Novel lysophospholipase A secreted by Legionella pneumophila

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...

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Bibliographic Details
Published in:Journal of bacteriology Vol. 183; no. 6; pp. 2121 - 2124
Main Authors: Flieger, A, Gong, S, Faigle, M, Stevanovic, S, Cianciotto, N P, Neumeister, B
Format: Journal Article
Language:English
Published: United States American Society for Microbiology 01-03-2001
Series:Note
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Summary: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.
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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@northwestern.edu.
Present address: Department of Microbiology and Immunology, Chandler Medical Center, University of Kentucky, Lexington, KY 40536.
ISSN:0021-9193
1098-5530
DOI:10.1128/JB.183.6.2121-2124.2001