Brucella abortus HtrA functions as an authentic stress response protease but is not required for wild-type virulence in BALB/c mice.
A second mutation has recently been identified in the previously described Brucella abortus htrA mutant PHE1. As a result of this finding, a new B. abortus htrA mutant, designated RWP11, was constructed to evaluate the biological function of the Brucella HtrA protease. RWP11 is more sensitive to oxidative killing in vitro and less resistant to killing by cultured murine neutrophils and macrophages than the virulent parental strain 2308 but is not attenuated in BALB/c mice through 4 weeks postinfection. The in vitro phenotype of B. abortus RWP11 is consistent with the proposed function of bacterial HtrA proteases as components of a secondary line of defense against oxidative damage. The in vivo phenotype of this mutant, however, indicates that, unlike the corresponding Salmonella and Yersinia proteins, Brucella HtrA does not play a critical role in virulence in the mouse model.
Phillips
R W
RW
Department of Microbiology and Immunology, Louisiana State University Health Sciences Center, Shreveport, Louisiana 71130-3932, USA.
Roop
R M
RM
D000818:Animals; D002003:Brucella abortus / Q000235:genetics / Q000472:pathogenicity* / Q000502:physiology*; D002006:Brucellosis / Q000382:microbiology; D006360:Heat-Shock Proteins; D008264:Macrophages / Q000382:microbiology; D051379:Mice; D008807:Mice, Inbred BALB C; D009154:Mutation; D033903:Periplasmic Proteins; D012697:Serine Endopeptidases / Q000235:genetics* / Q000378:metabolism*; D013154:Spleen / Q000382:microbiology; D014774:Virulence
D006360:Heat-Shock Proteins; D033903:Periplasmic Proteins; C061682:DegP protease; D012697:Serine Endopeptidases