AI Article Synopsis

  • Bacteriocins are antimicrobial peptides produced by bacteria for survival advantages in competitive environments; a new strain called SKDU10 from the Brevibacillus genus was isolated and found to produce a class IId bacteriocin named laterosporulin10.
  • Laterosporulin10 shows 57.6% homology with the known bacteriocin laterosporulin but has a different antimicrobial spectrum, effectively inhibiting Staphylococcus aureus and Mycobacterium tuberculosis at low concentrations.
  • It demonstrates membrane-permeabilizing properties, can kill M. tuberculosis inside macrophages, and does not cause hemolysis, making it a promising candidate for further study in antimicrobial treatments.

Article Abstract

Bacteriocins are antimicrobial peptides (AMPs) produced by bacteria to acquire survival benefits during competitive inter- and intra-species interactions in complex ecosystems. In this study, an AMP-producing soil bacterial strain designated SKDU10 was isolated and identified as a member of the genus Brevibacillus. The AMP produced by strain SKDU10 identified as a class IId bacteriocin with 57.6 % homology to laterosporulin, a defensin-like class IId bacteriocin. However, substantial differences were observed in the antimicrobial activity spectrum of this bacteriocin named laterosporulin10 when compared to laterosporulin. Laterosporulin10 effectively inhibited the growth of Staphylococcus aureus and Mycobacterium tuberculosis (Mtb H37Rv) with LD50 values of 4.0 µM and 0.5 µM, respectively. Furthermore, laterosporulin10 inhibited the growth of Mtb H37Rv strain at about 20 times lower MIC value compared to S. aureus MTCC 1430 or M. smegmatis MC2 155 in vitro and ex vivo. Electron micrographs along with membrane permeabilization studies using FACS analysis revealed that laterosporulin10 is a membrane-permeabilizing peptide. Interestingly, laterosporulin10 was able to efficiently kill Mtb H37Rv strain residing inside the macrophages and did not show haemolysis up to 40 µM concentration.

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Source
http://dx.doi.org/10.1099/mic.0.000316DOI Listing

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