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PMID: 18156339 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

The inhibitory spectrum of thermophilin 9 from Streptococcus thermophilus LMD-9 depends on the production of multiple peptides and the activity of BlpG(St), a thiol-disulfide oxidase.

Applied and environmental microbiology ·Vol. 74 ·No. 4 ·2008-02-00 ·Pages 1102-10

Fontaine L, Hols P

Abstract

The blp(St) cluster of Streptococcus thermophilus LMD-9 was recently shown to contain all the genetic information required for the production of bacteriocins active against other S. thermophilus strains. In this study, we further investigated the antimicrobial activity of S. thermophilus LMD-9 by testing the susceptibility of 31 bacterial species (87 strains). We showed that LMD-9 displays an inhibitory spectrum targeted toward related gram-positive bacteria, including pathogens such as Listeria monocytogenes. Using deletion mutants, we investigated the contribution of the three putative bacteriocin-encoding operons blpD(St)-orf2, blpU(St)-orf3, and blpE(St)-blpF(St) (bac(St) operons) and of the blpG(St) gene, which encodes a putative modification protein, to the inhibitory spectrum and immunity of strain LMD-9. Our results present evidence that the blp(St) locus encodes a multipeptide bacteriocin system called thermophilin 9. Among the four class II bacteriocin-like peptides encoded within the bac(St) operons, BlpD(St) alone was sufficient to inhibit the growth of most thermophilin 9-sensitive species. The blpD(St) gene forms an operon with its associated immunity gene(s), and this functional bacteriocin/immunity module could easily be transferred to Lactococcus lactis. The remaining three Bac(St) peptides, BlpU(St), BlpE(St), and BlpF(St), confer poor antimicrobial activity but act as enhancers of the antagonistic activity of thermophilin 9 by an unknown mechanism. The blpG(St) gene was also shown to be specifically required for the antilisteria activity of thermophilin 9, since its deletion abolished the sensitivities of most Listeria species. By complementation of the motility deficiency of Escherichia coli dsbA, we showed that blpG(St) encodes a functional thiol-disulfide oxidase, suggesting an important role for disulfide bridges within thermophilin 9.

MeSH Terms
Amino Acid Sequence Bacteriocins/genetics,pharmacology Base Sequence DNA Primers/genetics Gene Deletion Genetic Vectors/genetics Gram-Positive Bacteria/drug effects Molecular Sequence Data Multigene Family/genetics Operon/genetics Peptides/genetics,metabolism Protein Disulfide Reductase (Glutathione)/genetics,metabolism Sequence Analysis, DNA Species Specificity Streptococcus thermophilus/genetics,pathogenicity
Chemicals
Bacteriocins DNA Primers Peptides Protein Disulfide Reductase (Glutathione)
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Fontaine Laetitia
Unité de Génétique, Université catholique de Louvain, Place Croix du Sud 5, B-1348 Louvain-la-Neuve, Belgium.
Hols Pascal
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Article Info
Journal
Applied and environmental microbiology
Abbr.
Appl Environ Microbiol
ISSN
1098-5336
DOI
10.1128/AEM.02030-07
Published
2008-02-00
Epub
2007-00-21
Pages
1102-10
Language
English
Region
United States
NLM ID
7605801
PMCID
PMC2258595
Subset
IM
External Links
PubMed source DOI: 10.1128/AEM.02030-07 PMC Full Text View journal details
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