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Infection and Immunity, September 2001, p. 5911-5913, Vol. 69, No. 9
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

Robert W. Phillipsdagger and R. Martin Roop II*

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.


* 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.

dagger Present address: Department of Microbiology, University of Georgia, Athens, GA 30602.


Infection and Immunity, September 2001, p. 5911-5913, Vol. 69, No. 9
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.9.5911-5913.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



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