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

Author:

Zubair Muhammad12,Wang Jia12,Yu Yanfei1234,Rasheed Muhammad Asif5,Faisal Muhammad6,Dawood Ali Sobhy78ORCID,Ashraf Muhammad9,Shao Guoqing123,Feng Zhixin12,Xiong Qiyan12410

Affiliation:

1. Key Laboratory of Veterinary Biological Engineering and Technology, Ministry of Agriculture, Institute of Veterinary Medicine, Jiangsu Academy of Agricultural Sciences, Nanjing 210000, China

2. GuoTai (Taizhou) Center of Technology Innovation for Veterinary Biologicals, Taizhou 225300, China

3. School of Food and Biological Engineering, Jiangsu University, Zhenjiang 212013, China

4. College of Veterinary Medicine, Nanjing Agricultural University, Nanjing 210095, China

5. Department of Biosciences, COMSATS University Islamabad, Sahiwal Campus, Islamabad 45550, Pakistan

6. Division of Hematology, Department of Medicine, The Ohio State University College of Medicine, The Ohio State University Comprehensive Cancer Center, Columbus, OH 43210, USA

7. The State Key Laboratory of Agricultural Microbiology, Department of Preventive Veterinary Medicine, Huazhong Agricultural University, Wuhan 430070, China

8. Faculty of Veterinary Medicine, University of Sadat City, Sadat City 32897, Egypt

9. Institute of Microbiology, University of Agriculture Faisalabad, Faisalabad 37000, Pakistan

10. School of Life Sciences, Jiangsu University, Zhenjiang 212013, China

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.

Funder

National Key R&D program of China

Jiangsu Agricultural Science and Technology Fund

National Natural Science Foundation of China

Publisher

MDPI AG

Subject

General Veterinary

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