Lantibiotics from
            <i>Geobacillus thermodenitrificans</i>

Garg, Neha; Tang, Weixin; Goto, Yuki; Nair, Satish K.; Donk, Wilfred A. van der

doi:10.1073/pnas.1116815109

Cited by 127 publications

(138 citation statements)

References 46 publications

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“…These results demonstrate convergent evolution to arrive at nisin-like architectures. When also taking into consideration the distinct C-terminal ring topologies of subtilin (6), ericin A (24), and geobacillin (25) (Fig. 3), and their closely related LanCs (Fig.…”

Section: Resultsmentioning

confidence: 99%

Evolution of lanthipeptide synthetases

Zhang

Velásquez

et al. 2012

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

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Lanthionine-containing peptides (lanthipeptides) are a family of ribosomally synthesized and posttranslationally modified peptides containing (methyl)lanthionine residues. Here we present a phylogenomic study of the four currently known classes of lanthipeptide synthetases (LanB and LanC for class I, LanM for class II, LanKC for class III, and LanL for class IV). Although they possess very similar cyclase domains, class II-IV synthetases have evolved independently, and LanB and LanC enzymes appear to not always have coevolved. LanM enzymes from various phyla that have three cysteines ligated to a zinc ion (as opposed to the more common CysCys-His ligand set) cluster together. Most importantly, the phylogenomic data suggest that for some scaffolds, the ring topology of the final lanthipeptides may be determined in part by the sequence of the precursor peptides and not just by the biosynthetic enzymes. This notion was supported by studies with two chimeric peptides, suggesting that the nisin and prochlorosin biosynthetic enzymes can produce the correct ring topologies of epilancin 15X and lacticin 481, respectively. These results highlight the potential of lanthipeptide synthetases for bioengineering and combinatorial biosynthesis. Our study also demonstrates unexplored areas of sequence space that may be fruitful for genome mining. molecular evolution | natural products | phylogeny | posttranslational modification | lantibiotics

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Section: Resultsmentioning

confidence: 99%

Evolution of lanthipeptide synthetases

Zhang

Velásquez

et al. 2012

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

Self Cite

173

244

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“…strain HIL Y-85 (22), and amylolysin from Bacillus amyloliquefaciens GA1 (23). Bacillus genus-related Geobacillus strains produce geobacillin I, and its unproduced geobacillin II is obtained in vitro (24). As an important member of the Bacillus group, Bacillus cereus is ubiquitous in soil as well as food, and some strains have been commonly treated as opportunistic pathogens that cause gastrointestinal as well as nongastrointestinal diseases (25).…”

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confidence: 99%

Cerecidins, Novel Lantibiotics from Bacillus cereus with Potent Antimicrobial Activity

Wang

Zhang

Teng

et al. 2014

Appl Environ Microbiol

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Lantibiotics are ribosomally synthesized and posttranslationally modified antimicrobial peptides that are widely produced by Gram-positive bacteria, including many species of the Bacillus group. In the present study, one novel gene cluster coding lantibiotic cerecidins was unveiled in Bacillus cereus strain As 1.1846 through genomic mining and PCR screening. The designated cer locus is different from that of conventional class II lantibiotics in that it included seven tandem precursor cerA genes, one modification gene (cerM), two processing genes (cerT and cerP), one orphan regulator gene (cerR), and two immunity genes (cerF and cerE). In addition, one unprecedented quorum sensing component, comQXPA, was inserted between cerM and cerR. The expression of cerecidins was not detected in this strain of B. cereus, which might be due to repressed transcription of cerM. We constitutively coexpressed cerA genes and cerM in Escherichia coli, and purified precerecidins were proteolytically processed with the endoproteinase GluC and a truncated version of putative serine protease CerP. Thus, two natural variants of cerecidins A1 and A7 were obtained which contained two terminal nonoverlapping thioether rings rarely found in lantibiotics. Both cerecidins A1 and A7 were active against a broad spectrum of Gram-positive bacteria. Cerecidin A7, especially its mutant Dhb13A, showed remarkable efficacy against multidrug-resistant Staphylococcus aureus (MDRSA), vancomycin-resistant Enterococcus faecalis (VRE), and even Streptomyces.

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“…The genome of G.stearothermophilus NG80-2 contains a gene product with a ring topology distinct from any known lantibiotics. The geobacillin II exhibits antibiotic activity against Bacillus only (Garg et al, 2012). Only bacteriocins type I nisin, mutacin (Fig.…”

Section: Introductionmentioning

confidence: 99%