed, Muhammad Asif 5 ; Faisal, Muhammad 6 ; Dawood, Ali Sobhy 7 ; Ashraf, Muhammad 9 ; Shao, Guoqing 1 ; Feng, Zhixin 1 ; Xiong, Qiyan 1 ;
作者机构: 1.Jiangsu Acad Agr Sci, Inst Vet Med, Key Lab Vet Biol Engn & Technol, Minist Agr, Nanjing 210000, Peoples R China
2.GuoTai Taizhou Ctr Technol Innovat Vet Biol, Taizhou 225300, Peoples R China
3.Jiangsu Univ, Sch Food & Biol Engn, Zhenjiang 212013, Peoples R China
4.Nanjing Agr Univ, Coll Vet Med, Nanjing 210095, Peoples R China
5.COMSATS Univ Islamabad, Dept Biosci, Sahiwal Campus, Islamabad 45550, Pakistan
6.Ohio State Univ, Coll Med, Comprehens Canc Ctr, Div Hematol,Dept Med, Columbus, OH 43210 USA
7.Huazhong Agr Univ, Dept Prevent Vet Med, State Key Lab Agr Microbiol, Wuhan 430070, Peoples R China
8.Univ Sadat City, Fac Vet Med, Sadat City 32897, Egypt
9.Univ Agr Faisalabad, Inst Microbiol, Faisalabad 37000, Pakistan
10.Jiangsu Univ, Sch Life Sci, Zhenjiang 212013, Peoples R China
关键词: conserved domains; immunoinformatics; multiepitope-based vaccine; M. hyorhinis; reverse vaccinology; variable surface lipoproteins
期刊名称:VETERINARY SCIENCES ( 影响因子:2.4; )
ISSN:
年卷期: 2023 年 10 卷 9 期
页码:
收录情况: SCI
摘要: Mycoplasma hyorhinis (M. hyorhinis) is responsible for infections in the swine population. Such infections are usually cured by using antimicrobials and lead to develop resistance. Until now, there has been no effective vaccine to eradicate the disease. This study used conserved domains found in seven members of the variable lipoprotein (VlpA-G) family in order to design a multi-epitope candidate vaccine (MEV) against M. hyorhinis. The immunoinformatics approach was followed to predict epitopes, and a vaccine construct consisting of an adjuvant, two B cell epitopes, two HTL epitopes, and one CTL epitope was designed. The suitability of the vaccine construct was identified by its non-allergen, non-toxic, and antigenic nature. A molecular dynamic simulation was executed to assess the stability of the TLR2 docked structure. An immune simulation showed a high immune response toward the antigen. The protein sequence was reverse-translated, and codons were optimized to gain a high expression level in E. coli. The proposed vaccine construct may be a candidate for a multi-epitope vaccine. Experimental validation is required in future to test the safety and efficacy of the hypothetical candidate vaccine.
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