Sensitivity to the two‐peptide bacteriocin lactococcin <scp>G</scp> is dependent on <scp>UppP</scp>, an enzyme involved in cell‐wall synthesis

Kjos, Morten; Oppegård, Camilla; Diep, Dzung B.; Nes, Ingolf F.; Veening, Jan‐Willem; Nissen‐Meyer, Jon; Kristensen, Tom

doi:10.1111/mmi.12632

Cited by 84 publications

(77 citation statements)

References 46 publications

(76 reference statements)

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“…Types of receptors appear to be targeted by several related and sometimes also nonrelated bacteriocins. For instance, the permease mannose-phosphotransferase (PTS) is targeted by many pediocin-like bacteriocins, in addition to the unrelated lactococcins A and B (48), whereas a zinc-dependent membrane-bound protease belonging to the M50 family is targeted by several related leaderless bacteriocins (49; unpublished results), and the undecaprenyl pyrophosphate phosphatase UppP (a membrane protein involved in peptidoglycan synthesis) is targeted by the two-peptide bacteriocins lactococcin G and enterocin 1071 (50).…”

Section: Antimicrobial Spectrum and Mode Of Actionmentioning

confidence: 99%

Circular Bacteriocins: Biosynthesis and Mode of Action

Gabrielsen

Brede

Nes

et al. 2014

Appl Environ Microbiol

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127

147

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b Circular bacteriocins are a group of N-to-C-terminally linked antimicrobial peptides, produced by Gram-positive bacteria of the phylum Firmicutes. Circular bacteriocins generally exhibit broad-spectrum antimicrobial activity, including against common food-borne pathogens, such as Clostridium and Listeria spp. These peptides are further known for their high pH and thermal stability, as well as for resistance to many proteolytic enzymes, properties which make this group of bacteriocins highly promising for potential industrial applications and their biosynthesis of particular interest as a possible model system for the synthesis of highly stable bioactive peptides. In this review, we summarize the current knowledge on this group of bacteriocins, with emphasis on the recent progress in understanding circular bacteriocin genetics, biosynthesis, and mode of action; in addition, we highlight the current challenges and future perspectives for the application of these peptides.

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Section: Antimicrobial Spectrum and Mode Of Actionmentioning

confidence: 99%

Circular Bacteriocins: Biosynthesis and Mode of Action

Gabrielsen

Brede

Nes

et al. 2014

Appl Environ Microbiol

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127

147

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“…Lactococcin G consists of two unmodified subunits, LcnG-a (GTWDDIGGGIGRVAYWVGKA MGNMSDVNQASRINRKKKH) and LcnG-b (KKWGWLAWVDPAY EFIKGFGKGAIKEGNKDKWKNI) (Kjos et al, 2014). Both LcnG-a and LcnG-b were commercially synthesized with 90 % purity (Pepmic).…”

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confidence: 99%

Identification and characterization of SMU.244 encoding a putative undecaprenyl pyrophosphate phosphatase protein required for cell wall biosynthesis and bacitracin resistance in Streptococcus mutans

et al. 2015

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Streptococcus mutans in dental biofilms often faces life-threatening threats such as killing by antimicrobial molecules from competing species or from the host. The ability of S. mutans to cope with such threats is crucial for its survival and persistence in dental biofilms. By screening a transposon mutant library, we identified 11 transposon insertion mutants that were sensitive to bacitracin. Two of these mutants, XTn-01 and XTn-03, had an independent insertion in the same locus, SMU.244, which encoded a homologue of undecaprenyl pyrophosphate phosphatase (UppP). In this study, we describe the genetic and phenotypic characterization of SMU.244 in antibiotic resistance. The results revealed that deletion of SMU.244 results in a mutant (XTD244) that is highly sensitive to bacitracin, but confers more resistance to lactococcin G, a class IIb bacteriocin. Introduction of the intact SMU.244 into XTD244 in trans completely restores its resistance to bacitracin and the susceptibility to lactococcin G. The XTD244 was also defective in forming the WT biofilm, although its growth was not significantly affected. Using recombinant protein technology, we demonstrated that the SMU.244-encoded protein displays enzyme activity to catalyse dephosphorylation of the substrate. The lux transcriptional reporter assays showed that S. mutans maintains a moderate level of expression of SMU.244 in the absence of bacitracin, but bacitracin at sub-MICs can further induce its expression. We concluded that SMU.244 encodes an UppP protein that plays important roles in cell wall biosynthesis and bacitracin resistance in S. mutans. The results described here may further our understanding of the molecular mechanisms by which S. mutans copes with antibiotics such as bacitracin.

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“…Recently, UppP/BacA has been found to be the receptor for lactococcin G and is presumed also to be the receptor for lactococcin Q (Kjos et al, 2014). In addition, the regions including the N-terminal end of lactococcin Ga (residues 1 to 13) and the C-terminal part of lactococcin Gb (residues 14 to 24) were identified as recognition regions by LagC.…”

Section: Discussionmentioning

confidence: 99%

“…More recently, Kjos et al (2014) showed that the undecaprenylpyrophosphate phosphatase (termed UppP in L. lactis subsp. lactis IL1403 and BacA in L. lactis subsp.…”

Section: Introductionmentioning

confidence: 99%

Molecular characterization of the genes involved in the secretion and immunity of lactococcin Q, a two-peptide bacteriocin produced by Lactococcus lactis QU 4

et al. 2015

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Lactococcin Q is a two-peptide (Qa and Qb) bacteriocin produced by Lactococcus lactis QU 4, which exhibits specific antimicrobial activity against L. lactis strains. The lactococcin Q gene cluster (approximately 4.5 kb) was sequenced and found to include genes encoding lactococcin Q immunity (laqC), an ATP-binding cassette transporter (laqD) and a transport accessory protein (laqE), downstream of the lactococcin Q structural genes (laqA and laqB). In addition, the gene cluster showed high sequence identity with that of a lactococcin Q homologue bacteriocin, lactococcin G. Heterologous expression studies showed that LaqD was responsible for lactococcin Q secretion in a manner dependent on LaqE expression, and that LaqC conferred self-immunity to lactococcin Q and cross-immunity to lactococcin G. Amino acid alignment of both lactococcin transporters revealed that LaqD contains an insertion (160-168 residues) that is essential for lactococcin Q secretion, as L. lactis cells that expressed LaqD D160-168 were devoid of this function. Additional experiments demonstrated that the LaqD D160-168 mutant was, however, able to secrete lactococcin G, suggesting that the insertion is necessary only for the lactococcin Q secretion by LaqD. This report demonstrates the biosynthetic mechanism of lactococcin Q/G-type bacteriocins and the complementarity of the genes responsible for the secretion of lactococcins Q and G.

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Sensitivity to the two‐peptide bacteriocin lactococcin G is dependent on UppP, an enzyme involved in cell‐wall synthesis

Cited by 84 publications

References 46 publications

Circular Bacteriocins: Biosynthesis and Mode of Action

Circular Bacteriocins: Biosynthesis and Mode of Action

Identification and characterization of SMU.244 encoding a putative undecaprenyl pyrophosphate phosphatase protein required for cell wall biosynthesis and bacitracin resistance in Streptococcus mutans

Molecular characterization of the genes involved in the secretion and immunity of lactococcin Q, a two-peptide bacteriocin produced by Lactococcus lactis QU 4

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