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Infection and Immunity, September 2001, p. 5911-5913, Vol. 69, No. 9
Department of Microbiology and Immunology, Louisiana
State University Health Sciences Center, Shreveport, Louisiana
71130-3932
Received 20 November 2000/Returned for modification 15 February
2001/Accepted 6 June 2001
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.
0019-9567/01/$04.00+0 DOI: 10.1128/IAI.69.9.5911-5913.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Brucella abortus HtrA Functions as an Authentic Stress
Response Protease but Is Not Required for Wild-Type Virulence in
BALB/c Mice
and
*
Corresponding author. Present address: Department of
Microbiology and Immunology, East Carolina University School of
Medicine, Greenville, NC 27858-4354. Phone: (252) 816-1357. Fax: (252)
816-3535. E-mail: roopr{at}mail.ecu.edu.
Present address: Department of Microbiology, University of Georgia,
Athens, GA 30602.
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