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J. Bacteriol. doi:10.1128/JB.00976-06
Copyright (c) 2006, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes

Maja Baumgärtner, Uwe Kärst, Birgit Gerstel, Martin Loessner, Jürgen Wehland, and Lothar Jänsch*

Department of Cell Biology, Helmholtz Centre for Infection Research (HZI), Inhoffenstra{beta}e 7, D-38124 Braunschweig, Germany; Institut für Lebensmittel-u.Ernährungswissenschaften, ETH-Zentrum, Schmelzbergstrasse 9, CH-8092 Zürich, Switzerland

* To whom correspondence should be addressed. Email: lothar.jaensch{at}helmholtz-hzi.de.


  Abstract

Lipoprotein anchoring in bacteria is mediated by the prolipoprotein diacylglyceryl transferase (Lgt), which catalyses the transfer of a diacylglyceryl moiety to the prospective N-terminal cysteine of the mature lipoprotein. Deletion of the lgt gene in the Gram-positive pathogen Listeria monocytogenes (i) impairs intracellular growth of the bacteria in different eukaryotic cell lines and (ii) leads to an increased release of lipoproteins into the culture supernatant. Comparative extracellular proteome analyses of the EGDe wild-type and the {Delta}lgt mutant provide systematic insight into the relative expression of lipoproteins. Twenty-six of the 68 predicted lipoproteins were specifically released into the extracellular proteome of the {Delta}lgt strain and proved deletion of lgt is an excellent approach for the experimental verification of listerial lipoproteins. Consequently, we generated {Delta}lgt/{Delta}prfA double mutants to detect lipoproteins belonging to the main virulence regulon that is controlled by PrfA. Overall we identified three lipoproteins whose extracellular levels are regulated and one that is post-translational modified by PrfA. Noteworthy, in contrast to earlier studies in E. coli we unambiguously demonstrated that lipidation by Lgt is not a prerequisite for activity of the lipoprotein-specific signal peptidase II (Lsp) in Listeria.




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