The binding of Candida tropicalis to fibronectin (FN) was studied in order to characterize the FN receptor in this species. FN binding was saturable at a concentration of 1.8 x 10(-9) M and exhibited a Kd of 2.3 x 10(-9) M and a receptor density of 854 receptors per cell. Extracts of C. tropicalis cell membrane at dilutions of 1:100-1:1000 significantly inhibited the binding of 3H-labeled FN to C. tropicalis cells (P < .03). Purified FN, antibodies to the integrin alpha 5 beta 1 (FN receptor on human placenta), and antibodies specific for the integrin beta 1 subunit recognized a C. tropicalis membrane protein of 125 +/- 25 kDa on immunoblots. Immunoprecipitation of radiolabeled proteins from C. tropicalis with purified human FN yielded a protein of 105 +/- 15 kDa. Thus, C. tropicalis expresses a protein with antigenic and functional similarity to the vertebrate beta 1 integrin FN receptor.