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Journal of Bacteriology, September 2007, p. 6580-6586, Vol. 189, No. 18
0021-9193/07/$08.00+0     doi:10.1128/JB.00809-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

MglA Regulates Francisella tularensis subsp. novicida (Francisella novicida) Response to Starvation and Oxidative Stress{triangledown} ,{dagger}

Tina Guina,1* Dragan Radulovic,2* Arya J. Bahrami,1 Diana L. Bolton,1 Laurence Rohmer,3 Kendan A. Jones-Isaac,1 Jinzy Chen,4 Larry A. Gallagher,3 Byron Gallis,4 Soyoung Ryu,4 Greg K. Taylor,4 Mitchell J. Brittnacher,3 Colin Manoil,3 and David R. Goodlett4

Department of Pediatrics, Division of Infectious Diseases,1 Department of Medicinal Chemistry,4 Department of Genome Sciences, University of Washington, Seattle, Washington,3 Department of Mathematics, Florida Atlantic University, Boca Raton, Florida2

Received 24 May 2007/ Accepted 3 July 2007

MglA is a transcriptional regulator of genes that contribute to the virulence of Francisella tularensis, a highly infectious pathogen and the causative agent of tularemia. This study used a label-free shotgun proteomics method to determine the F. tularensis subsp. novicida (F. novicida) proteins that are regulated by MglA. The differences in relative protein amounts between wild-type F. novicida and the mglA mutant were derived directly from the average peptide precursor ion intensity values measured with the mass spectrometer by using a suite of mathematical algorithms. Among the proteins whose relative amounts changed in an F. novicida mglA mutant were homologs of oxidative and general stress response proteins. The F. novicida mglA mutant exhibited decreased survival during stationary-phase growth and increased susceptibility to killing by superoxide generated by the redox-cycling agent paraquat. The F. novicida mglA mutant also showed increased survival upon exposure to hydrogen peroxide, likely due to increased amounts of the catalase KatG. Our results suggested that MglA coordinates the stress response of F. tularensis and is likely essential for bacterial survival in harsh environments.

* Corresponding author. Mailing address for Tina Guina (correspondent for biological experiments and protein annotation): Department of Pediatrics, Division of Infectious Diseases, University of Washington, Seattle, WA. Phone: (206) 616-3468. Fax: (206) 543-5383. E-mail: tguina{at}u.washington.edu. Mailing address for Dragan Radulovic (correspondent for mathematical algorithm for determination of relative peptide abundance): Department of Mathematics, Florida Atlantic University, Boca Raton, FL. Phone: (561) 297-3346. Fax: (561) 297-2436. E-mail: radulovi{at}fau.edu

{triangledown} Published ahead of print on 20 July 2007.

{dagger} Supplemental material for this article may be found at http://www.jb.asm.org/.

Journal of Bacteriology, September 2007, p. 6580-6586, Vol. 189, No. 18
0021-9193/07/$08.00+0     doi:10.1128/JB.00809-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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