Characterization of a Multipeptide Lantibiotic Locus in Streptococcus pneumoniae
Bacterial communities are established through a combination of cooperative and antagonistic interactions between the inhabitants. Competitive interactions often involve the production of antimicrobial substances, including bacteriocins, which are small antimicrobial peptides that target other commun...
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American Society for Microbiology
2016-01-01
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doaj-029aebf3c95841dab601e508a602a92a2021-07-02T06:48:28ZengAmerican Society for MicrobiologymBio2150-75112016-01-0171e01656-1510.1128/mBio.01656-15Characterization of a Multipeptide Lantibiotic Locus in Streptococcus pneumoniaeNatalie MaricicErica S. AndersonAnneMarie E. OpipariEmily A. YuSuzanne DawidBacterial communities are established through a combination of cooperative and antagonistic interactions between the inhabitants. Competitive interactions often involve the production of antimicrobial substances, including bacteriocins, which are small antimicrobial peptides that target other community members. Despite the nearly ubiquitous presence of bacteriocin-encoding loci, inhibitory activity has been attributed to only a small fraction of gene clusters. In this study, we characterized a novel locus (the pld locus) in the pathogen Streptococcus pneumoniae that drives the production of a bacteriocin called pneumolancidin, which has broad antimicrobial activity. The locus encodes an unusual tandem array of four inhibitory peptides, three of which are absolutely required for antibacterial activity. The three peptide sequences are similar but appear to play distinct roles in regulation and inhibition. A modification enzyme typically found in loci encoding a class of highly modified bacteriocins called lantibiotics was required for inhibitory activity. The production of pneumolancidin is controlled by a two-component regulatory system that is activated by the accumulation of modified peptides. The locus is located on a mobile element that has been found in many pneumococcal lineages, although not all elements carry the pld genes. Intriguingly, a minimal region containing only the genes required for pneumolancidin immunity was found in several Streptococcus mitis strains. The pneumolancidin-producing strain can inhibit nearly all pneumococci tested to date and provided a competitive advantage in vivo. These peptides not only represent a unique strategy for bacterial competition but also are an important resource to guide the development of new antimicrobials.http://mbio.asm.org/cgi/content/full/7/1/e01656-15 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Natalie Maricic Erica S. Anderson AnneMarie E. Opipari Emily A. Yu Suzanne Dawid |
spellingShingle |
Natalie Maricic Erica S. Anderson AnneMarie E. Opipari Emily A. Yu Suzanne Dawid Characterization of a Multipeptide Lantibiotic Locus in Streptococcus pneumoniae mBio |
author_facet |
Natalie Maricic Erica S. Anderson AnneMarie E. Opipari Emily A. Yu Suzanne Dawid |
author_sort |
Natalie Maricic |
title |
Characterization of a Multipeptide Lantibiotic Locus in Streptococcus pneumoniae |
title_short |
Characterization of a Multipeptide Lantibiotic Locus in Streptococcus pneumoniae |
title_full |
Characterization of a Multipeptide Lantibiotic Locus in Streptococcus pneumoniae |
title_fullStr |
Characterization of a Multipeptide Lantibiotic Locus in Streptococcus pneumoniae |
title_full_unstemmed |
Characterization of a Multipeptide Lantibiotic Locus in Streptococcus pneumoniae |
title_sort |
characterization of a multipeptide lantibiotic locus in streptococcus pneumoniae |
publisher |
American Society for Microbiology |
series |
mBio |
issn |
2150-7511 |
publishDate |
2016-01-01 |
description |
Bacterial communities are established through a combination of cooperative and antagonistic interactions between the inhabitants. Competitive interactions often involve the production of antimicrobial substances, including bacteriocins, which are small antimicrobial peptides that target other community members. Despite the nearly ubiquitous presence of bacteriocin-encoding loci, inhibitory activity has been attributed to only a small fraction of gene clusters. In this study, we characterized a novel locus (the pld locus) in the pathogen Streptococcus pneumoniae that drives the production of a bacteriocin called pneumolancidin, which has broad antimicrobial activity. The locus encodes an unusual tandem array of four inhibitory peptides, three of which are absolutely required for antibacterial activity. The three peptide sequences are similar but appear to play distinct roles in regulation and inhibition. A modification enzyme typically found in loci encoding a class of highly modified bacteriocins called lantibiotics was required for inhibitory activity. The production of pneumolancidin is controlled by a two-component regulatory system that is activated by the accumulation of modified peptides. The locus is located on a mobile element that has been found in many pneumococcal lineages, although not all elements carry the pld genes. Intriguingly, a minimal region containing only the genes required for pneumolancidin immunity was found in several Streptococcus mitis strains. The pneumolancidin-producing strain can inhibit nearly all pneumococci tested to date and provided a competitive advantage in vivo. These peptides not only represent a unique strategy for bacterial competition but also are an important resource to guide the development of new antimicrobials. |
url |
http://mbio.asm.org/cgi/content/full/7/1/e01656-15 |
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