Jpn. J. Infect. Dis., 54, 229-236, 2001
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Original Article
Characterization of Phenotype-Based Pathogenic Determinants of Various Candida albicans Strains in Jordan
Khaled H. Abu-Elteen*, Ali Z. Elkarmi and Mawieh Hamad
Department of Biological Sciences, Faculty of Science and Arts, The Hashemite University, P.O. Box 330077, Zarqa 13133, Jordan
(Received October 15, 2001. December 25, 2001)
SUMMARY: Sixty-six clinical isolates of Candida albicans
representing 14 different strain types were tested for their phospholipase
and proteinase activities in correlation with adherence to buccal
epithelial cells (BECs) and lethality to mice. Variations in phospholipase
and proteinase production as well as adherence to BECs were observed
both among isolates of the same strain type and between isolates
of different strain types. All isolates tested, irrespective of
strain type, produced low levels of phopholipase (0.5 mm for strain
-BCD- and 2.7 mm for strain ABC--) and acid proteinase (0.6 mm
for strain A---E and 2.2 mm for strain --C--). A correlation was
noted between adherence, phospholipase and proteinase production,
and lethality to mice. C. albicans isolates, which adhered
most strongly to BECs, exhibited higher levels of phospholipase
and proteinase activities as well as higher pathogenicity. This
was most evident in strain type --C--, which exhibited higher
adherence ability (mean 717 ± 21 yeasts/100 BEC), and proteinase
activity (mean 2.2 mm), and relatively higher phospholipase activity
(mean 2.4 mm) compared with those of other strains. Additionally,
this type was more prevalent and showed significantly higher levels
of tissue colonization in the liver, kidneys, and spleen compared
with most other strain types in both subjects with healthy dentates
and complete denture wearers. These results clearly demonstrate
the significant role of phospholipase and proteinase activities
on the adherence of C. albicans and their overall influence
on the pathogenesis of Candida species.
* Corresponding author: Tel/Fax: +962-6-4128772, E-mail: Salma@hu.edu.jo
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