A Review: Lantibiotics, a Promising  Antimicrobial Agent

Basi-Chipalu, Shradha

doi:10.3126/jist.v21i1.16063

Cited by 5 publications

(4 citation statements)

References 56 publications

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“…The arsenal of antimicrobial compounds that this genus produces includes polyketides, nonribosomal, and ribosomal peptides (Donadio, Monciardini, & Sosio, ; Zhang, Doroghazi, Zhao, Walker, & Donk, ). Recent studies have focussed on the discovery of ribosomally synthesized and posttranslationally modified peptides (RiPPs), in light of the need for novel antimicrobials to combat the rising antimicrobial drug resistance (Basi‐Chipalu, ). A particular focus has been on the discovery of novel lantibiotics (a class of RiPPs) that display antimicrobial activity against the drug‐resistant pathogenic bacteria (Basi‐Chipalu, ).…”

Section: Introductionmentioning

confidence: 99%

“…Recent studies have focussed on the discovery of ribosomally synthesized and posttranslationally modified peptides (RiPPs), in light of the need for novel antimicrobials to combat the rising antimicrobial drug resistance (Basi‐Chipalu, ). A particular focus has been on the discovery of novel lantibiotics (a class of RiPPs) that display antimicrobial activity against the drug‐resistant pathogenic bacteria (Basi‐Chipalu, ). Here, we have heterologously produced and characterized a novel lantibiotic roseocin from Streptomyces roseosporus NRRL 11379, by employing a semi‐in vitro reconstitution approach (Garg, Tang, Goto, Nair, & Donk, ).…”

Section: Introductionmentioning

confidence: 99%

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Roseocin, a novel two‐component lantibiotic from an actinomycete

Singh

Chaudhary

Sareen

2019

Molecular Microbiology

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Lantibiotics are lanthionine ring containing natural products that belong to the class of ribosomally synthesized and posttranslationally modified peptides (RiPPs). Recent expansion in the availability of microbial genome data and in silico analysis tools have accelerated the discovery of these promising alternatives to antibiotics. Following the genome‐mining approach, a biosynthetic gene cluster for a putative two‐component lantibiotic, roseocin, was identified in the genome of an Actinomycete, Streptomyces roseosporus NRRL 11379. Posttranslationally modified lanthipeptides of this cluster were obtained by heterologous expression of the genes in Escherichia coli, and were in vitro reconstituted to their bioactive form by exploiting commercial proteases like endoproteinase GluC, and proteinase K. The two peptides displayed synergistic antimicrobial activity against Gram‐positive bacteria including the WHO high‐priority pathogens, MRSA and VRE. Structural characterization confirmed the installation of four (methyl)lanthionine rings with an indispensable disulfide bond in the α‐peptide, and six (methyl)lanthionine rings in the β‐peptide, by a single promiscuous lanthionine synthetase, RosM. Roseocin is the first two‐component lantibiotic from a non‐Firmicute, with extensive lanthionine bridging.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Roseocin, a novel two‐component lantibiotic from an actinomycete

Singh

Chaudhary

Sareen

2019

Molecular Microbiology

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“…The biosynthesis of lanthipeptides includes the dehydration reaction of serine and threonine residues to generate didehydroalanine (Dha) and didehydrobutyrine (Dhb) residues that would be subsequently converted into Lan or MeLan residues via a cyclization reaction [ 19 ]. The biosynthetic gene cluster of lanthipeptides contains the gene encoding the core peptide termed lanA ; modification genes ( lanB , lanC , lanM , and lanKC ) mediating the enzymes involved in the dehydration and cyclization reactions; regulation genes encoding a response regulator ( lanR ) and histidine kinase ( lanK ); and other genes encoding transport ( lanT ), immunity ( lanI (H) and lanFEG ), and leader cleavage ( lanP ) [ 3 , 20 ].…”

Section: Resultsmentioning

confidence: 99%

In Silico Screening of Bacteriocin Gene Clusters within a Set of Marine Bacillota Genomes

Teber,

Asakawa

2024

IJMS

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Due to their potential application as an alternative to antibiotics, bacteriocins, which are ribosomally synthesized antimicrobial peptides produced by bacteria, have received much attention in recent years. To identify bacteriocins within marine bacteria, most of the studies employed a culture-based method, which is more time-consuming than the in silico approach. For that, the aim of this study was to identify potential bacteriocin gene clusters and their potential producers in 51 marine Bacillota (formerly Firmicutes) genomes, using BAGEL4, a bacteriocin genome mining tool. As a result, we found out that a majority of selected Bacillota (60.78%) are potential bacteriocin producers, and we identified 77 bacteriocin gene clusters, most of which belong to class I bacteriocins known as RiPPs (ribosomally synthesized and post-translationally modified peptides). The identified putative bacteriocin gene clusters are an attractive target for further in vitro research, such as the production of bacteriocins using a heterologous expression system.

