Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes.
Cast your vote
You can rate an item by clicking the amount of stars they wish to award to this item.
When enough users have cast their vote on this item, the average rating will also be shown.
Your vote was cast
Thank you for your feedback
Thank you for your feedback
MetadataShow full item record
AbstractLipoprotein anchoring in bacteria is mediated by the prolipoprotein diacylglyceryl transferase (Lgt), which catalyzes 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 bacterium in different eukaryotic cell lines and (ii) leads to increased release of lipoproteins into the culture supernatant. Comparative extracellular proteome analyses of the EGDe wild-type strain and the Delta lgt mutant provided 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 this proved that deletion of lgt is an excellent approach for 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 lipoprotein that is posttranslationally modified depending on PrfA. It is noteworthy that in contrast to previous studies of Escherichia coli, we unambiguously demonstrated that lipidation by Lgt is not a prerequisite for activity of the lipoprotein-specific signal peptidase II (Lsp) in Listeria.
CitationInactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes. 2007, 189 (2):313-24 J. Bacteriol.
AffiliationDepartment of Cell Biology, Helmholtz Centre for Infection Research (HZI), D-38124 Braunschweig, Germany.
JournalJournal of bacteriology
The following license files are associated with this item:
- Role of prolipoprotein diacylglyceryl transferase (Lgt) and lipoprotein-specific signal peptidase II (LspA) in localization and physiological function of lipoprotein MsmE in Streptococcus mutans.
- Authors: Arimoto T, Igarashi T
- Issue date: 2008 Dec
- Comparative proteome analysis of secretory proteins from pathogenic and nonpathogenic Listeria species.
- Authors: Trost M, Wehmhöner D, Kärst U, Dieterich G, Wehland J, Jänsch L
- Issue date: 2005 Apr
- New Listeria monocytogenes prfA* mutants, transcriptional properties of PrfA* proteins and structure-function of the virulence regulator PrfA.
- Authors: Vega Y, Rauch M, Banfield MJ, Ermolaeva S, Scortti M, Goebel W, Vázquez-Boland JA
- Issue date: 2004 Jun
- Negative control of Listeria monocytogenes virulence genes by a diffusible autorepressor.
- Authors: Ermolaeva S, Novella S, Vega Y, Ripio MT, Scortti M, Vázquez-Boland JA
- Issue date: 2004 Apr
- Lipoproteins of Listeria monocytogenes are critical for virulence and TLR2-mediated immune activation.
- Authors: Machata S, Tchatalbachev S, Mohamed W, Jänsch L, Hain T, Chakraborty T
- Issue date: 2008 Aug 1