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Journal of Bacteriology, June 2007, p. 4153-4160, Vol. 189, No. 11
0021-9193/07/$08.00+0     doi:10.1128/JB.01909-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Purification and Characterization of Mycobacterial Phospholipase A: an Activity Associated with Mycobacterial Cutinase{triangledown}

Sarah K. Parker,1* Kathryn M. Curtin,2 and Michael L. Vasil2

Department of Pediatrics,1 Department of Microbiology, University of Colorado Health Sciences Center, Aurora, Colorado 800452

Received 18 December 2006/ Accepted 12 March 2007

We describe mycobacterial phospholipase A activity (MPLA) and, using reverse genetics, have associated this activity with putative mycobacterial cutinase. PLAs, which hydrolyze fatty acids on phospholipids, play a significant role in human inflammatory states and disease pathogenesis. In prokaryotes, the recognition of their role in virulence is more recent. Cutinases are serine esterases whose primary substrate is cutin, the waxy exterior layer of plants. Mycobacterium tuberculosis has maintained seven putative cutinases, though it should not encounter cutin; we demonstrate that known cutinases and MPLA cleave phospholipids in a PLA-type manner and also hydrolyze Tween. We analyzed cutinase motifs in mycobacteria and found the motif very prevalent. All mycobacteria tested had MPLA activity. These studies suggest an alternative use for putative cutinases by the M. tuberculosis group that is likely related to MPLA activity and lipid metabolism.

* Corresponding author. Mailing address: Microbiology MS833, RC-1 P18-9403M, 12800 E. 19th Ave., P.O. Box 6511, Aurora, CO 80045. Phone: (303) 724-4244. Fax: (303) 724-4226. E-mail: sarah.parker{at}uchsc.edu

{triangledown} Published ahead of print on 6 April 2007.

Journal of Bacteriology, June 2007, p. 4153-4160, Vol. 189, No. 11
0021-9193/07/$08.00+0     doi:10.1128/JB.01909-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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