Lantibiotics: biosynthesis, mode of action and applications

Kraaij, Cindy van; Vos, Willem M. de; Siezen, Roland J.; Kuipers, Oscar P.

doi:10.1039/a804531c

Cited by 124 publications

(97 citation statements)

References 147 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…The lantibiotics represent a diverse family of bacterially produced antimicrobial peptides Sahl et al, 1995;van Kraaij et al, 1999). They are characterized by the presence of lanthionine and b-methyllanthionine, which form intramolecular thioether rings.…”

Section: Introductionmentioning

confidence: 99%

Characteristics of the bovicin HJ50 gene cluster in Streptococcus bovis HJ50

Liu

Zhong

et al. 2009

Microbiology

View full text Add to dashboard Cite

Bovicin HJ50 is a new lantibiotic containing a disulfide bridge produced by Streptococcus bovis HJ50; its encoding gene bovA was reported in our previous publication. To identify other genes involved in bovicin HJ50 production, DNA fragments flanking bovA were cloned and sequenced. The bovicin HJ50 biosynthesis gene locus was encoded by a 9.9 kb region of chromosomal DNA and consisted of at least nine genes in the following order: bovA, -M, -T, -E, -F, ORF1, ORF2, bovK and bovR. A thiol-disulfide oxidoreductase gene named sdb1 was located downstream of bovR. A knockout mutant of this gene retained antimicrobial activity and the molecular mass of bovicin HJ50 in the mutant was the same as that of bovicin HJ50 in S. bovis HJ50, implying that sdb1 is not involved in bovicin HJ50 production. Transcriptional analyses showed that bovA, bovM and bovT constituted an operon, and the transcription start site of the bovA promoter was located at a G residue 45 bp upstream of the translation start codon for bovA, while bovE through bovR were transcribed together and the transcription start site of the bovE promoter was located at a C residue 35 bp upstream of bovE. We also demonstrated successful heterologous expression of bovicin HJ50 in Lactococcus lactis MG1363, which lacks thiol-disulfide oxidoreductase genes; this showed that thiol-disulfide oxidoreductase genes other than sdb1 are not essential for bovicin HJ50 biosynthesis.

show abstract

Section: Introductionmentioning

confidence: 99%

Characteristics of the bovicin HJ50 gene cluster in Streptococcus bovis HJ50

Liu

Zhong

et al. 2009

Microbiology

View full text Add to dashboard Cite

show abstract

“…It has been described that parts of the mature protein are also required for export by a dedicated ABC transporter. Moreover, the leader peptide has an important function in the prevention of premature antimicrobial activity and is required for the posttranslational modification of lantibiotics (141,144). The two known leader peptides of this type in B. subtilis 168 direct the secretion of sublancin 168 (89) and ComX (67).…”

mentioning

confidence: 99%

Proteomics of Protein Secretion by Bacillus subtilis : Separating the “Secrets” of the Secretome

Tjalsma¹,

Antelmann

Jongbloed³

et al. 2004

Microbiol Mol Biol Rev

Self Cite

513

519

View full text Add to dashboard Cite

SUMMARY Secretory proteins perform a variety of important“ remote-control” functions for bacterial survival in the environment. The availability of complete genome sequences has allowed us to make predictions about the composition of bacterial machinery for protein secretion as well as the extracellular complement of bacterial proteomes. Recently, the power of proteomics was successfully employed to evaluate genome-based models of these so-called secretomes. Progress in this field is well illustrated by the proteomic analysis of protein secretion by the gram-positive bacterium Bacillus subtilis, for which ∼90 extracellular proteins were identified. Analysis of these proteins disclosed various“ secrets of the secretome,” such as the residence of cytoplasmic and predicted cell envelope proteins in the extracellular proteome. This showed that genome-based predictions reflect only∼ 50% of the actual composition of the extracellular proteome of B. subtilis. Importantly, proteomics allowed the first verification of the impact of individual secretion machinery components on the total flow of proteins from the cytoplasm to the extracellular environment. In conclusion, proteomics has yielded a variety of novel leads for the analysis of protein traffic in B. subtilis and other gram-positive bacteria. Ultimately, such leads will serve to increase our understanding of virulence factor biogenesis in gram-positive pathogens, which is likely to be of high medical relevance.

show abstract

“…The defining characteristic of lantibiotics is that they contain the unusual amino acid lanthionine (or β-methyllanthionine). Generally, type A lantibiotics are characterized by being strongly cationic (with 2 to 7 net positive charge), having molecular masses more than 2 kDa, and having rigid ring conformations separated by areas of flexibility [2,3]. It is currently believed that their primary bactericidal activity is mediated through the formation of voltage-dependent membrane channels.…”

Section: Introductionmentioning

confidence: 99%

Phylogenetic signatures of functional conservedness in lantibiotics- an in-silico regulomics study

Basu¹,

Chakraborty²,

Ganguli³

et al. 2010

Int J of Micr Res

View full text Add to dashboard Cite

Abstract-The name Lantibiotics was introduced in 1988 as an abbreviation for "Lanthionine-containing peptide antibiotics". In spite of this naming, Lantibiotics are not classed as antibiotics. The first structures of these antimicrobial agents were produced by pioneering work by Gross and Morell in the late sixties and early seventies, thus marking the formal introduction of Lantibiotics. Since then Lantibiotics such as Nisin have been for food preservation and have yet to encounter significant bacterial resistance. These attributes of lantibiotics have led to more detailed research into them. IntroductionA comprehensive structural analysis of the lantibiotics was performed. Phosphorylation sites were detected for the sequences. Conserved domains were also analyzed for phylogenetic signatures (PHYLIP) and molecular modeling of representative members of the major groups of the lantibiotics were performed using Modeler 9.2. Several plant homologues were detected sharing sequence identity of over 85% with the lantibiotics mostly belonging to the bacteriocin superfamily. Most of the plant homologues identified were transcription factors induced by phytohormones. Phosphorylation sites detected in the sequences show a bias for serine phosphorylation in most of the conserved regions. Phylogenetic analysis revealed that blocks of lantibiotics are phylogenetically related to certain members of the mammalian immune response pathways as they share a stretch of conserved region in them. Apart from them certain sequences had metallothionein sequences as their sister groups indicative of a stress related functional conservedness.

show abstract

Lantibiotics: biosynthesis, mode of action and applications

Cited by 124 publications

References 147 publications

Characteristics of the bovicin HJ50 gene cluster in Streptococcus bovis HJ50

Characteristics of the bovicin HJ50 gene cluster in Streptococcus bovis HJ50

Proteomics of Protein Secretion by Bacillus subtilis : Separating the “Secrets” of the Secretome

Phylogenetic signatures of functional conservedness in lantibiotics- an in-silico regulomics study

Contact Info

Product

Resources

About