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Thionin-like peptide from Capsicum annuum fruits: mechanism of action and synergism with fluconazole against Candida species

Authors
  • Taveira, Gabriel B.1
  • Carvalho, André O.1
  • Rodrigues, Rosana2
  • Trindade, Fernanda G.3
  • Da Cunha, Maura3
  • Gomes, Valdirene M.1
  • 1 Universidade Estadual do Norte Fluminense, Laboratório de Fisiologia e Bioquímica de Microrganismos, Centro de Biociências e Biotecnologia, Campos dos Goytacazes, RJ, 28013-602,, Brazil , Campos dos Goytacazes (Brazil)
  • 2 Universidade Estadual do Norte Fluminense, Laboratório de Melhoramento Genético Vegetal, Centro de Ciências e Tecnologias Agropecuárias, Campos dos Goytacazes, RJ, 28013-602,, Brazil , Campos dos Goytacazes (Brazil)
  • 3 Universidade Estadual do Norte Fluminense, Laboratório de Biologia Celular e Tecidual, Centro de Biociências e Biotecnologia, Campos dos Goytacazes, RJ, 28013-602,, Brazil , Campos dos Goytacazes (Brazil)
Type
Published Article
Journal
BMC Microbiology
Publisher
Springer (Biomed Central Ltd.)
Publication Date
Jan 27, 2016
Volume
16
Issue
1
Identifiers
DOI: 10.1186/s12866-016-0626-6
Source
Springer Nature
Keywords
License
Green

Abstract

BackgroundThionins are a family of plant antimicrobial peptides (AMPs), which participate in plant defense system against pathogens. Here we describe some aspects of the CaThi thionin-like action mechanism, previously isolated from Capsicum annuum fruits. Thionin-like peptide was submitted to antimicrobial activity assays against Candida species for IC50 determination and synergism with fluconazole evaluation. Viability and plasma membrane permeabilization assays, induction of intracellular ROS production analysis and CaThi localization in yeast cells were also investigated.ResultsCaThi had strong antimicrobial activity against six tested pathogenic Candida species, with IC50 ranging from 10 to 40 μg.mL−1. CaThi antimicrobial activity on Candida species was candidacidal. Moreover, CaThi caused plasma membrane permeabilization in all yeasts tested and induces oxidative stresses only in Candida tropicalis. CaThi was intracellularly localized in C. albicans and C. tropicalis, however localized in nuclei in C. tropicalis, suggesting a possible nuclear target. CaThi performed synergistically with fluconazole inhibiting all tested yeasts, reaching 100 % inhibition in C. parapsilosis. The inhibiting concentrations for the synergic pair ranged from 1.3 to 4.0 times below CaThi IC50 and from zero to 2.0 times below fluconazole IC50.ConclusionThe results reported herein may ultimately contribute to future efforts aiming to employ this plant-derived AMP as a new therapeutic substance against yeasts.

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