Identification of an elongation factor 1Bγ protein with glutathione transferase activity in both yeast and mycelial morphologies from human pathogenic Blastoschizomyces capitatus.

Autor: Allocati N; Department of Experimental and Clinical Sciences, University 'G. d'Annunzio', Via dei Vestini, 66013, Chieti, Italy, allocati@unich.it., Masulli M, Del Boccio P, Pieragostino D, D'Antonio D, Sheehan D, Di Ilio C
Jazyk: angličtina
Zdroj: Folia microbiologica [Folia Microbiol (Praha)] 2014 Mar; Vol. 59 (2), pp. 107-13. Date of Electronic Publication: 2013 Aug 03.
DOI: 10.1007/s12223-013-0273-3
Abstrakt: Blastoschizomyces capitatus is an uncommon, opportunistic pathogenic fungus, which causes invasive and disseminated infections. This microorganism is normally present in both environmental and normal human flora. Within a host, B. capitatus is able to grow in both unicellular yeast and multicellular filamentous growth forms. In this study, we obtained in vitro morphological conversion of B. capitatus from yeast-to-mycelial phase to investigate the presence and expression of glutathione transferase (GST) enzymes in both cell forms. A protein with GST activity using the model substrate 1-chloro-2,4-dinitrobenzene was detected in both morphologies and identified by tandem mass spectrometry as a eukaryotic elongation factor 1Bγ (eEF1Bγ) protein, a member of the GST superfamily. No significant difference in GST-specific activity and kinetic constants were observed between mycelial and yeast forms, indicating that eEF1Bγ protein did not show differential expression between the two phases.
Databáze: MEDLINE
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