Two-peptide bacteriocins produced by lactic acid bacteria

Garneau, Sylvie; Martin, Nathaniel I.; Vederas, John C.

doi:10.1016/s0300-9084(02)01414-1

Cited by 207 publications

(155 citation statements)

References 129 publications

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“…An alternative possibility that would result in the absence of the 2-oxobutyryl group is that Thr-42 is not dehydrated resulting in Thr-1 at the N terminus of Hal␤ after proteolysis. However, this model is inconsistent with the MS͞MS data because the masses of a series of fragment ions (b 5 , b 6 , b 7 , b 8 , and b 15 ; Fig. 3B) clearly indicate the dehydration of Thr-1 in Hal␤.…”

Section: Discussionmentioning

confidence: 88%

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Discovery and in vitro biosynthesis of haloduracin, a two-component lantibiotic

McClerren¹,

Cooper

Quan

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

234

321

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Lantibiotics are ribosomally synthesized peptides that undergo posttranslational modifications to their mature, antimicrobial form. They are characterized by the unique amino acids lanthionine and methyllanthionine, introduced by means of dehydration of Ser͞Thr residues followed by reaction of the resulting dehydro amino acids with cysteines to form thioether linkages. Two-component lantibiotics use two peptides that are each posttranslationally modified to yield two functionally distinct products that act in synergy to provide bactericidal activity. By using genetic data instead of isolation, a two-component lantibiotic, haloduracin, was identified in the genome of the Gram-positive alkaliphilic bacterium Bacillus halodurans C-125. We show that heterologously expressed and purified precursor peptides HalA1 and HalA2 are processed by the purified modification enzymes HalM1 and HalM2 in an in vitro reconstitution of the biosynthesis of a two-component lantibiotic. The activity of each HalM enzyme is substratespecific, and the assay products exhibit antimicrobial activity after removal of their leader sequences at an engineered Factor Xa cleavage site, indicating that correct thioether formation has occurred. Haloduracin's biological activity depends on the presence of both modified peptides. The structures of the two mature haloduracin peptides Hal␣ and Hal␤ were investigated, indicating that they have similarities as well as some distinct differences compared with other two-component lantibiotics.lanthionine ͉ dehydroalanine ͉ antibiotic

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Section: Discussionmentioning

confidence: 88%

“…A growing class of two-component lantibiotic systems utilize two peptides that are each posttranslationally modified to an active form and act in synergy to provide antibacterial activity (8). Dehydration and cyclization of the prepeptides to form lanthionine bridges in these systems are likely performed by bifunctional LanM proteins.…”

mentioning

confidence: 99%

Discovery and in vitro biosynthesis of haloduracin, a two-component lantibiotic

McClerren¹,

Cooper

Quan

et al. 2006

Proc. Natl. Acad. Sci. U.S.A.

234

321

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“…On one side, this cluster ends with a gene that can be clearly assigned to primary metabolism (a DNA photolyase homolog), and on the other side a putative structural gene was identified extending Ϸ1 kbp upstream of patA. These genes and the organization of the cluster are reminiscent of the lantibiotic and microcin biosynthetic machinery, which has been characterized in other bacteria (30)(31)(32). In particular, the microcin B17 peptide contains heterocycles (18,33), whereas microcin J25 (21, 34) is cyclic.…”

Section: Resultsmentioning

confidence: 98%

Patellamide A and C biosynthesis by a microcin-like pathway inProchloron didemni, the cyanobacterial symbiont ofLissoclinum patella

Schmidt

Nelson

Rasko

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

551

717

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Prochloron spp. are obligate cyanobacterial symbionts of many didemnid family ascidians. It has been proposed that the cyclic peptides of the patellamide class found in didemnid extracts are synthesized by Prochloron spp., but studies in which host and symbiont cells are separated and chemically analyzed to identify the biosynthetic source have yielded inconclusive results. As part of the Prochloron didemni sequencing project, we identified patellamide biosynthetic genes and confirmed their function by heterologous expression of the whole pathway in Escherichia coli. The primary sequence of patellamides A and C is encoded on a single ORF that resembles a precursor peptide. We propose that this prepatellamide is heterocyclized to form thiazole and oxazoline rings, and the peptide is cleaved to yield the two cyclic patellamides, A and C. This work represents the full sequencing and functional expression of a marine natural-product pathway from an obligate symbiont. In addition, a related cluster was identified in Trichodesmium erythraeum IMS101, an important bloom-forming cyanobacterium.heterocycle ͉ tunicate ͉ ascidian ͉ genome sequencing ͉ lantibiotic

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“…They are only inhibited by purified LAB-bacteriocins if the permeability barrier properties of their outer membrane are impaired by chemical agents (e.g., organic acids, EDTA and other chelating agents) or stressing environmental Table 1. Classification of bacteriocins produced by LAB (Garneau et al, 2002;Jack et al, 1995;Kaškonienė et al, 2017;Klaenhammer, 1993;Nes et al, 1996;Słońska and Klimuszko, 2010 conditions (e.g., pH, freezing, mild heating or high hydrostatic pressure) (Chen and Hoover, 2003;Cintas et al, 2001;O'Shea et al, 2013;Servin, 2004). Nisin, a bacteriocin produced by many strains of Lactococcus lactis subsp.…”

Section: Bacteriocins Produced By Lab -General Characteristicsmentioning

confidence: 99%

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2015

Acta Sci Pol Technol Aliment

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Two-peptide bacteriocins produced by lactic acid bacteria

Cited by 207 publications

References 129 publications

Discovery and in vitro biosynthesis of haloduracin, a two-component lantibiotic

Discovery and in vitro biosynthesis of haloduracin, a two-component lantibiotic

Patellamide A and C biosynthesis by a microcin-like pathway inProchloron didemni, the cyanobacterial symbiont ofLissoclinum patella

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