The present study was undertaken to investigate whether less pathogenic species () express a fibronectin receptor (FNr) antigenically related to α5βl integrin, which mediates their binding to fibronectin (FN). By flow cytometric analysis, a monoclonal antibody (MAb) directed against human α5 integrin subunit (clone SAM-1) and two different antisera to FNr positively stained , with the greatest expression observed for No or only marginal immunoreactivity was found on yeasts specifically adhered to FN; higher levels of adhesion were found for with respect to Less pathogenic Candida spp. bound to the Arg-Gly-Asp (RGD) containing 120-kDa fragment of FN and adhesion to intact FN was markedly inhibited by Gly-Arg-Gly-Asp-Ser-Pro (GRGDSP), but not by Gly-Arg-Gly-Glu-Ser-Pro (GRGESP) peptides. In addition, anti-α5 SAM-1 MAb and both anti-FNr antisera strongly blocked binding of less pathogenic spp. to FN. Overall, these results indicate that less pathogenic spp., including , express a receptor antigenically related to α5βl integrin which mediates their adhesion to FN.


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