Calderone R A, Braun P C
Department of Microbiology, Georgetown University School of Medicine, Washington, D.C. 20007.
Microbiol Rev. 1991 Mar;55(1):1-20. doi: 10.1128/mr.55.1.1-20.1991.
The cell surface of Candida albicans is composed of a variety of polysaccharides such as glucan, chitin, and mannan. The first two components primarily provide structure, while the mannan, often covalently linked to protein, constitutes the major antigen of the organism. Mannoproteins also have enzymatic activity (acid protease) and ligand-receptor functions. The complement receptors of C. albicans appear to be mannoproteins that are required for the adherence of the organism to endothelial cells. This is certainly true of the CR3-like protein of C. albicans. Proof that the CR3 is the Candida receptor for endothelial cells is derived from two observations. First, mutants lacking CR3 activity are less adherent in vitro and, in fact, less virulent. Second, the ligand recognized by the CR3 receptor (C3bi) as well as anti-CR3 antibodies blocks adherence of the organism to endothelial cells. The CR2 of C. albicans appears to promote the adherence of the organism to plastic substrates. Unlike the CR2 of mammalian cells, the Candida CR2 recognizes ligands containing the RGD sequence of amino acids in addition to the C3d ligand, which does not contain the RGD sequence. There is uncertainty as to whether the Candida CR2 and CR3 are, in fact, different proteins. A mannoprotein has also been described as the adhesin for epithelial cells. In this case, the receptor has a lectinlike activity and recognizes fucose- or glucosamine-containing glycoproteins of epithelial cells, depending on the strain of C. albicans. The oligosaccharide component of the receptor is probably not involved in ligand recognition and may serve to stabilize the receptor. However, the oligosaccharide factor 6 epitope of mannan may also provide adhesin activity in the recognition of epithelial cells. Mannoproteins can be extracted from cells by a number of reagents. Zymolyase, for instance, tends to remove structural mannoproteins, which contain relatively little protein and are linked to glucan. Reagents such as dithiothreitol, on the other hand, tend to extract mannoproteins containing higher amounts of protein that appear to have receptor function. The mannoproteins of C. albicans are dynamically expressed and may be growth phase and growth form specific.
白色念珠菌的细胞表面由多种多糖组成,如葡聚糖、几丁质和甘露聚糖。前两种成分主要提供结构支撑,而通常与蛋白质共价连接的甘露聚糖则构成了该生物体的主要抗原。甘露糖蛋白还具有酶活性(酸性蛋白酶)和配体 - 受体功能。白色念珠菌的补体受体似乎是甘露糖蛋白,是该生物体黏附于内皮细胞所必需的。白色念珠菌的CR3样蛋白肯定是这样。证明CR3是白色念珠菌与内皮细胞的受体来自两个观察结果。首先,缺乏CR3活性的突变体在体外黏附性较差,实际上毒力也较低。其次,CR3受体识别的配体(C3bi)以及抗CR3抗体可阻断该生物体与内皮细胞的黏附。白色念珠菌的CR2似乎促进该生物体与塑料底物的黏附。与哺乳动物细胞的CR2不同,白色念珠菌的CR2除了识别不含RGD序列的C3d配体外,还能识别含有RGD氨基酸序列的配体。白色念珠菌的CR2和CR3实际上是否为不同的蛋白质尚不确定。一种甘露糖蛋白也被描述为上皮细胞的黏附素。在这种情况下,该受体具有类似凝集素的活性,根据白色念珠菌的菌株不同,可识别上皮细胞中含岩藻糖或葡糖胺的糖蛋白。受体的寡糖成分可能不参与配体识别,也许起到稳定受体的作用。然而,甘露聚糖的寡糖因子6表位在识别上皮细胞时也可能提供黏附素活性。多种试剂可从细胞中提取甘露糖蛋白。例如,溶菌酶倾向于去除结构甘露糖蛋白,这些蛋白含相对较少的蛋白质且与葡聚糖相连。另一方面,二硫苏糖醇等试剂倾向于提取含较多蛋白质且似乎具有受体功能的甘露糖蛋白。白色念珠菌的甘露糖蛋白是动态表达的,可能具有生长阶段和生长形式特异性。