119
Views
3
CrossRef citations to date
0
Altmetric
Research Article

Proteinase, phospholipase, biofilm forming abilities and antifungal susceptibilities of Malaysian Candida isolates from blood cultures

, , &
Pages 556-560 | Received 11 Apr 2010, Accepted 24 Dec 2010, Published online: 24 Jan 2011
 

Abstract

This study was conducted to determine the proteinase, phospholipase, and biofilm forming abilities of Candida isolates in blood cultures of specimens from patients at the University Malaya Medical Center, Kuala Lumpur, Malaysia. Proteinase and phospholipase activities were detected in 93.7% and 73.3%, respectively, of 15 Candida albicans isolates. Amongst the 26 non-C. albicans Candida isolates, proteinase and phospholipase activities were detected in 88.5% and 7.7% of the isolates, respectively. There was no significant difference in the expression levels of proteinase amongst the Candida isolates studied (P = 0.272), but the phospholipase activity of C. albicans was significantly higher than that of the non-C. albicans Candida isolates (P = 0.003). There was no significant difference in the biofilm forming abilities of C. albicans and non-C. albicans Candida isolates on the polystyrene microtiter wells (P = 0.379). In addition, the findings of this study demonstrate increased resistance of Candida isolates in biofilms to amphotericin and fluconazole, as compared to their planktonic counterparts.

Acknowledgement

This study was supported by a research grant (FS240/2008B) provided by the University of Malaya, Malaysia. The assistance given by Ms Na SL and Ms Tan Hui Wee is greatly appreciated.

Declaration of interest: The authors report no conflicts of interest. The authors alone are responsible for the content and writing of the paper.

This paper was first published online on Early Online on 26 January 2011.

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.