Pathogenicity of Vibrio penaeicida or white shrimp Litopenaeus vannamei: a cysteine protease-like exotoxin as a virulence factor

Type Article
Date 2005-11
Language English
Author(s) Aguirre Guzman G1, Ascencio F1, Saulnier Denis2
Affiliation(s) 1 : Ctr Invest Biol Noroeste, Unidad Patol Marina, La Paz, Baja California, Mexico.
2 : IFREMER, French Res Inst Exploitat Sea, Lab Genet & Pathol, F-17390 La Tremblade, France.
Source Diseases of aquatic organisms (0177-5103) (Inter-Research), 2005-11 , Vol. 67 , N. 3 , P. 201-207
DOI 10.3354/dao067201
WOS© Times Cited 10
Keyword(s) Pathogenicity, Exotoxin, Shrimp, Litopenaeus vannamei, Cysteine protease, Vibrio penaeicida
Abstract The pathogenicity of Vibrio penaeicida Strains KH-1 and AM101, their culture-free supernatant (CFS), and their protein fraction obtained by 40% of ammonium sulfate precipitation (PFs40) were assessed in experimental challenges against juvenile Litopenaeus vannamei. Live Vibrio cells, CFS, and PFs40 from the AM101 strain produced a significantly higher mortality (p < 0.05) compared to the KH-1 strain. Toxicity and median lethal doses (LD50) of Fast Protein Liquid Chromatography (FPLC) products were evaluated on L. vannamei. The first FPLC fraction sample (A) from PFs40 of the AM101 strain displayed LD50 values of 1.68 and 5.61 mu g protein ind.(-1), respectively. The second FPLC process from Fraction A showed a peak (A1) also with toxic effects to shrimp. PFs40, Fraction A, and Peak At showed a 38.5 kDa molecular band (SDS-PAGE), with activity on a gelatin protease zymogram. The lethal effect of PFs40 and Fraction A was inhibited by Proteinase K, CuCl2, E-64, and heat (60 and 100 degrees C) treatments, but was not inhibited by EDTA-Na-2, aprotinin, and soy trypsin treatments. These results and the zymogram inhibition test suggest the presence of a cysteine protease-like proteinaceous exotoxin as a dominant protease, secreted by V. penaeicida Strain AM101.
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