Spreghini E, Gismondi A, Piccoli M, Santoni G
Department of Pharmacological Sciences and Experimental Medicine, University of Camerino, Camerino, Italy.
J Infect Dis. 1999 Jul;180(1):156-66. doi: 10.1086/314822.
The expression of integrin vitronectin (VN) receptors on Candida albicans yeasts and their involvement in the adhesion to VN were investigated. By immunofluorescence and cytofluorimetric analysis, several antibodies directed against human alphav, beta3, beta5, alphavbeta3, or alphavbeta5 integrin positively stained C. albicans yeasts. Biochemical analysis on yeast lysates with anti-human alphav, beta3, or beta5 antibody revealed molecular species of 130, 110, 100, and 84 kDa. The 130-kDa band was identified as alphav, whereas the doublet of 110/100 kDa and the 84-kDa band likely correspond to the beta3 and beta5 subunits, respectively. Some 48%-54% of Candida yeasts specifically adhered to VN, and this binding was strongly inhibited by anti-human alphav, beta3, alphavbeta3, and alphavbeta5 antibodies and by RGD- but not RGE-containing peptides. In addition, VN inhibited C. albicans adherence to a human endothelial cell line. Thus, C. albicans in the yeast phase expresses VN receptors antigenically related to the vertebrate alphavbeta3 and alphavbeta5 integrins, which mediate its adhesion to VN.
研究了白色念珠菌酵母上玻连蛋白（VN）受体的表达及其在与VN黏附中的作用。通过免疫荧光和细胞荧光分析，几种针对人αv、β3、β5、αvβ3或αvβ5整合素的抗体对白色念珠菌酵母进行了阳性染色。用抗人αv、β3或β5抗体对酵母裂解物进行生化分析，发现了分子量为130、110、100和84 kDa的分子种类。130 kDa的条带被鉴定为αv，而110/100 kDa的双峰和84 kDa的条带可能分别对应于β3和β5亚基。约48%-54%的念珠菌酵母特异性黏附于VN，这种结合被抗人αv、β3、αvβ3和αvβ5抗体以及含RGD而非含RGE的肽强烈抑制。此外，VN抑制白色念珠菌对人内皮细胞系的黏附。因此，酵母阶段的白色念珠菌表达与脊椎动物αvβ3和αvβ5整合素抗原相关的VN受体，这些受体介导其与VN的黏附。
