exists as a member of the commensal flora of the skin and gut where many complex polymicrobial interactions occur with genera such as , , and . Some of these interactions potentiate or inhibit virulence. The bacterial gastrointestinal commensal speciesEnterococcus faecalisproduces a small peptide, EntV, that modulates virulence. The active 68 amino acid EntV peptide inhibits biofilm formationin vitro; biofilm-related infections are difficult to treat with current therapeutics. EntV also attenuates fungal virulence in a Caenorhabditis elegansinfection model and a murine oral candidiasis model. We sought to identify the regions of EntV responsible for the anti-fungal activity, and based on structural information, we hypothesized that it could be localized to a single helix of the mature peptide. In this study, we report that smaller peptides derived from this helix ranging from 12 to 16 amino acids have equal to improved efficacy in inhibiting virulence andbiofilm formation. These smaller peptides attenuate virulence in the infection model, inhibit initial adhesion to abiotic surfaces, and reduce the size of mature biofilms measured by confocal microscopy. Further trimming of these peptides to fewer than 11 amino acids reduces and eventually eliminates activity. These data indicate that EntV-derived peptides warrant further investigation as potential non-fungicidal additives to medical devices and antifungal therapeutics.

  • This is an open-access article distributed under the terms of the Creative Commons Attribution License.

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