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“…The arsenal of antimicrobial compounds that this genus produces includes polyketides, non-ribosomal, and ribosomal peptides. Recent studies have focussed on the discovery of ribosomally synthesized and post-translationally modified peptides (RiPPs) in light of the need for novel antimicrobials to combat the rising antimicrobial drug resistance (Basi-Chipalu, 2016). A particular focus has been on the discovery of novel lantibiotics (a class of RiPPs) that display their activity against the drug-resistant bacteria.…”

Section: Introductionmentioning

confidence: 99%

Semi-in vitro Reconstitution of Roseocin, a Two-Component Lantibiotic from an Actinomycete

Singh

Sareen

2018

Preprint

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7Lantibiotics are lanthionine containing peptide natural products that belong to the class of 8 ribosomally synthesized and post-translationally modified peptides (RiPPs). Recent expansion 9 in the availability of microbial genomic data and in silico analysis tools have accelerated the 10 discovery of these promising alternatives to antibiotics. Following the genome-mining 11 approach, a biosynthetic gene cluster for a putative two-component lantibiotic roseocin was 12 identified in the genome of an Actinomycete, Streptomyces roseosporus NRRL 11379. Post-13 translationally modified lanthipeptides of this cluster were obtained by heterologous expression 14 of the genes in E. coli, and were in vitro reconstituted to their bioactive form. The two 15 lanthipeptides displayed antimicrobial activity against Gram-positive bacteria only 16 synergistically, a property reminiscent of two-component lantibiotics. Structural analysis of the 17 α-component identified a disulfide bridge flanking two of its four thioether bridges and the β-18 component having six thioether bridges with its C-terminus extended than the previously 19 known two-component lantibiotics. 20 21 roseocin, synergistic, thioether 22 lantibiotic roseocin from Streptomyces roseosporus NRRL 11379, by employing a semi-in 32 vitro reconstitution approach. 33As with the polyketides and non-ribosomal peptide antibiotics, lantibiotics are also synthesized 34 from a biosynthetic gene cluster (BGC). A genetically encoded lantibiotic is initially 35 synthesized as a linear peptide (precursor peptide) with two important regions, an N-terminal 36 leader peptide region separated by a proteolytic cleavage site from its C-terminal core-peptide 37 region that is rich in Cys/Ser/Thr residues. While the leader peptide guides the precursor 38 peptide to different enzymes, the core-peptide forms the final lantibiotic structure. Lantibiotics 39 are synthesized in two steps by (1) dehydration of Ser/Thr residues in the core-peptide followed 40 by (2) intra-peptide Michael addition of cysteine residues to form lanthionine or thioether 41 bridges (cyclization). These lanthionine rings are installed by various enzymes which define 42 the four classes of lantibiotics. In class I lantibiotics, two separate enzymes for dehydration 43 (LanB) and cyclization (LanC) are encoded in the BGC along with the gene for the precursor 44 peptide (LanA). Besides this, a lantibiotic BGC encodes a protease (LanP) for the proteolytic 45 removal of the leader peptide, a transporter (LanT) for extracellular transport of the modified 46 peptide, immunity proteins (LanF, LanE, LanG and sometimes LanI) and a two-component 47 response regulation system (LanR and LanK). Class II, III and IV lantibiotic BGCs encode a 48 single lanthionine synthetase instead of separate dehydratase and cyclase enzymes for the 49 lanthionine ring formation. The class III and IV lantibiotics have bioactivities majorly other 50 than antimicrobial action like morphogenetic (Ueda et al., 2002), antiviral, antiallodynic(Férir ...

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A Review: Lantibiotics, a Promising Antimicrobial Agent

Cited by 5 publications

References 56 publications

Roseocin, a novel two‐component lantibiotic from an actinomycete

Roseocin, a novel two‐component lantibiotic from an actinomycete

In Silico Screening of Bacteriocin Gene Clusters within a Set of Marine Bacillota Genomes

Semi-in vitro Reconstitution of Roseocin, a Two-Component Lantibiotic from an Actinomycete

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