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Journal of Bacteriology, May 1999, p. 3114-3122, Vol. 181, No. 10
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Molecular Characterization of KatY (Antigen 5), a Thermoregulated Chromosomally Encoded Catalase-Peroxidase of Yersinia pestis

Emilio Garcia,1 Yuri A. Nedialkov,2,dagger Jeffrey Elliott,1 Vladimir L. Motin,2,Dagger and Robert R. Brubaker2,*

Human Genome Center, Lawrence Livermore Laboratory, Livermore, California 94550,1 and Department of Microbiology, Michigan State University, East Lansing, Michigan 488242

Received 11 December 1998/Accepted 8 March 1999

The first temperature-dependent proteins (expressed at 37°C, but not 26°C) to be identified in Yersinia pestis were antigens 3 (fraction 1), 4 (pH 6 antigen), and 5 (hereafter termed KatY). Antigens 3 and 4 are now established virulence factors, whereas little is known about KatY, except that it is encoded chromosomally, produced in abundance, possesses modest catalase activity, and is shared by Yersinia pseudotuberculosis, but not Yersinia enterocolitica. We report here an improved chromatographic method (DEAE-cellulose, calcium hydroxylapatite, and Sephadex G-150) that yields enzymatically active KatY (2,423 U/mg of protein). Corresponding mouse monoclonal antibody 1B70.1 detected plasminogen activator-mediated hydrolysis of KatY, and a polyclonal rabbit antiserum raised against outer membranes of Y. pestis was enriched for anti-KatY. A sequenced ~16-kb Y. pestis DNA insert of a positive pLG338 clone indicated that katY encodes an 81.4-kDa protein (pI 6.98) containing a leader sequence of 2.6 kDa; the deduced molecular mass and pI of processed KatY were 78.8 kDa and 6.43, respectively. A minor truncated variant (predicted molecular mass of 53.6 kDa) was also expressed. KatY is similar (39 to 59% identity) to vegetative bacterial catalase-peroxidases (KatG in Escherichia coli) and is closely related to plasmid-encoded KatP of enterohemorrhagic E. coli O157:H7 (75% identity). katY encoded a putative Ca2+-binding site, and its promoter contained three homologues to the consensus recognition sequence of the pCD-encoded transcriptional activator LcrF. rbsA was located upstream of katY, and cybB, cybC, dmsABC, and araD were mapped downstream. These genes are not linked to katG or katP in E. coli.

* Corresponding author. Mailing address: Department of Microbiology, 57 Giltner Hall, Michigan State University, East Lansing, MI 48824-1101. Phone: (517) 355-6466. Fax: (517) 353-8957. E-mail: brubake3{at}pilot.msu.edu.

dagger Present address: Department of Biochemistry, Michigan State University, East Lansing, MI 48824.

Dagger Present address: Human Genome Center, Lawrence Livermore Laboratory, Livermore, CA 94550.

Journal of Bacteriology, May 1999, p. 3114-3122, Vol. 181, No. 10
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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