Cell adhesion molecules, by regulating host-micro-organism interaction, play major role in the pathogenesis of infectious diseases. The present study was undertaken to investigate the expression of the fibronectin (FN) receptor prototype, α5β1 integrin, on and its involvement in the adhesion to FN. By immunofluorescence and fluorescence activated cell sorter (FACS) analysis, several monoclonal antibodies (mAbs) directed against human α5 or β1 integrin subunits, or two different antisera to FN receptor positively stained yeast and germ tube phases, this immunoreactivity increasing upon germ tube transition. Twenty-five to thirty per cent of [H]glucose-labelled yeasts specifically adhered to FN and this adhesion was increased upon germ tube transition. yeast and gerr 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 phases to FN was strongly inhibited by anti-α5 SAM-1 mAb, or both anti-fibronectin receptor (FNr) antisera. Overall these results indicate that yeast and germ tube phases express a receptor antigenically related to α5β1 integrin which mediates their adhesion to FN. The α5β1 integrin-like receptor expression on could be relevant for fungus-host interaction and in the dissemination process of infection.


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