Evaluating the feasibility of lantibiotics as an alternative therapy against bacterial infections in humans

Heel, Auke J. van; Montalbán-López, Manuel; Kuipers, Oscar P.

doi:10.1517/17425255.2011.573478

Cited by 109 publications

(72 citation statements)

References 35 publications

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“…Therefore, attributing to their high efficacy and low occurrence of resistance, lantibiotics have been recognized as prominent and attractive substitutes for conventional antibiotics (6). As the prototype lantibiotic, nisin is active against a wide range of Gram-positive pathogens at nanomolar concentrations and has been long used as preservatives in the food industry without significant occurrence of resistance (7).…”

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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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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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“…In addition, they can complement or, in certain cases, replace antibiotics and chemical preservatives, the use of which is increasingly being called into question (14,16). Moreover, some bacteriocins have demonstrated a remarkable therapeutic potential for the treatment of local and systemic bacterial infections (17,18).…”

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confidence: 99%

Discovering the Bacterial Circular Proteins: Bacteriocins, Cyanobactins, and Pilins

Montalbán-López

Sánchez‐Hidalgo

Cebrián

et al. 2012

Journal of Biological Chemistry

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“…They are very potent antimicrobials that can target a narrow range of bacteria or can inhibit a broad range of sensitive strains depending on their type [1]. Many bacteriocins especially from LAB have been used for many years as food-grade food preservatives in many countries [3,4], and their application as therapeutic antibiotics is now seriously being considered [5,6].…”

Section: Introductionmentioning

confidence: 99%

Mutations near the cleavage site of enterocin NKR-5-3B prepeptide reveal new insights into its biosynthesis

et al. 2017

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Enterocin NKR-5-3B (Ent53B) is a 64-residue novel circular bacteriocin synthesized from an 87-residue prepeptide. Albeit through a still unknown mechanism, the EnkB1234 biosynthetic enzyme complex processes the prepeptide to yield its mature active, circular form. To gain insights into the key region/residue that plays a role in Ent53 maturation, several mutations near the cleavage site on the precursor peptide were generated. The interaction of the precursor peptide and EnkB1234 appeared to be hydrophobic in nature. At the Leu1 position, only mutations with helix structure-promoting hydrophobic residues (Ala, Ile, Val or Phe) were able to yield the mature Ent53B derivative. In this study, we also highlight the possible conformation-stabilizing role of the Ent53B leader peptide on the precursor peptide for its interaction with its biosynthetic enzyme complex. Any truncations of the leader peptide moiety interfered in the processing of the prepeptide. However, when propeptides of other circular bacteriocins (circularin A, leucocyclicin Q or lactocyclicin Q) were cloned at the C-terminus of the leader peptide, EnkB1234 could not process them to yield a mature bacteriocin. Taken together, these findings offer new perspectives in our understanding of the possible molecular mechanism of the biosynthesis of this circular bacteriocin. These new perspectives will help advance our current understanding to eventually elucidate circular bacteriocin biosynthesis. Understanding the biosynthetic mechanism of circular bacteriocins will materialize their application potential.

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Evaluating the feasibility of lantibiotics as an alternative therapy against bacterial infections in humans

Cited by 109 publications

References 35 publications

Cerecidins, Novel Lantibiotics from Bacillus cereus with Potent Antimicrobial Activity

Cerecidins, Novel Lantibiotics from Bacillus cereus with Potent Antimicrobial Activity

Discovering the Bacterial Circular Proteins: Bacteriocins, Cyanobactins, and Pilins

Mutations near the cleavage site of enterocin NKR-5-3B prepeptide reveal new insights into its biosynthesis

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