This study demonstrated the anti-adherent activity of caspofungin but indicated a reduced effect in the case of in vitro fluconazole resistance. These results indicated a possible relationship between the efficiency of caspofungin to inhibit the first step of the development of C. albicans biofilm and the resistance of C. albicans to fluconazole in vitro.

Azole antifungals act by inhibiting the activity of a lanosterol demethylase involved in the generation of the ergosterol of the cellular membrane of fungi. These drugs could also have action on other yeast components, like secreted aspartyl proteases. We demonstrate in this study that the in vitro secretion of a metallopeptidase could be modified during the growth of Candida albicans with subinhibitory concentrations of some azoles. Eight isolates of this yeast have been cultivated in presence of MIC, MIC/2 and MIC/4 of voriconazole, fluconazole and itraconazole. The presence of voriconazole and fluconazole decreased the secretion of the metallopeptidase in the culture medium, whereas itraconazole increased this secretion for three isolates. This study points to the fact that some antifungals, given in prophylaxis, could act in an unfavourable way on some potential factors of pathogenicity.

Some carbohydrates are known to decrease the attachment of Acanthamoeba sp. to biological surfaces. By a method based on the reduction of a tetrazolium salt (XTT) by the mitochondrial dehydrogenases of the parasites, d-mannose and alpha-d-mannopyranoside have been shown to reduce Acanthamoeba attachment to inert surfaces, indicating that the mannose binding protein of Acanthamoeba trophozoites is involved in adherence to inert surfaces. The reduction in attachment is dose dependant and is not linked with a potential toxicity of the carbohydrates. All the species of Acanthamoeba tested were concerned by this mannose binding protein, but the adhesion of A. culbertsoni was also reduced by the presence of glucose.

Some carbohydrates are known to decrease the attachment of Acanthamoeba sp. to biological surfaces. By a method based on the reduction of a tetrazolium salt (XTT) by the mitochondrial dehydrogenases of the parasites, d-mannose and alpha-d-mannopyranoside have been shown to reduce Acanthamoeba attachment to inert surfaces, indicating that the mannose binding protein of Acanthamoeba trophozoites is involved in adherence to inert surfaces. The reduction in attachment is dose dependant and is not linked with a potential toxicity of the carbohydrates. All the species of Acanthamoeba tested were concerned by this mannose binding protein, but the adhesion of A. culbertsoni was also reduced by the presence of glucose.