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Infection and Immunity, June 2000, p. 3569-3573, Vol. 68, No. 6
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Metalloprotease Is Not Essential for Vibrio vulnificus Virulence in Mice

Chung-Ping Shao and Lien-I Hor*

Department of Microbiology and Immunology, College of Medicine, National Cheng-Kung University, Tainan 701, Taiwan

Received 8 September 1999/Returned for modification 17 December 1999/Accepted 29 February 2000

Previous work suggested that a metalloprotease, Vvp, may be a virulence factor of Vibrio vulnificus, which causes severe wound infection and septicemia in humans. To determine the role of Vvp in pathogenesis, we isolated an isogenic protease-deficient (PD) mutant of Vibrio vulnificus by in vivo allelic exchange. This PD mutant was as virulent as its parental strain in mice infected intraperitoneally and was 10-fold more virulent in mice infected via the oral route. Furthermore, the PD mutant was indistinguishable from its parental strain in invasion from peritoneal cavity into blood stream, enhancement of vascular permeability, growth in murine blood, and utilization of hemoglobin and transferrin. These data suggest that Vvp is not essential for virulence in the mouse. However, the cytolysin activity in the culture supernatant of the PD mutant was found to be twofold higher than that of the wild-type strain and remained for a much longer period. The higher cytolysin activity of the PD mutant may be associated with the enhanced virulence in mice infected via the oral route.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, College of Medicine, National Cheng-Kung University, Tainan 701, Taiwan. Phone: 886-6-2353535, ext. 5635. Fax: 886-6-2082705. E-mail: h061453{at}mail.ncku.edu.tw.

Infection and Immunity, June 2000, p. 3569-3573, Vol. 68, No. 6
0019-9567/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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