Expression of mptC of Listeria monocytogenes induces sensitivity to class IIa bacteriocins in Lactococcus lactis

Ramnath, Manilduth; Arous, Safia; Gravesen, Anne; Hastings, John W.; Héchard, Yann

doi:10.1099/mic.0.27002-0

Cited by 93 publications

(80 citation statements)

References 24 publications

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“…As IIC and IID subunits are probably present in the membrane, they are candidates as targets of class IIa bacteriocins. Finally, the mptACD operon of L. monocytogenes was heterologously expressed in an insensitive species, Lactococcus lactis (153). Upon induction of the mpt operon, the recombinant Lactococcus lactis became sensitive to various class IIa bacteriocins.…”

Section: Mode Of Action At the Molecular Levelmentioning

confidence: 99%

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The Continuing Story of Class IIa Bacteriocins

Drider

Fimland

Héchard

et al. 2006

Microbiol Mol Biol Rev

646

543

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SUMMARY Many bacteria produce antimicrobial peptides, which are also referred to as peptide bacteriocins. The class IIa bacteriocins, often designated pediocin-like bacteriocins, constitute the most dominant group of antimicrobial peptides produced by lactic acid bacteria. The bacteriocins that belong to this class are structurally related and kill target cells by membrane permeabilization. Despite their structural similarity, class IIa bacteriocins display different target cell specificities. In the search for new antibiotic substances, the class IIa bacteriocins have been identified as promising new candidates and have thus received much attention. They kill some pathogenic bacteria (e.g., Listeria) with high efficiency, and they constitute a good model system for structure-function analyses of antimicrobial peptides in general. This review focuses on class IIa bacteriocins, especially on their structure, function, mode of action, biosynthesis, bacteriocin immunity, and current food applications. The genetics and biosynthesis of class IIa bacteriocins are well understood. The bacteriocins are ribosomally synthesized with an N-terminal leader sequence, which is cleaved off upon secretion. After externalization, the class IIa bacteriocins attach to potential target cells and, through electrostatic and hydrophobic interactions, subsequently permeabilize the cell membrane of sensitive cells. Recent observations suggest that a chiral interaction and possibly the presence of a mannose permease protein on the target cell surface are required for a bacteria to be sensitive to class IIa bacteriocins. There is also substantial evidence that the C-terminal half penetrates into the target cell membrane, and it plays an important role in determining the target cell specificity of these bacteriocins. Immunity proteins protect the bacteriocin producer from the bacteriocin it secretes. The three-dimensional structures of two class IIa immunity proteins have been determined, and it has been shown that the C-terminal halves of these cytosolic four-helix bundle proteins specify which class IIa bacteriocin they protect against.

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Section: Mode Of Action At the Molecular Levelmentioning

confidence: 99%

“…Accordingly, it has been proposed that the IIC subunit (Fig. 6) is the target molecule of the class IIa bacteriocins (153).…”

Section: Mode Of Action At the Molecular Levelmentioning

confidence: 99%

The Continuing Story of Class IIa Bacteriocins

Drider

Fimland

Héchard

et al. 2006

Microbiol Mol Biol Rev

646

543

View full text Add to dashboard Cite

show abstract

“…In this interaction, one protein expressed by the targeted cell has been suggested to be the targeted molecule (bacteriocin receptor): the membrane-associated mannose phosphotransferase system (PTS) permease, named EII t Man Ramnath et al 2004;Xue et al 2005;Drider et al 2006). In both G + and G -bacteria, PTSs are involved in transport and phosphorylation of carbohydrates (Postma et al 1993).…”

Section: Class Iia Bacteriocinsmentioning

confidence: 99%

“…lactis strain to divergent class IIa bacteriocins (Ramnath et al 2004). Meanwhile, separate expression of each gene encoding fused IIAB, IIC and IID domains specified that the IIC itself is sufficient in the target recognition by class IIa bacteriocins (Ramnath et al 2004). The membrane-located IIC and IID have both been shown to be necessary for the receptor ).…”

Section: Class Iia Bacteriocinsmentioning

confidence: 99%

Genetic characterisation and heterologous expression of leucocin C, a class IIa bacteriocin from Leuconostoc carnosum 4010

Wan

Saris

et al. 2012

Appl Microbiol Biotechnol

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“…Finally, synthesis of the IIC Man component of Listeria monocytogenes (mptC gene) enhances sensitivity to class IIa bacteriocins (Ramnath et al, 2004).…”

Section: Introductionmentioning

confidence: 99%

Molecular analysis of the glucose-specific phosphoenolpyruvate : sugar phosphotransferase system from Lactobacillus casei and its links with the control of sugar metabolism

et al. 2006

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Lactobacillus casei transports glucose preferentially by a mannose-class phosphoenolpyruvate : sugar phosphotransferase system (PTS). The genomic analysis of L. casei allowed the authors to find a gene cluster (manLMNO) encoding the IIAB (manL), IIC (manM) and IID (manN) proteins of a mannose-class PTS, and a putative 121 aa protein of unknown function (encoded by manO), homologues of which are also present in man clusters that encode glucose/mannose transporters in other Gram-positive bacteria. The L. casei man operon is constitutively expressed into a manLMNO messenger, but an additional manO transcript was also detected. Upstream of the man operon, two genes (upsR and upsA) were found which encode proteins resembling a transcriptional regulator and a membrane protein, respectively. Disruption of either upsR or upsA did not affect manLMNO transcription, and had no effect on glucose uptake. Cells carrying a manO deletion transported glucose at a rate similar to that of the wild-type strain. By contrast, a manM disruption resulted in cells unable to transport glucose by the PTS, thus confirming the functional role of the man genes. In addition, the manM mutant exhibited neither inducer exclusion of maltose nor glucose repression. This result confirms the need for glucose transport through the PTS to trigger these regulatory processes in L. casei.

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Expression of mptC of Listeria monocytogenes induces sensitivity to class IIa bacteriocins in Lactococcus lactis

Cited by 93 publications

References 24 publications

The Continuing Story of Class IIa Bacteriocins

The Continuing Story of Class IIa Bacteriocins

Genetic characterisation and heterologous expression of leucocin C, a class IIa bacteriocin from Leuconostoc carnosum 4010

Molecular analysis of the glucose-specific phosphoenolpyruvate : sugar phosphotransferase system from Lactobacillus casei and its links with the control of sugar metabolism

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