ArticleJournal of bacteriology2007
Inactivation of Lgt allows systematic characterization of lipoproteins from Listeria monocytogenes.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 91 citations in OpenAlex.
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- Functional and genomic profiling of lactic acid bacteria reveals specific traits as potential probiotics.Frontiers in microbiology · 2026Article
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- Identification of genetic elements required forFrontiers in microbiology · 2022Article
- Breaking down the cell wall: Still an attractive antibacterial strategy.Frontiers in microbiology · 2022Review
- NisI Maturation and Its Influence on Nisin Resistance in Lactococcus lactis.Applied and environmental microbiology · 2020Article
- TLR2 and endosomal TLR-mediated secretion of IL-10 and immune suppression in response to phagosome-confined Listeria monocytogenes.PLoS pathogens · 2020Article
- Orchestration of human macrophage NLRP3 inflammasome activation byProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Serotype-Independent Protection Against Invasive Pneumococcal Infections Conferred by Live Vaccine WithFrontiers in immunology · 2019Article
- Lipoproteins of Gram-Positive Bacteria: Key Players in the Immune Response and Virulence.Microbiology and molecular biology reviews : MMBR · 2016Review
- A structural comparison of Listeria monocytogenes protein chaperones PrsA1 and PrsA2 reveals molecular features required for virulence.Molecular microbiology · 2016Article
- Evaluation of Staphylococcus aureus Lipoproteins: Role in Nutritional Acquisition and Pathogenicity.Frontiers in microbiology · 2016Article
- T(H)17-Mediated Protection against Pneumococcal Carriage by a Whole-Cell Vaccine Is Dependent on Toll-Like Receptor 2 and Surface Lipoproteins.Clinical and vaccine immunology : CVI · 2015Article
- Identification of a peptide-pheromone that enhances Listeria monocytogenes escape from host cell vacuoles.PLoS pathogens · 2015Article
- Article
- Genetic redundancy, proximity, and functionality of lspA, the target of antibiotic TA, in the Myxococcus xanthus producer strain.Journal of bacteriology · 2014Article
- Listeria monocytogenes virulence factor secretion: don't leave the cell without a chaperone.Frontiers in cellular and infection microbiology · 2014Review
- How Listeria monocytogenes organizes its surface for virulence.Frontiers in cellular and infection microbiology · 2014Review
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lipoprotein 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.
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