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Gene Review

plcB  -  phospholipase C

Listeria monocytogenes serotype 4b str. F2365

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Disease relevance of plcB

  • Listeria monocytogenes Mutants Carrying Newcastle Disease Virus F Gene Fused to its actA and plcB: In vitro Expression and Immunogenicity in Chickens [1].
  • In the present study, we characterized the mechanisms of enhanced E-selectin expression using L. monocytogenes wild type (EGD), the isogenic in-frame deletion mutants for phosphatidylcholine (PC)- and phosphatidylinositol (PI)-specific phospholipases EGD delta plcA and EGD delta plcB, as well as the nonvirulent control strain Listeria innocua [2].
  • The lecithinase gene of the intracellular pathogen Listeria monocytogenes, plcB, was identified in a 5,648-bp DNA fragment which expressed lecithinase activity when cloned into Escherichia coli [3].
  • Phospholipase C plays a key role in the pathogenesis of several bacterial infections, for example, those caused by Clostridium perfringens and Listeria monocytogenes [4].

High impact information on plcB

  • Infection of endothelial cells with EGD delta plcA or EGD delta plcB for 6 h induced, as compared with EGD wild type, intermediate levels of E-selectin mRNA and protein as well as PMN rolling and adhesion at a shear rate of 1 dyne/cm2, indicating that both bacterial phospholipases are required for a maximal effect [2].
  • Escape from these vacuoles is mediated in part by a bacterial phospholipase C (PC-PLC), whose activation requires cleavage of an N-terminal peptide [5].
  • A mutant of Listeria monocytogenes EGD was constructed that carries an extended deletion removing the entire PrfA-regulated gene cluster from plcA to plcB and a second deletion inactivating the inlA gene [6].
  • Compartmentalization of the Broad-Range Phospholipase C Activity to the Spreading Vacuole Is Critical for Listeria monocytogenes Virulence [7].
  • Membrane fusion induced by the catalytic activity of a phospholipase C/sphingomyelinase from Listeria monocytogenes [8].

Chemical compound and disease context of plcB

  • Subcytolytic concentrations of phospholipase C can perturb host cells by activating the arachidonic acid cascade or protein kinase C. Nonlethal phospholipases C, such as the Listeria monocytogenes PLC-A, appear to enhance the release of the organism from the host cell phagosome [9].

Biological context of plcB

  • Given the pathogenic potential of L. monocytogenes, we created an attenuated mutant strain bearing double deletions in the actA and plcB virulence genes for an initial clinical safety study of a prototype L. monocytogenes vector in adults [10].
  • We assessed the effect of carbohydrates on virulence gene expression in a panel of wild-type isolates of L. monocytogenes by using the PrfA-dependent phospholipase C gene plcB as a reporter [11].
  • Diheptanoylphosphatidyl-2-O-methylinositol is a good inhibitor of PI-specific phospholipase C because it blocks the initial phosphotransferase step in PI hydrolysis [12].
  • Listeria monocytogenes phospholipase C-dependent calcium signaling modulates bacterial entry into J774 macrophage-like cells [13].
  • DNA sequences of M. kansasii and M. marinum homologous to the genes encoding phospholipase C from M. tuberculosis and M. ulcerans were identified by DNA-DNA hybridization and sequencing [4].

Anatomical context of plcB


Associations of plcB with chemical compounds

  • The bacterium secretes a phospholipase C (PLC(LM)) that is active on glycerophospholipids, e.g., phosphatidylcholine, and on sphingomyelin; thus, PLC(LM) should be described more appropriately as a phospholipase C/sphingomyelinase [8].
  • Modeling of the 2-O-methylinositol derivative suggests that the methyl group blocks one side of the phosphate, consistent with the observation that nonspecific phospholipase C enzymes which are able to hydrolyze PI, albeit poorly, are unable to hydrolyze diheptanoylphosphatidyl-2-O-methylinositol [12].
  • By using the hly-based system as an in vivo expression technology tool, nine in vivo-induced loci of L. monocytogenes were identified, including genes encoding (i) the previously known in vivo-inducible phosphatidylinositol phospholipase C and (ii) a putative N-acetylglucosamine epimerase, possibly involved in teichoic acid biosynthesis [19].
  • Chromogenic media are based on both the specific chromogenic detection of phosphatidylinositol phospholipase C and the xylose fermentation and give specific and direct identification of L. monocytogenes and L. ivanovii [20].

