1. Academic Validation
  2. Identification and epitope mapping of monoclonal antibodies against p150 protein of African swine fever virus

Identification and epitope mapping of monoclonal antibodies against p150 protein of African swine fever virus

  • Int J Biol Macromol. 2025 Oct 16;331(Pt 2):148358. doi: 10.1016/j.ijbiomac.2025.148358.
Hua Cao 1 Junhua Dong 2 Mengjia Zhang 1 Pengfei Li 1 Ahmed H Ghonaim 3 Xuexiang Yu 4 Suphot Wattanaphansak 5 Yongtao Li 6 Anan Jongkaewwattana 7 Chao Kang 8 Pan Tao 2 Qigai He 9 Wentao Li 10
Affiliations

Affiliations

  • 1 National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, 430070 Wuhan, PR China; Key Laboratory of Prevention & Control for African Swine Fever and Other Major Pig Diseases, Key Laboratory of Development of Veterinary Diagnostic Products, Ministry of Agriculture and Rural Affairs, 430070, Wuhan, PR China; Hubei Hongshan Laboratory, 430070, Wuhan, PR China.
  • 2 National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, 430070 Wuhan, PR China; Hubei Hongshan Laboratory, 430070, Wuhan, PR China.
  • 3 National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, 430070 Wuhan, PR China; Key Laboratory of Prevention & Control for African Swine Fever and Other Major Pig Diseases, Key Laboratory of Development of Veterinary Diagnostic Products, Ministry of Agriculture and Rural Affairs, 430070, Wuhan, PR China; Hubei Hongshan Laboratory, 430070, Wuhan, PR China; Desert Research Center, Cairo, 11435, Egypt.
  • 4 National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, 430070 Wuhan, PR China; Key Laboratory of Prevention & Control for African Swine Fever and Other Major Pig Diseases, Key Laboratory of Development of Veterinary Diagnostic Products, Ministry of Agriculture and Rural Affairs, 430070, Wuhan, PR China.
  • 5 Department of Veterinary Medicine, Faculty of Veterinary Science, Chulalongkorn University, Pathum Wan, Bangkok, Thailand.
  • 6 College of Veterinary Medicine, Henan Agricultural University, Zhengzhou, 450002, PR China.
  • 7 National Center for Genetic Engineering and Biotechnology, Pathum Thani, 12120, Thailand.
  • 8 National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, 430070 Wuhan, PR China.
  • 9 National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, 430070 Wuhan, PR China; Key Laboratory of Prevention & Control for African Swine Fever and Other Major Pig Diseases, Key Laboratory of Development of Veterinary Diagnostic Products, Ministry of Agriculture and Rural Affairs, 430070, Wuhan, PR China. Electronic address: he628@mail.hzau.edu.cn.
  • 10 National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, 430070 Wuhan, PR China; Key Laboratory of Prevention & Control for African Swine Fever and Other Major Pig Diseases, Key Laboratory of Development of Veterinary Diagnostic Products, Ministry of Agriculture and Rural Affairs, 430070, Wuhan, PR China; Hubei Hongshan Laboratory, 430070, Wuhan, PR China; Frontiers Science Center for Animal Breeding and Sustainable Production, Wuhan, Hubei, 430070, PR China; Hubei Jiangxia Laboratory, Wuhan, Hubei, 430070, PR China. Electronic address: wentao@mail.hzau.edu.cn.
Abstract

African swine fever (ASF) is an acute and highly contagious disease caused by the African swine fever virus (ASFV) that poses a significant threat to domestic pigs and wild boars worldwide. The ASFV pp220 polyprotein plays a critical role in maintaining the structural integrity of the viral particle. The p150 protein, a cleavage product of pp220, is the second most abundant viral particle protein after the major capsid protein p72. In this study, monoclonal antibodies (mAbs) were produced using inactivated ASFV particles as the immunogen. Seven monoclonal antibodies targeting the ASFV-p150 protein were successfully generated, all exhibiting strong reactivity with ASFV. Using phage display technology, we mapped the epitope recognized by antibody 20D5, identifying the key binding region as Amino acids 975-996 (NVIYQHFNLEYGEQEATKKALI). Moreover, this epitope was recognized by ASFV-positive sera, suggesting it is a naturally occurring linear B-cell epitope. Conservation analysis showed that this epitope is highly conserved in genotype I and II ASFV endemic strains. These findings enhance the understanding of p150 antigenicity and provide a basis for developing improved ASFV diagnostic tools and future vaccines.

Keywords

African swine fever virus (ASFV); Antibody; CP2475L; p150 protein.

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