Cited by 46Antimicrobial Peptides and ActivitiesMicrobial Natural Products and BiosynthesisBiochemical and Structural Characterization

Antifungal activity of the Enterococcus faecalis peptide EntV requires protease cleavage and disulfide bond formation

Open access
Brown, Armand O., Graham, Carrie E., Cruz, Melissa R., Singh, Kavindra V., Murray, Barbara E., Lorenz, Michael C., Garsin, Danielle A.·2019·mBio

Abstract

Enterococcus faecalis and Candida albicans are among the most important and problematic pathobionts, organisms that normally are harmless commensals but can cause dangerous infections in immunocompromised hosts. In fact, both organisms are listed by the Centers for Disease Control and Prevention as serious global public health threats stemming from the increased prevalence of antimicrobial resistance. The rise in antifungal resistance is of particular concern considering the small arsenal of currently available therapeutics. EntV is a peptide with antifungal properties, and it, or a similar compound, could be developed into a therapeutic alternative, either alone or in combination with existing agents. However, to do so requires understanding what properties of EntV are necessary for its antifungal activity. In this work, we studied the posttranslational processing of EntV and what modifications are necessary for inhibition of C. albicans in order to fill this gap in knowledge.

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Crossref · 10.1128/mbio.01334-19

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  • The effect of E. faecalis on C. albicans is associated with a signaling event in which a bacterial-derived product, identified as EntV, a bacteriocin produced by E. faecalis as a pre-pro-peptide, inhibits C. albicans filamentation and biofilm formation.

    “This effect was associated with a signaling event in which a bacterial-derived product inhibited C. albicans filamentation and biofilm formation, with subsequent studies identifying this product as EntV, a bacteriocin produced by E. faecalis as a pre-pro-peptide.”
  • The active form of EntV is 68 amino acids, does not exhibit antifungal activity per se, and inhibits C. albicans biofilm formation both in vitro and in vivo.

    “The active form of EntV is 68 amino acids [60], which per se does not exhibit antifungal activity, inhibits C. albicans biofilm formation both in vitro and in vivo [61].”

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Research works printed but not linked: 1

  1. [30]Garsin DA, Frank KL, Silanpaa J, Ausubel FM, Hartke A, Shankar N, Murray BE 2014 Pathogenesis and models of enterococcal infection, p 185– 258. In Gilmore MS, Clewell DB, Ike Y, Shankar N (ed), Enterococci: from commensals to leading causes of drug resistant infection. Massachusetts Eye and Ear Infirmary, Boston, MA. 24649512

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Authors
Brown, A. O., Graham, C. E., Cruz, M. R., Singh, K. V., Murray, B. E., Lorenz, M. C., & Garsin, D. A.
Affiliations
  • The University of Texas Health Science Center at Houston (US)
  • The University of Texas MD Anderson Cancer Center (US)
Corresponding author
Garsin, Danielle A.
Venue
mBio
Published
2019-08-27
Volume
10
Issue
4
ISSN
  • 2150-7511 (ISSN-L)
  • 2161-2129
OpenAlex
W2956045308
Cited by
46
References
58
Citations by year
2026: 4 · 2025: 9 · 2024: 6 · 2023: 7 · 2022: 8 · 2021: 5 · 2020: 6 · 2019: 1
FWCI
3.67
Type
journal article
Language
en
Open access
Locations
  • mBio (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
Funders
  • HHS | NIH | National Institute of Allergy and Infectious Diseases (F31AI122725)
  • HHS | NIH | National Institute of Dental and Craniofacial Research (R01DE027608, F32DE027580)
Topics
  • Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
  • Health Sciences › Medicine › Pharmacology › Microbial Natural Products and Biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Structural Characterization
Keywords
Enterococcus faecalis, Candida albicans, antifungal activity, protease cleavage, disulfide bond formation, post-translational processing, pathobionts, antifungal resistance, antimicrobial peptides
MeSH terms
Antifungal Agents, Bacteriocins, Candida albicans, Disulfides, Protein Processing, Post-Translational, Enterococcus faecalis, Gelatinases, Hyphae, Proteolysis

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