Other interactions of plcB

  • NDV F or its truncated fragment Fa was used as the model heterologous gene to be integrated into actA or plcB downstream of their signal sequences [1].
  • In order to avoid a possible failure in the detection of virulent L. monocytogenes, a one-step procedure which enabled demonstration of three virulence-associated genes, prfA, hlyA, and plcB, simultaneously in a single PCR mixture was developed [21].
  • All L. monocytogenes isolates tested positive for the presence of 3 major virulence factors (hlyA, inlB, and plcB) [22].
  • Significantly decreased transcription of the plcA gene, encoding a phospholipase C involved in vacuolar escape and cell-to-cell spread, was observed in acid-adapted bacteria [23].

Analytical, diagnostic and therapeutic context of plcB

  • Western immunoblot analysis using a rabbit immune serum raised against the enzyme showed that all virulent strains of L. monocytogenes tested produced in the culture supernatant a 29-kDa PLC [24].
  • Detection of phospholipase C enzymatic activity was carried out using thin-layer chromatography to detect diglycerides in the hydrolysates of radiolabeled phosphatidylcholine [4].


  1. Listeria monocytogenes Mutants Carrying Newcastle Disease Virus F Gene Fused to its actA and plcB: In vitro Expression and Immunogenicity in Chickens. Jiang, L., Ke, C., Xu, J., Chen, J., Chen, X., Chen, N., Shuai, J., Fang, W. Acta Biochim. Biophys. Sin. (Shanghai) (2007) [Pubmed]
  2. Two distinct phospholipases C of Listeria monocytogenes induce ceramide generation, nuclear factor-kappa B activation, and E-selectin expression in human endothelial cells. Schwarzer, N., Nöst, R., Seybold, J., Parida, S.K., Fuhrmann, O., Krüll, M., Schmidt, R., Newton, R., Hippenstiel, S., Domann, E., Chakraborty, T., Suttorp, N. J. Immunol. (1998) [Pubmed]
  3. Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread. Vazquez-Boland, J.A., Kocks, C., Dramsi, S., Ohayon, H., Geoffroy, C., Mengaud, J., Cossart, P. Infect. Immun. (1992) [Pubmed]
  4. Detection of phospholipase C in nontuberculous mycobacteria and its possible role in hemolytic activity. Gomez, A., Mve-Obiang, A., Vray, B., Rudnicka, W., Shamputa, I.C., Portaels, F., Meyers, W.M., Fonteyne, P.A., Realini, L. J. Clin. Microbiol. (2001) [Pubmed]
  5. pH-regulated activation and release of a bacteria-associated phospholipase C during intracellular infection by Listeria monocytogenes. Marquis, H., Hager, E.J. Mol. Microbiol. (2000) [Pubmed]
  6. A new PrfA-regulated gene of Listeria monocytogenes encoding a small, secreted protein which belongs to the family of internalins. Engelbrecht, F., Chun, S.K., Ochs, C., Hess, J., Lottspeich, F., Goebel, W., Sokolovic, Z. Mol. Microbiol. (1996) [Pubmed]
  7. Compartmentalization of the Broad-Range Phospholipase C Activity to the Spreading Vacuole Is Critical for Listeria monocytogenes Virulence. Yeung, P.S., Na, Y., Kreuder, A.J., Marquis, H. Infect. Immun. (2007) [Pubmed]
  8. Membrane fusion induced by the catalytic activity of a phospholipase C/sphingomyelinase from Listeria monocytogenes. Montes, L.R., Goñi, F.M., Johnston, N.C., Goldfine, H., Alonso, A. Biochemistry (2004) [Pubmed]
  9. Bacterial phospholipases C. Titball, R.W. Microbiol. Rev. (1993) [Pubmed]
