Aspartyl proteinase, phospholipase, esterase and hemolysin activities of clinical isolates of the Candida parapsilosis species complex. (April 2013)
- Record Type:
- Journal Article
- Title:
- Aspartyl proteinase, phospholipase, esterase and hemolysin activities of clinical isolates of the Candida parapsilosis species complex. (April 2013)
- Main Title:
- Aspartyl proteinase, phospholipase, esterase and hemolysin activities of clinical isolates of the Candida parapsilosis species complex
- Authors:
- Treviño-Rangel, Rogelio de J.
González, J. Gerardo
González, Gloria M. - Abstract:
- <abstract> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>Candida parapsilosis</italic> is considered as an important emerging fungal pathogen and was recently found to be a complex that include three species, i.e., <italic>Candida parapsilosis</italic> sensu stricto, <italic>Candida orthopsilosis</italic> and <italic>Candida metapsilosis</italic>. The aim of this study was to determine the <italic>in vitro</italic> aspartyl proteinase, phospholipase, esterase and hemolysin activities of 65 clinical isolates of the <italic>C. parapsilosis</italic> complex, which had been previously identified by RFLP-<italic>Ban</italic>I analysis. Of the enzymes evaluated, aspartyl proteinase was the least produced by the <italic>C. parapsilosis</italic> species complex. Phospholipase and esterase were strongly expressed by <italic>C. orthopsilosis</italic> (67% of isolates), while 10% and 13% of <italic>C. parapsilosis</italic> sensu stricto isolates were strong producers, respectively, of these two enzymes. In contrast, high production of both enzymes was not detected in <italic>C. metapsilosis</italic>. Hemolysin activity was significantly more abundant in <italic>C. orthopsilosis</italic> (87%) than <italic>C. parapsilosis</italic> sensu stricto (67%). Overall, <italic>C. orthopsilosis</italic> isolates were statistically associated with the production of hemolysins (<italic>P</italic> = 0.048) and phospholipases (<italic>P</italic> &lt; 0.0001) compared to isolates<abstract> <title> <x xml:space="preserve">Abstract</x> </title> <p> <italic>Candida parapsilosis</italic> is considered as an important emerging fungal pathogen and was recently found to be a complex that include three species, i.e., <italic>Candida parapsilosis</italic> sensu stricto, <italic>Candida orthopsilosis</italic> and <italic>Candida metapsilosis</italic>. The aim of this study was to determine the <italic>in vitro</italic> aspartyl proteinase, phospholipase, esterase and hemolysin activities of 65 clinical isolates of the <italic>C. parapsilosis</italic> complex, which had been previously identified by RFLP-<italic>Ban</italic>I analysis. Of the enzymes evaluated, aspartyl proteinase was the least produced by the <italic>C. parapsilosis</italic> species complex. Phospholipase and esterase were strongly expressed by <italic>C. orthopsilosis</italic> (67% of isolates), while 10% and 13% of <italic>C. parapsilosis</italic> sensu stricto isolates were strong producers, respectively, of these two enzymes. In contrast, high production of both enzymes was not detected in <italic>C. metapsilosis</italic>. Hemolysin activity was significantly more abundant in <italic>C. orthopsilosis</italic> (87%) than <italic>C. parapsilosis</italic> sensu stricto (67%). Overall, <italic>C. orthopsilosis</italic> isolates were statistically associated with the production of hemolysins (<italic>P</italic> = 0.048) and phospholipases (<italic>P</italic> &lt; 0.0001) compared to isolates of <italic>C. parapsilosis</italic> sensu stricto or <italic>C. metapsilosis</italic>. Furthermore, a statistical association was found between isolates recovered from blood and phospholipase production (<italic>P</italic> = 0.017). The distribution of isolates obtained from blood was 30% of <italic>C. parapsilosis</italic> sensu stricto, 67% of <italic>C. orthopsilosis</italic> and 20% of <italic>C. metapsilosis</italic>.</p> </abstract> … (more)
- Is Part Of:
- Medical mycology. Volume 51:Number 3(2013)
- Journal:
- Medical mycology
- Issue:
- Volume 51:Number 3(2013)
- Issue Display:
- Volume 51, Issue 3 (2013)
- Year:
- 2013
- Volume:
- 51
- Issue:
- 3
- Issue Sort Value:
- 2013-0051-0003-0000
- Page Start:
- 331
- Page End:
- 335
- Publication Date:
- 2013-04
- Subjects:
- Medical mycology -- Periodicals
Veterinary mycology -- Periodicals
Mycology -- Periodicals
Mycoses -- Periodicals
Pathogenic fungi -- Periodicals
616.969005 - Journal URLs:
- http://mmy.oxfordjournals.org/ ↗
http://ukcatalogue.oup.com/ ↗ - DOI:
- 10.3109/13693786.2012.712724 ↗
- Languages:
- English
- ISSNs:
- 1369-3786
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5530.168000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 2980.xml