51
Views
0
CrossRef citations to date
0
Altmetric
Research Article

Analysis of the response of Candida albicans cells to Silver(I)

, &
Pages 498-505 | Received 07 Jul 2009, Accepted 30 Jul 2009, Published online: 06 Apr 2010
 

Abstract

The response of the pathogenic yeast Candida albicans to the silver(I) perchlorate salt (AgClO4) was assessed. By employing an anti-phospho-p38 MAPK antibody, dual phosphorylation of a high osmolarity protein (Hog1p) in C. albicans in the presence of AgClO4 was demonstrated. Phosphorylation of C. albicans Hog1p in response to hydrogen peroxide or AgClO4 resulted in the translocation of this mitogen-activated protein (MAP) kinase to the nucleus. Nuclear translocation of C. albicans activating protein-1 (Cap1p) was demonstrated by Western blot analysis and detected using polyclonal anti-Cap1p antibody. Upon AgClO4-induced translocation of Cap1p there was a concomitant activation of genes coding for glutathione reductase-1 and Mn-superoxide dismutase but no increase in the expression of flavin oxidoreductase or mitochondrial processing protease was recorded. In addition, exposure to AgClO4 increased the activity of superoxide dismutase, glutathione reductase and catalase. The activation of C. albicans oxidative stress response genes and enzymes following exposure to AgClO4 is evidence of the generation of oxidative stress within this medically important yeast.

Acknowledgements

This work was supported by funding from the Higher Education Authority of Ireland through the Programme for Research in Third Level Institutes III.

Declaration of interest: The authors have no conflicts of interest to declare. The authors alone are responsible for the content and writing of this paper.

This paper was first published online on Early Online on 29 September 2009.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.