Jakab E, Paulsson M, Ascencio F, Ljungh A
Department of Medical Microbiology, University of Lund, Sweden.
APMIS. 1993 Mar;101(3):187-93.
Expression of binding to vitronectin (Vn or S-protein) and fibronectin (Fn) was common among clinical isolates of Candida albicans. Growth at 37 degrees C enhanced expression of both Vn and Fn binding. Some strains expressed higher binding after growth in liquid media and others after growth on solid media. Most strains expressed higher cell surface hydrophobicity after growth on agar media. Vn binding was less influenced by expression of cell surface hydrophobicity than Fn binding. Vn binding to yeast cells was optimal around pH 4 and Fn binding around pH 6. Binding to soluble Vn was inhibited by unlabelled Vn and to a lesser extent by Fn. Fn binding to the same C. albicans strain was inhibited by unlabelled Fn, Vn, fibrinogen and to some extent collagens. C. albicans strain 3248 expressed specific high binding of Vn, and high binding of Fn. Binding of both proteins was sensitive to heat and protease treatment, but in different ways. Vn binding differed significantly from the earlier reported Fn binding and may represent a novel type of tissue adherence.
白色念珠菌临床分离株中普遍存在与玻连蛋白(Vn或S蛋白)和纤连蛋白(Fn)的结合表达。37℃培养可增强Vn和Fn结合的表达。一些菌株在液体培养基中生长后表达更高的结合,而另一些菌株在固体培养基中生长后表达更高。大多数菌株在琼脂培养基上生长后表现出更高的细胞表面疏水性。与Fn结合相比,Vn结合受细胞表面疏水性表达的影响较小。Vn与酵母细胞的结合在pH4左右最佳,Fn结合在pH6左右最佳。未标记的Vn可抑制与可溶性Vn的结合,Fn在较小程度上也有抑制作用。未标记的Fn、Vn、纤维蛋白原以及在一定程度上的胶原蛋白可抑制Fn与同一白色念珠菌菌株的结合。白色念珠菌菌株3248表现出对Vn的特异性高结合以及对Fn的高结合。两种蛋白质的结合对热和蛋白酶处理敏感,但方式不同。Vn结合与早期报道的Fn结合有显著差异,可能代表一种新型的组织黏附。