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Screening for a single-chain variable-fragment antibody that can effectively neutralize the cytotoxicity of the Vibrio parahaemolyticus thermolabile hemolysin.
Wang, Rongzhi; Fang, Sui; Wu, Dinglong; Lian, Junwei; Fan, Jue; Zhang, Yanfeng; Wang, Shihua; Lin, Wenxiong.
Affiliation
  • Wang R; The Ministry of Education Key Laboratory of Biopesticide and Chemical Biology and the College of Life Sciences, Fujian Agriculture and Forestry University, Fuzhou, China.
Appl Environ Microbiol ; 78(14): 4967-75, 2012 Jul.
Article in En | MEDLINE | ID: mdl-22562997
Vibrio parahaemolyticus is a halophilic bacterium that is widely distributed in water resources. The bacterium causes lethal food-borne diseases and poses a serious threat to human and animal health all over the world. The major pathogenic factor of V. parahaemolyticus is thermolabile hemolysin (TLH), encoded by the tlh gene, but its toxicity mechanisms are unknown. A high-affinity antibody that can neutralize TLH activity effectively is not available. In this study, we successfully expressed and purified the TLH antigen and discovered a high-affinity antibody to TLH, named scFv-LA3, by phage display screening. Cytotoxicity analysis showed that scFv-LA3 has strong neutralization effects on TLH-induced cell toxicity.
Subject(s)

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Vibrio parahaemolyticus / Antibodies, Neutralizing / Single-Chain Antibodies / Hemolysin Proteins Type of study: Diagnostic_studies / Screening_studies Limits: Animals / Humans Language: En Journal: Appl Environ Microbiol Year: 2012 Document type: Article Affiliation country: China Country of publication: United States

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Bacterial Proteins / Vibrio parahaemolyticus / Antibodies, Neutralizing / Single-Chain Antibodies / Hemolysin Proteins Type of study: Diagnostic_studies / Screening_studies Limits: Animals / Humans Language: En Journal: Appl Environ Microbiol Year: 2012 Document type: Article Affiliation country: China Country of publication: United States