β-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3
β-1,2-linked oligomannosides from Candida albicans bind to a 32-kilodalton macrophage membrane protein homologous to the mammalian lectin galectin-3
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DOI：
10.1128/iai.68.8.4391-4398.2000
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发表时间：
2000-08-01
影响因子：
3.1
通讯作者：
Jouault, T
中科院分区：
文献类型：
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作者：
Fradin, C;Poulain, D;Jouault, T
白色念珠菌细胞壁表面存在 β-1,2 连接的寡甘露糖苷残基，与甘露聚糖和糖脂（磷脂甘露聚糖）相关。 β-1,2-连接的寡甘露糖苷残基充当巨噬细胞的粘附素并刺激这些细胞产生细胞因子。为了表征参与白色念珠菌β-1,2-寡甘露糖苷识别的巨噬细胞受体，我们使用了J774小鼠细胞系，该细胞系缺乏α-连接甘露糖残基特异性的受体。基于白色念珠菌酵母细胞或 β-1,2-低聚甘露糖苷缀合的牛血清白蛋白 (BSA) 上的亲和结合的一系列实验以及随后使用生物素化的缀合 BSA 的重复公开导致了 32-kDa 巨噬细胞蛋白的检测。对该 32 kDa 蛋白具有特异性的抗血清可抑制白色念珠菌与巨噬细胞的结合，并可用于免疫沉淀该分子。来自 32 kDa 胰蛋白酶消化物的两种高压液相色谱纯化的肽显示出与半乳糖凝集素 3（以前称为 Mac-2 抗原）完全同源，半乳糖凝集素是一种具有多效性功能的内源凝集素，在多种细胞类型中表达，白色念珠菌作为腐生菌或寄生虫与这些细胞类型相互作用。
beta-1,2-linked oligomannoside residues are present, associated with mannan and a glycolipid, the phospholipomannan, at the Candida albicans cell wall surface. beta-1,2-linked oligomannoside residues act as adhesins for macrophages and stimulate these cells to undergo cytokine production. To characterize the macrophage receptor involved in the recognition of C. albicans beta-1,2-oligomannoside we used the J774 mouse cell line, which is devoid of the receptor specific for alpha-linked mannose residues. A series of experiments based on affinity binding on either C. albicans yeast cells or beta-1,2-oligomannoside-conjugated bovine serum albumin (BSA) and subsequent disclosure with biotinylated conjugated BSA repeatedly led to the detection of a 32-kDa macrophage protein. An antiserum specific for this 32-kDa protein inhibited C. albicans binding to macrophages and was used to immunoprecipitate the molecule. Two high-pressure liquid chromatography-purified peptides from the 32-kDa tryptic digest showed complete homology to galectin-3 (previously designated Mac-2 antigen), an endogenous lectin with pleiotropic functions which is expressed in a wide variety of cell types with which C. albicans interacts as a saprophyte or a parasite.