Send to

Choose Destination
Exp Clin Immunogenet. 1996;13(3-4):161-72.

Temperature-dependent surface expression of the beta-2-integrin analogue of Candida albicans and its role in adhesion to the human endothelium.

Author information

Institut für Hygiene, University of Innsbruck, Austria.


Candida albicans has become one of the most important pathogens in intensive care units. Adherence of C. albicans to the vascular endothelium is believed to represent a critical step in the pathogenesis of disseminated candidiasis and may involve molecules analogous to human beta 2-integrins such as the complement receptor 3 (CR3) analogue of C. albicans (C.a.-CR3). Its expression was detected by a sensitive rosetting assay when Candida was present in its hyphal form but not in its yeast form, the latter being generally considered to be less pathogenic. However, the presence of hyphae alone was not sufficient: C.a.-CR3 expression was found to be temperature-dependent for 4 (out of 10) clinical isolates. Two rosetted better after growth at 30 degrees C, the other 2 after growth at 37 degrees C. This temperature dependence was most pronounced for 1 laboratory strain: C.a.-CR3 expression was best at 30 degrees C and markedly decreased with increasing temperatures. At 37 degrees C no rosettes were detected at all. Modifications of the culture conditions (e.g. agitation, pH) exerted a marked influence on the morphology of this strain but always allowed rosette formation once hyphae were formed at 30 degrees C. However, none of these modifications was able to induce rosettes at 37 degrees C. Adhesion of C. albicans isolates to an endothelial cell line was also temperature-dependent but not strongly correlated with C.a.-CR3 expression. Most strains exhibited a better adherence when grown at 30 degrees C. This finding may be of importance for exogenous infections, with Candida spp. invading the body from the outside, where the temperature is usually lower than the physiological body temperature.

[Indexed for MEDLINE]

Supplemental Content

Loading ...
Support Center