Novel lysophospholipase a secreted by Legionella pneumophila

A. Flieger*, S. Gong, M. Faigle, S. Stevanovic, N. P. Cianciotto, B. Neumeister

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

43 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)2121-2124
Number of pages4
JournalJournal of bacteriology
Volume183
Issue number6
DOIs
StatePublished - 2001

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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