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dc.contributor.author
Soares, Júlia Ribeiro
dc.contributor.author
José Tenório de Melo, Edésio
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da Cunha, Maura
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Fernandes, Kátia Valevski Sales
dc.contributor.author
Taveira, Gabriel Bonan
dc.contributor.author
da Silva Pereira, Lidia
dc.contributor.author
Pimenta, Samy
dc.contributor.author
Trindade, Fernanda Gomes
dc.contributor.author
Regente, Mariana Clelia
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dc.contributor.author
Pinedo, Marcela Lilian
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de la Canal, Laura
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Gomes, Valdirene Moreira
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de Oliveira Carvalho, André
dc.date.available
2018-11-28T18:06:24Z
dc.date.issued
2017-01
dc.identifier.citation
Soares, Júlia Ribeiro; José Tenório de Melo, Edésio; da Cunha, Maura; Fernandes, Kátia Valevski Sales; Taveira, Gabriel Bonan; et al.; Interaction between the plant ApDef1 defensin and Saccharomyces cerevisiae results in yeast death through a cell cycle- and caspase-dependent process occurring via uncontrolled oxidative stress; Elsevier Science; Biochimica et Biophysica Acta- General Subjects; 1861; 1; 1-2017; 3429-3443
dc.identifier.issn
0304-4165
dc.identifier.uri
http://hdl.handle.net/11336/65475
dc.description.abstract
Background Plant defensins were discovered at beginning of the 90s' however, their precise mechanism of action is still unknown. Herein, we studied ApDef1-Saccharomyces cerevisiae interaction. Methods ApDef1-S. cerevisiae interaction was studied by determining the MIC, viability and death kinetic assays. Viability assay was repeated with hydroxyurea synchronized-yeast and pretreated with CCCP. Plasma membrane permeabilization, ROS induction, chromatin condensation, and caspase activation analyses were assessed through Sytox green, DAB, DAPI and FITC-VAD-FMK, respectively. Viability assay was done in presence of ascorbic acid and Z-VAD-FMK. Ultrastructural analysis was done by electron microscopy. Results ApDef1 caused S. cerevisiae cell death and MIC was 7.8 μM. Whole cell population died after 18 h of ApDef1 interaction. After 3 h, 98.76% of synchronized cell population died. Pretreatment with CCCP protected yeast from ApDef1 induced death. ApDef1-S. cerevisiae interaction resulted in membrane permeabilization, H2O2 increased production, chromatin condensation and caspase activation. Ascorbic acid prevented yeast cell death and membrane permeabilization. Z-VAD-FMK prevented yeast cell death. Conclusions ApDef1-S. cerevisiae interaction caused cell death through cell cycle dependentprocess which requires preserved membrane potential. After interaction, yeast went through uncontrolled ROS production and accumulation, which led to plasma membrane permeabilization, chromatin condensation and, ultimately, cell death by activation of caspase-dependent apoptosis via. General significance We show novel requirements for the interaction between plant defensin and fungi cells, i.e. cell cycle phase and membrane potential, and we indicate that membrane permeabilization is probably caused by ROS and therefore, it would be an indirect event of the ApDef1-S. cerevisiae interaction.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Elsevier Science
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Antimicrobial Peptides
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Caspase
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Cell Cycle
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Membrane Permeabilization
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Microbicidal
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Ros Induction
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Interaction between the plant ApDef1 defensin and Saccharomyces cerevisiae results in yeast death through a cell cycle- and caspase-dependent process occurring via uncontrolled oxidative stress
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-10-23T14:12:28Z
dc.journal.volume
1861
dc.journal.number
1
dc.journal.pagination
3429-3443
dc.journal.pais
Países Bajos
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dc.journal.ciudad
Amsterdam
dc.description.fil
Fil: Soares, Júlia Ribeiro. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.description.fil
Fil: José Tenório de Melo, Edésio. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.description.fil
Fil: da Cunha, Maura. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.description.fil
Fil: Fernandes, Kátia Valevski Sales. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.description.fil
Fil: Taveira, Gabriel Bonan. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.description.fil
Fil: da Silva Pereira, Lidia. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.description.fil
Fil: Pimenta, Samy. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.description.fil
Fil: Trindade, Fernanda Gomes. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.description.fil
Fil: Regente, Mariana Clelia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Pinedo, Marcela Lilian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: de la Canal, Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Mar del Plata. Instituto de Investigaciones Biológicas. Universidad Nacional de Mar del Plata. Facultad de Ciencias Exactas y Naturales. Instituto de Investigaciones Biológicas; Argentina
dc.description.fil
Fil: Gomes, Valdirene Moreira. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.description.fil
Fil: de Oliveira Carvalho, André. Universidade Estadual Do Norte Fluminense Darcy Ribeiro; Brasil
dc.journal.title
Biochimica et Biophysica Acta- General Subjects
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.bbagen.2016.09.005
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0304416516303270
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