DeMuri G P, Hostetter M K
Department of Pediatrics, University of Minnesota, Minneapolis, USA.
J Infect Dis. 1996 Jul;174(1):127-32. doi: 10.1093/infdis/174.1.127.
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.
为了鉴定热带假丝酵母中的纤连蛋白(FN)受体,对热带假丝酵母与纤连蛋白的结合进行了研究。在1.8×10⁻⁹ M的浓度下,FN结合具有饱和性,其解离常数(Kd)为2.3×10⁻⁹ M,每个细胞的受体密度为854个受体。热带假丝酵母细胞膜提取物在1:100 - 1:1000的稀释度下显著抑制³H标记的FN与热带假丝酵母细胞的结合(P < 0.03)。纯化的FN、抗整合素α5β1(人胎盘上的FN受体)抗体以及针对整合素β1亚基的特异性抗体在免疫印迹中识别出一种125±25 kDa的热带假丝酵母膜蛋白。用纯化的人FN对热带假丝酵母的放射性标记蛋白进行免疫沉淀,得到一种105±15 kDa的蛋白。因此,热带假丝酵母表达一种与脊椎动物β1整合素FN受体具有抗原性和功能相似性的蛋白。