Fungal cell adhesion molecules in Candida albicans.

Adherence of Candida albicans to host tissues is considered a crucial step in the pathogenesis of candidiasis. Using in vitro assays, it was demonstrated that the yeast-mycelium transition was an important phenomenon in the acquisition of adhesive properties. Proteins with MWs of 60, 68, 200 and greater than 200 kDa seemed to be involved in germ tube adherence to plastic surfaces. Likewise, recent investigations have revealed that C. albicans expresses on its surface receptors which interact with a wide variety of host proteins, particularly some extracellular matrix components like fibronectin, laminin and collagen. Plasmatic components, such as fibrinogen, iC3b and C3d, have also been proposed as mediators of adherence of C. albicans. Thus, by their reaction with laminin, fibrinogen and C3d, the mannoproteins of 68 and 60 kDa demonstrated multiple biological activities. Proteins of similar MWs were detected as C3d and iC3b receptors, the latter showing similarities with the neutrophil CR3. Based upon the antigenic, structural and functional homologies between the candidal receptors and mammalian integrins, it was postulated that these fungal cell adhesion molecules (F-CAM) are members of the integrin family. Interactions with host proteins and molecular mimicry of mammalian adhesion molecules may be a fertile area for further research.