Identification and characterization of the Vibrio anguillarum prtV gene encoding a new metalloprotease

• Published in: Chinese journal of oceanology and limnology Vol. 28; no. 1; pp. 55 - 61
• Main Author: 莫照兰 郭东升 茅云翔 叶旭红 邹玉霞 肖鹏 郝斌
• Format: Journal Article
• Language: English
• Published: Heidelberg SP Science Press 2010; Springer Nature B.V
• Subjects: Amino acids; Animal diseases; Azocasein; Bacteria; Biology; Cloning; Earth and Environmental Science; Earth Sciences; Erythrocytes; Esterases; Fish; Gelatin; Gelatinase; Genes; Glycosidases; Marine; Marine biology; Marine fishes; Metalloproteinase; Mortality causes; Mucus; Mutants; Oceanography; Pathogenesis; Pathogens; Proteases; Proteins; PrtV gene; Scophthalmus maximus; Strain; Toxicity tests; Vibrio anguillarum; 基因编码; 大菱鲆; 突变株; 蛋白酶活性; 金属蛋白酶; 鳗弧菌; LD; proteolysis; hemolysis; mucus
• ISSN: 0254-4059; 2096-5508; 1993-5005; 2523-3521
• DOI: 10.1007/s00343-010-9246-4

We cloned and sequenced a prtV-like gene from Vibrio anguillarum M3 strain. This prtV gene encodes a putative protein of 918 amino acids, and is highly homologous to the V. cholerae prtV gene. We found that a prtV insertion mutant strain displayed lower gelatinase activity on gelatin agar, lower protease activity against azocasein, and lower activity for four glycosidases. This prtV mutant strain also had increased activity for two esterases in its extracellular products, as analyzed by the API ZYM system. In addition, the prtV mutant strain exhibited decreased growth in turbot intestinal mucus and reduced hemolytic activity on turbot erythrocytes. Infection experiments showed that the LD50 of the prtV mutant strain increased by at least 1 log compared to the wild-type in turbot fish. We propose that prtV plays an important role in the pathogenesis of V, anguillarum.