Identification of two novel rabbit hemorrhagic disease virus (RHDV) B cell epitopes and evaluation of its immunoprotection against RHDV

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• 作者：Kong DeSheng ; Liu HuaiRan ; Liu JiaSen ; Yu Zuo…
• 关键词：Rabbit hemorrhagic disease virus ; VP60 protein monoclonal antibody ; Epitope immunogenicity
• 刊名：Applied Microbiology and Biotechnology
• 出版年：2015
• 出版时间：July 2015
• 年：2015
• 卷：99
• 期：14
• 页码：5951-5966
• 全文大小：902 KB
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• 作者单位：Kong DeSheng (1)
  Liu HuaiRan (1)
  Liu JiaSen (1)
  Yu Zuo (1)
  Jiang Qian (1)
  Guo DongChun (1)
  Hu XiaoLiang (1)
  Wang FengJie (1)
  Huang QianQian (1)
  Qu LianDong (1)
  
  1. Zoonosis of Natural Foci, State Key Laboratory of Veterinary Biotechnology, Harbin Vet Res Institute, Chinese Academy of Agricultural Sciences, 427 Maduan Street, Nangang District, Harbin, 150001, People鈥檚 Republic of China
  
• 刊物类别：Chemistry and Materials Science
• 刊物主题：Chemistry
  Biotechnology
  Microbiology
  Microbial Genetics and Genomics
  
• 出版者：Springer Berlin / Heidelberg
• ISSN：1432-0614

文摘

The VP60 protein of rabbit hemorrhagic disease virus (RHDV) is a structural protein with important roles in viral replication and assembly. In this study, we immunized BALB/c mice with the RHDV-TP strain. Six monoclonal antibodies (mAbs) were selected and characterized by enzyme-linked immunosorbent assay, Western blotting, and indirectly immunofluorescence analysis (IFA). All six mAbs (AD4, AG10, BC9, BE8, BH3, and DE2) had positive reactions with recombinant VP60 as analyzed by IFA, but only two (AG10 and DE2) reacted with denatured RHDV by Western blotting. Fifty-four partially overlapping fragments of the VP60 gene were expressed with His or Glutathione S-transferase (GST) tags to identify the epitopes recognized by AG10 and DE2. These two epitopes were located at the C-terminal of VP60 and were longer (64 and 53 amino acids, respectively) than normal B cell epitopes. However, both AG10 and DE2 also interacted with RHDV2 VP60 expressed in insect cells. Amino acid alignments of the AG10 and DE2 epitope regions between RHDV and RHDV2 VP60 indicated several mutations, suggesting that the epitopes recognized by the mAbs AG10 and DE2 were discontinuous. Epitope immunogenicity was evaluated by inoculating specific pathogen-free rabbits with saline, purified DE2 epitope, or RHDV inactive vaccine. Rabbits immunized with the DE2 epitope developed high levels of RHDV-specific antibodies but no cellular immune response and died after challenge with RHDV-HYD isolate. Despite their lack of neutralizing activity, these mAb reagents and epitopes may have useful clinical applications and will be valuable tools in further studies of the structure and function of the RHDV VP60 protein.