Research

pagP is required for resistance to antibody-mediated complement lysis during Bordetella bronchiseptica respiratory infection


Reference:

Pilione, M. R., Pishko, E. J., Preston, A., Maskell, D. J. and Harvill, E. T., 2004. pagP is required for resistance to antibody-mediated complement lysis during Bordetella bronchiseptica respiratory infection. Infection and Immunity, 72 (5), pp. 2837-2842.

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Official URL:

http://dx.doi.org/10.1128/​IAI.72.5.2837-2842.2004

Abstract

To efficiently colonize and persist in the lower respiratory tract, bacteria must survive multiple host immune mechanisms. Bordetella bronchiseptica is a gram-negative respiratory pathogen that naturally infects mice and persists in the lower respiratory tract for up to 49 days postinoculation. In this work, we examined the effect of mutation of the pagP gene on the persistence of B. bronchiseptica in the lower respiratory tract of mice. The pagP gene encodes a palmitoyl transferase that is responsible for the addition of a palmitoyl group to the lipid A region of B. bronchiseptica lipopolysaccharide. Data presented here confirm that a B. bronchiseptica deltapagP mutant demonstrates defective persistence in the lower respiratory tract of wild-type mice. We hypothesized that the defective persistence of the B. bronchiseptica deltapagP mutant was due to an increased susceptibility of this mutant to a host immune response. In vivo data indicate that both B cells and the complement component C3 are required for the reduced bacterial numbers of the deltapagP mutant on day 14 postinoculation. In addition, an in vitro complement killing assay demonstrated that B. bronchiseptica exhibits pagP-dependent resistance to antibody-mediated complement killing at low concentrations of immune serum. Taken together, these results suggest that pagP is required for B. bronchiseptica to resist antibody-mediated complement lysis during respiratory infection.

Details

Item Type Articles
CreatorsPilione, M. R., Pishko, E. J., Preston, A., Maskell, D. J. and Harvill, E. T.
DOI10.1128/​IAI.72.5.2837-2842.2004
DepartmentsFaculty of Science > Biology & Biochemistry
RefereedYes
StatusPublished
ID Code32664

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