  10. Safety and shedding of an attenuated strain of Listeria monocytogenes with a deletion of actA/plcB in adult volunteers: a dose escalation study of oral inoculation. Angelakopoulos, H., Loock, K., Sisul, D.M., Jensen, E.R., Miller, J.F., Hohmann, E.L. Infect. Immun. (2002) [Pubmed]
  11. The bvr locus of Listeria monocytogenes mediates virulence gene repression by beta-glucosides. Brehm, K., Ripio, M.T., Kreft, J., Vázquez-Boland, J.A. J. Bacteriol. (1999) [Pubmed]
  12. Short-chain phosphatidylinositol conformation and its relevance to phosphatidylinositol-specific phospholipase C. Zhou, C., Garigapati, V., Roberts, M.F. Biochemistry (1997) [Pubmed]
  13. Listeria monocytogenes phospholipase C-dependent calcium signaling modulates bacterial entry into J774 macrophage-like cells. Wadsworth, S.J., Goldfine, H. Infect. Immun. (1999) [Pubmed]
  14. Examination of Listeria monocytogenes intracellular gene expression by using the green fluorescent protein of Aequorea victoria. Freitag, N.E., Jacobs, K.E. Infect. Immun. (1999) [Pubmed]
  15. The broad-range phospholipase C and a metalloprotease mediate listeriolysin O-independent escape of Listeria monocytogenes from a primary vacuole in human epithelial cells. Marquis, H., Doshi, V., Portnoy, D.A. Infect. Immun. (1995) [Pubmed]
  16. The metalloprotease of Listeria monocytogenes controls cell wall translocation of the broad-range phospholipase C. Yeung, P.S., Zagorski, N., Marquis, H. J. Bacteriol. (2005) [Pubmed]
  17. Phospholipase C in Listeria. Mencíková, E. Acta Microbiol. Hung. (1989) [Pubmed]
  18. Isolation of pathogenic Listeria monocytogenes in faeces of wild animals in captivity. Kalorey, D.R., Kurkure, N.V., Warke, S.R., Rawool, D.B., Malik, S.V., Barbuddhe, S.B. Comp. Immunol. Microbiol. Infect. Dis. (2006) [Pubmed]
  19. Listeriolysin O as a reporter to identify constitutive and in vivo-inducible promoters in the pathogen Listeria monocytogenes. Dubail, I., Berche, P., Charbit, A. Infect. Immun. (2000) [Pubmed]
  20. Listeria: growth, phenotypic differentiation and molecular microbiology. Allerberger, F. FEMS Immunol. Med. Microbiol. (2003) [Pubmed]
  21. Detection of multiple virulence-associated genes of Listeria monocytogenes by PCR in artificially contaminated milk samples. Cooray, K.J., Nishibori, T., Xiong, H., Matsuyama, T., Fujita, M., Mitsuyama, M. Appl. Environ. Microbiol. (1994) [Pubmed]
  22. Effectiveness of steam pasteurization in controlling microbiological hazards of cull cow carcasses in a commercial plant. Corantin, H., Quessy, S., Gaucher, M.L., Lessard, L., Leblanc, D., Houde, A. Can. J. Vet. Res. (2005) [Pubmed]
  23. Effect of acid adaptation on the fate of Listeria monocytogenes in THP-1 human macrophages activated by gamma interferon. Conte, M.P., Petrone, G., Di Biase, A.M., Longhi, C., Penta, M., Tinari, A., Superti, F., Fabozzi, G., Visca, P., Seganti, L. Infect. Immun. (2002) [Pubmed]
  24. Purification and characterization of an extracellular 29-kilodalton phospholipase C from Listeria monocytogenes. Geoffroy, C., Raveneau, J., Beretti, J.L., Lecroisey, A., Vazquez-Boland, J.A., Alouf, J.E., Berche, P. Infect. Immun. (1991) [Pubmed]
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