Candida albicans expresses a fibronectin receptor antigenically related to alpha 5 beta 1 integrin.

Cell adhesion molecules, by regulating host-micro-organism interaction, play a major role in the pathogenesis of infectious diseases. The present study was undertaken to investigate the expression of the fibronectin (FN) receptor prototype, alpha 5 beta 1 integrin, on Candida albicans and its involvement in the adhesion to FN. By immunofluorescence and fluorescence activated cell sorter (FACS) analysis, several monoclonal antibodies (mAbs) directed against human alpha 5 or beta 1 integrin subunits, or two different antisera to FN receptor positively stained C. albicans yeast and germ tube phases, this immunoreactivity increasing upon germ tube transition. Twenty-five to thirty per cent of [3H]glucose-labelled Candida yeasts specifically adhered to FN and this adhesion was increased upon germ tube transition. C. albicans yeast and germ tube forms bound to an RGD-containing 120 kDa tryptic fragment of FN and adhesion to FN was markedly inhibited by GRGDSP, but not GRGESP peptides. Moreover, binding of both C. albicans phases to FN was strongly inhibited by anti-alpha 5 SAM-1 mAb, or both anti-fibronectin receptor (FNr) antisera. Overall these results indicate that C. albicans yeast and germ tube phases express a receptor antigenically related to alpha 5 beta 1 integrin which mediates their adhesion to FN. The alpha 5 beta 1 integrin-like receptor expression on C. albicans could be relevant for fungus-host interaction and in the dissemination process of Candida infection.