Analysis and application of a neutralizing linear epitope on liable toxin B of enterotoxin Escherichia coli

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• 作者：Weikun Guan ; Wenxin Liu ; Jun Bao ; Jinping Li…
• 关键词：LTB ; Monoclonal antibodies ; Epitope analysis ; Neutralizing activity
• 刊名：Applied Microbiology and Biotechnology
• 出版年：2015
• 出版时间：July 2015
• 年：2015
• 卷：99
• 期：14
• 页码：5985-5996
• 全文大小：2,623 KB
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• 作者单位：Weikun Guan (1)
  Wenxin Liu (1)
  Jun Bao (2) (3)
  Jinping Li (1)
  Chaowen Yuan (1)
  Jie Tang (1)
  Dongfang Shi (1) (3)
  
  1. Department of Preventive Veterinary Medicine, College of Veterinary Medicine, Northeast Agricultural University, Harbin, Heilongjiang, 150030, People鈥檚 Republic of China
  2. College of Animal Science and Technology, Northeast Agricultural University, Harbin, Heilongjiang, 150030, People鈥檚 Republic of China
  3. Synergetic Innovation Center of Food Safety and Nutrition, Northeast Agricultural University, Harbin, 150030, 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

Heat-labile enterotoxin (LT) of enterotoxigenic Escherichia coli (ETEC) is one of the major virulence factors for causing diarrhea in piglets, and LT is a strong immunogen. Thus, LT represents an important target for development of vaccines and diagnostic tests. In this study, bioinformatic tools were used to predict six antigenic B cell epitopes in the B subunit of LT protein (LTB) of ETEC strains. Then, seven antigenic B cell epitopes of LTB were identified by polyclonal antisera (polyclonal antibody (PAb)) using a set of LTB-derived peptides expressed as maltose-binding protein (MBP) fusion protein. In addition, one LTB-specific monoclonal antibody (MAb) was generated and defined its corresponding epitope as mentioned above. This MAb was able to specifically bind with native LT toxin and has no cross-reaction with LT-II (type II heat-labile enterotoxin), Stx1 (Shiga toxin I), Stx2 (Shiga toxin II), STa (heat-stable enterotoxin I), and STb (heat-stable enterotoxin II) toxins. Further, this MAb was able to interrupt LT toxin specific binding to GM1 receptor, indicating that the corresponding epitope is the specific binding region to GM1 receptor. Moreover, in vitro and in vivo assay showed that the MAb was able to neutralize the native LT toxin. Diarrheal suckling pigs challenged with LT-positive ETEC strain recovered when an enema with this purified MAb was administered. This study will provide the foundation for further studies about the interaction between LT toxin and GM1 receptor and about the developing of epitope-based vaccines and specific therapeutic agent.