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Inhibition of Paracoccidioides lutzii Pb01 isocitrate lyase by the natural compound argentilactone and its semi-synthetic derivatives.
PLoS One. 2014; 9(4):e94832.Plos

Abstract

The dimorphic fungus Paracoccidioides spp. is responsible for paracoccidioidomycosis, the most prevalent systemic mycosis in Latin America, causing serious public health problems. Adequate treatment of mycotic infections is difficult, since fungi are eukaryotic organisms with a structure and metabolism similar to those of eukaryotic hosts. In this way, specific fungus targets have become important to search of new antifungal compound. The role of the glyoxylate cycle and its enzymes in microbial virulence has been reported in many fungal pathogens, including Paracoccidioides spp. Here, we show the action of argentilactone and its semi-synthetic derivative reduced argentilactone on recombinant and native isocitrate lyase from Paracoccidioides lutzii Pb01 (PbICL) in the presence of different carbon sources, acetate and glucose. Additionally, argentilactone and its semi-synthetic derivative reduced argentilactone exhibited relevant inhibitory activity against P. lutzii Pb01 yeast cells and dose-dependently influenced the transition from the mycelium to yeast phase. The other oxygenated derivatives tested, epoxy argentilactone and diol argentilactone-, did not show inhibitory action on the fungus. The results were supported by in silico experiments.

Links

Publisher Full Text
ncbi.nlm.nih.gov
dx.plos.org
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Authors+Show Affiliations

Prado RS
Laboratório de Biologia Molecular, Instituto de Ciências Biológicas, Universidade Federal de Goiás, Goiânia, Goiás, Brazil.
Alves RJ
Laboratório de Produtos Naturais, Instituto de Química, Universidade Federal de Goiás, Goiânia, Goiás, Brazil.
Oliveira CM
Laboratório de Produtos Naturais, Instituto de Química, Universidade Federal de Goiás, Goiânia, Goiás, Brazil.
Kato L
Laboratório de Produtos Naturais, Instituto de Química, Universidade Federal de Goiás, Goiânia, Goiás, Brazil.
Silva RA
Núcleo Colaborativo de BioSistemas, Campus Jataí, Universidade Federal de Goiás, Jataí, Goiás, Brazil.
Quintino GO
Núcleo Colaborativo de BioSistemas, Campus Jataí, Universidade Federal de Goiás, Jataí, Goiás, Brazil.
do Desterro Cunha S
Instituto de Química, Departamento de Química Orgânica, Universidade Federal da Bahia, Salvador, Bahia, Brazil.
de Almeida Soares CM
Laboratório de Biologia Molecular, Instituto de Ciências Biológicas, Universidade Federal de Goiás, Goiânia, Goiás, Brazil.
Pereira M
Laboratório de Biologia Molecular, Instituto de Ciências Biológicas, Universidade Federal de Goiás, Goiânia, Goiás, Brazil.

MeSH

Binding SitesEnzyme InhibitorsIsocitrate LyaseLactonesMolecular Docking SimulationMolecular Dynamics SimulationMyceliumParacoccidioidesSolventsStructural Homology, ProteinThermodynamics

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

24752170

Citation

Prado, Renata Silva do, et al. "Inhibition of Paracoccidioides Lutzii Pb01 Isocitrate Lyase By the Natural Compound Argentilactone and Its Semi-synthetic Derivatives." PloS One, vol. 9, no. 4, 2014, pp. e94832.
Prado RS, Alves RJ, Oliveira CM, et al. Inhibition of Paracoccidioides lutzii Pb01 isocitrate lyase by the natural compound argentilactone and its semi-synthetic derivatives. PLoS One. 2014;9(4):e94832.
Prado, R. S., Alves, R. J., Oliveira, C. M., Kato, L., Silva, R. A., Quintino, G. O., do Desterro Cunha, S., de Almeida Soares, C. M., & Pereira, M. (2014). Inhibition of Paracoccidioides lutzii Pb01 isocitrate lyase by the natural compound argentilactone and its semi-synthetic derivatives. PloS One, 9(4), e94832. https://doi.org/10.1371/journal.pone.0094832
Prado RS, et al. Inhibition of Paracoccidioides Lutzii Pb01 Isocitrate Lyase By the Natural Compound Argentilactone and Its Semi-synthetic Derivatives. PLoS One. 2014;9(4):e94832. PubMed PMID: 24752170.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Inhibition of Paracoccidioides lutzii Pb01 isocitrate lyase by the natural compound argentilactone and its semi-synthetic derivatives. AU - Prado,Renata Silva do, AU - Alves,Ricardo Justino, AU - Oliveira,Cecília Maria Alves de, AU - Kato,Lucília, AU - Silva,Roosevelt Alves da, AU - Quintino,Guilherme Oliveira, AU - do Desterro Cunha,Silvio, AU - de Almeida Soares,Célia Maria, AU - Pereira,Maristela, Y1 - 2014/04/21/ PY - 2013/12/02/received PY - 2014/03/20/accepted PY - 2014/4/23/entrez PY - 2014/4/23/pubmed PY - 2015/1/21/medline SP - e94832 EP - e94832 JF - PloS one JO - PLoS One VL - 9 IS - 4 N2 - The dimorphic fungus Paracoccidioides spp. is responsible for paracoccidioidomycosis, the most prevalent systemic mycosis in Latin America, causing serious public health problems. Adequate treatment of mycotic infections is difficult, since fungi are eukaryotic organisms with a structure and metabolism similar to those of eukaryotic hosts. In this way, specific fungus targets have become important to search of new antifungal compound. The role of the glyoxylate cycle and its enzymes in microbial virulence has been reported in many fungal pathogens, including Paracoccidioides spp. Here, we show the action of argentilactone and its semi-synthetic derivative reduced argentilactone on recombinant and native isocitrate lyase from Paracoccidioides lutzii Pb01 (PbICL) in the presence of different carbon sources, acetate and glucose. Additionally, argentilactone and its semi-synthetic derivative reduced argentilactone exhibited relevant inhibitory activity against P. lutzii Pb01 yeast cells and dose-dependently influenced the transition from the mycelium to yeast phase. The other oxygenated derivatives tested, epoxy argentilactone and diol argentilactone-, did not show inhibitory action on the fungus. The results were supported by in silico experiments. SN - 1932-6203 UR - https://www.unboundmedicine.com/medline/citation/24752170/Inhibition_of_Paracoccidioides_lutzii_Pb01_isocitrate_lyase_by_the_natural_compound_argentilactone_and_its_semi_synthetic_derivatives_ L2 - https://dx.plos.org/10.1371/journal.pone.0094832 DB - PRIME DP - Unbound Medicine ER -