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Conserved Domains in Variable Surface Lipoproteins A-G of Mycoplasma hyorhinis May Serve as Probable Multi-Epitope Candidate Vaccine: Computational Reverse Vaccinology Approach

SIMPLE SUMMARY: In this study, we designed a multi-epitope vaccine candidate for M. hyorhinis. This is the first study using conserved regions of seven members of Vlps and has shown an effective approach toward vaccine development. The proposed vaccine candidate is highly stable and soluble. It elic...

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Detalles Bibliográficos
Autores principales: Zubair, Muhammad, Wang, Jia, Yu, Yanfei, Rasheed, Muhammad Asif, Faisal, Muhammad, Dawood, Ali Sobhy, Ashraf, Muhammad, Shao, Guoqing, Feng, Zhixin, Xiong, Qiyan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10535464/
https://www.ncbi.nlm.nih.gov/pubmed/37756079
http://dx.doi.org/10.3390/vetsci10090557
Descripción
Sumario:SIMPLE SUMMARY: In this study, we designed a multi-epitope vaccine candidate for M. hyorhinis. This is the first study using conserved regions of seven members of Vlps and has shown an effective approach toward vaccine development. The proposed vaccine candidate is highly stable and soluble. It elicits an impressive immune response and can be regarded as a hypothetical vaccine candidate in the future. Further laboratory tests and animal inoculation are required to validate vaccine efficacy and safety to combat swine infections. ABSTRACT: 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.