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Extracellular vesicles produced by the G ram‐positive bacterium B acillus subtilis are disrupted by the lipopeptide surfactin
Author(s) -
Brown Lisa,
Kessler Anne,
CabezasSanchez Pablo,
LuqueGarcia Jose L.,
Casadevall Arturo
Publication year - 2014
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.12650
Subject(s) - surfactin , vesicle , biology , extracellular vesicle , bacillus subtilis , bacteria , lysis , extracellular , microbiology and biotechnology , lipopeptide , bacterial outer membrane , biochemistry , microvesicles , escherichia coli , gene , membrane , genetics , microrna
Summary Previously, extracellular vesicle production in G ram‐positive bacteria was dismissed due to the absence of an outer membrane, where G ram‐negative vesicles originate, and the difficulty in envisioning how such a process could occur through the cell wall. However, recent work has shown that G ram‐positive bacteria produce extracellular vesicles and that the vesicles are biologically active. In this study, we show that B acillus subtilis produces extracellular vesicles similar in size and morphology to other bacteria, characterized vesicles using a variety of techniques, provide evidence that these vesicles are actively produced by cells, show differences in vesicle production between strains, and identified a mechanism for such differences based on vesicle disruption. We found that in wild strains of B . subtilis , surfactin disrupted vesicles while in laboratory strains harbouring a mutation in the gene sfp , vesicles accumulated in the culture supernatant. Surfactin not only lysed B . subtilis vesicles, but also vesicles from B acillus anthracis , indicating a mechanism that crossed species boundaries. To our knowledge, this is the first time a gene and a mechanism has been identified in the active disruption of extracellular vesicles and subsequent release of vesicular cargo in G ram‐positive bacteria. We also identify a new mechanism of action for surfactin.