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Journal of Bacteriology, March 2001, p. 2121-2124, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.2121-2124.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Novel Lysophospholipase A Secreted by Legionella pneumophila

Antje Flieger,1,2,* Shimei Gong,1,dagger Marion Faigle,1 Stefan Stevanovic,3 Nicholas P. Cianciotto,2 and Birgid Neumeister1

Abteilung für Transfusionsmedizin, Universitätsklinikum Tübingen,1 and Interfakultäres Institut für Zellbiologie, Abteilung Immunologie, Universität Tübingen,3 D-72076 Tübingen, Germany, and Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, Illinois 606112

Received 21 September 2000/Accepted 13 December 2000

We show that Legionella pneumophila possesses lysophospholipase A activity, which releases fatty acids from lysophosphatidylcholine. The NH2-terminal sequence of the enzyme contained FGDSLS, corresponding to a catalytic domain in a recently described group of lipolytic enzymes. Culture supernatants of a L. pneumophila pilD mutant lost the ability to cleave lysophosphatidylcholine.

* Corresponding author. Mailing address: Department of Microbiology-Immunology, Northwestern University Medical School, Searle 6-573, 320 E Superior St., Chicago, IL 60611. Phone: 001-312-503-1034. Fax: 001-312-503-1339. E-mail: a-flieger{at}northwestern.edu.

dagger Present address: Department of Microbiology and Immunology, Chandler Medical Center, University of Kentucky, Lexington, KY 40536.

Journal of Bacteriology, March 2001, p. 2121-2124, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.2121-2124.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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