ArticleInfection and immunity1998
Modulation of enzymatic activity and biological function of Listeria monocytogenes broad-range phospholipase C by amino acid substitutions and by replacement with the Bacillus cereus ortholog.
Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
16 citing papers in PubMed, 34 citations in OpenAlex.
- Structural basis for the unique molecular properties of broad-range phospholipase C from Listeria monocytogenes.Nature communications · 2023Article
- Molecular Cloning and Characterization of a SerotoninInternational journal of environmental research and public health · 2023Article
- Bacterial phospholipases C with dual activity: phosphatidylcholinesterase and sphingomyelinase.FEBS open bio · 2021Review
- Life without air.The Journal of biological chemistry · 2020Article
- Actin-based motility allows Listeria monocytogenes to avoid autophagy in the macrophage cytosol.Cellular microbiology · 2018Article
- Article
- Bacterial Sphingomyelinases and Phospholipases as Virulence Factors.Microbiology and molecular biology reviews : MMBR · 2016Review
- Recombinant broad-range phospholipase C from Listeria monocytogenes exhibits optimal activity at acidic pH.Biochimica et biophysica acta · 2016Article
- Protein transport across the cell wall of monoderm Gram-positive bacteria.Molecular microbiology · 2012Review
- Differentiation of propeptide residues regulating the compartmentalization, maturation and activity of the broad-range phospholipase C of Listeria monocytogenes.The Biochemical journal · 2010Article
- Characterization of Listeria monocytogenes expressing anthrolysin O and phosphatidylinositol-specific phospholipase C from Bacillus anthracis.Infection and immunity · 2005Article
- The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C.Journal of bacteriology · 2005Article
- Cross-species surface display of functional spirochetal lipoproteins by recombinant Borrelia burgdorferi.Infection and immunity · 2004Article
- Requirement of the Listeria monocytogenes broad-range phospholipase PC-PLC during infection of human epithelial cells.Journal of bacteriology · 2003Article
- Activation of host phospholipases C and D in macrophages after infection with Listeria monocytogenes.Infection and immunity · 2000Article
- pH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes.Molecular microbiology · 2000Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The secreted broad-range phosphatidylcholine (PC)-preferring phospholipase C (PC-PLC) of Listeria monocytogenes plays a role in the bacterium's ability to escape from phagosomes and spread from cell to cell. Based on comparisons with two orthologs, Clostridium perfringens alpha-toxin and Bacillus cereus PLC (PLCBc), we generated PC-PLC mutants with altered enzymatic activities and substrate specificities and analyzed them for biological function in tissue culture and mouse models of infection. Two of the conserved active-site zinc-coordinating histidines were confirmed by single amino acid substitutions H69G and H118G, which resulted in proteins inactive in broth culture and unstable intracellularly. Substitutions D4E and H56Y remodeled the PC-PLC active site to more closely resemble the PLCBc active site, while a gene replacement resulted in L. monocytogenes secreting PLCBc. All of these mutants yielded similar amounts of active enzyme as wild-type PC-PLC both in broth culture and intracellularly. D4E increased activity on and specificity for PC, while H56Y and D4E H56Y showed higher activity on both PC and sphingomyelin, with reduced specificity for PC. As expected, PLCBc expressed by L. monocytogenes was highly specific for PC. During early intracellular growth in human epithelial cells, the D4E mutant and the PLCBc-expressing strain performed significantly better than the wild type, while the H56Y and D4E H56Y mutants showed a significant defect. In assays for cell-to-cell spread, the H56Y and D4E mutants had close to wild-type characteristics, while the spreading efficiency of PLCBc was significantly lower. These studies emphasize the species-specific features of PC-PLC important for growth in mammalian cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.