Open AccessIn vivo and in vitro analysis of Bordetella pertussis catalase and Fe‐superoxide dismutase mutants
Author(s) -
Khelef Nadia,
DeShazer David,
Friedman Richard L.,
Guiso Nicole
Publication year - 1996
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1996.tb08435.x
Subject(s) - superoxide dismutase , bordetella pertussis , catalase , pertactin , microbiology and biotechnology , virulence , biology , in vivo , bordetella bronchiseptica , enzyme , pertussis toxin , bacteria , biochemistry , gene , signal transduction , g protein , genetics
Bordetella pertussis produces a catalase and a Fe‐superoxide dismutase. The importance of these enzymes in virulence was investigated, in vitro as well as in vivo, by using mutants deficient in their production. The catalase‐deficient mutant survived within polymorphonuclear leukocytes, killed J774A. 1 macrophages through apoptosis, and behaved as the parental strain in a murine respiratory infection model. These results suggest no direct role for catalase in B. pertussis virulence. The absence of expression of Fe‐superoxide dismutase had profound effects on the bacterium including a reduced ability to express adenylate cyclase‐hemolysin and pertactin, two factors important for B. pertussis pathogenesis. The Fe‐superoxide dismutase‐deficient mutant also had decreased abilities to colonize and persist in the murine respiratory infection model.