Effect of Dermaseptin S4 on C. albicans Growth and EAP1 and HWP1 Gene Expression.
Antimicrobial cationic peptides
Biofilm
Candida albicans
EAP1
Genes
Gingival fibroblast
HWP1
Journal
Probiotics and antimicrobial proteins
ISSN: 1867-1314
Titre abrégé: Probiotics Antimicrob Proteins
Pays: United States
ID NLM: 101484100
Informations de publication
Date de publication:
02 2021
02 2021
Historique:
pubmed:
22
7
2020
medline:
17
6
2021
entrez:
22
7
2020
Statut:
ppublish
Résumé
Increasing resistance and changes in the spectrum of Candida infections have generated considerable interest in the development of new antifungal molecules. The use of antimicrobial peptides (AMPs) appears to be a promising approach. Frog skin AMPs (such as dermaseptins) have shown antimicrobial activity against several pathogens. In this study, we aimed to test the antimicrobial efficacy of dermaseptin S4 (DS4) against C. albicans. We determined the minimal inhibitory concentration (MIC) of DS4, and investigated the effects of the DS4 at low concentrations on human primary gingival fibroblasts. Additionally, we evaluated the effect of DS4 on C. albicans growth, form changes, and biofilm formation, as well as the expression of certain virulent genes. Our data show that DS4 completely inhibits C. albicans growth at a concentration of 32 μg/mL referring to the MIC of DS4. It should be noted that even with low concentrations (below 16 μg/mL), DS4 still have significant growth reduction of C. albicans, but were not toxic to human gingival fibroblasts. DS4 inhibited the transition from yeast to hyphae, and decreased the biofilm formation by reducing the biofilm mass weight. Surface morphological changes in the yeast cell membrane were observed following exposure to DS4. The gene expression analyses revealed that DS4 significantly decreased the expression of EAP1 and HWP1 genes. Overall results suggest the potential use of DS4 as an antifungal therapy to prevent C. albicans pathogenesis.
Identifiants
pubmed: 32691243
doi: 10.1007/s12602-020-09685-0
pii: 10.1007/s12602-020-09685-0
doi:
Substances chimiques
Amphibian Proteins
0
Antimicrobial Cationic Peptides
0
Fungal Proteins
0
HWP1 protein, Candida albicans
0
Membrane Glycoproteins
0
dermaseptin 4 protein, Phyllomedusa
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
287-298Références
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