Human and mouse macrophage-inducible C-type lectin (Mincle) bind Candida albicans
Human and mouse macrophage-inducible C-type lectin (Mincle) bind Candida albicans
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DOI：
10.1093/glycob/cwn046
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发表时间：
2008-09-01
期刊：
影响因子：
4.3
通讯作者：
Blanchard, Helen
中科院分区：
文献类型：
--
作者：
Bugarcic, Andrea;Hitchens, Kelly;Blanchard, Helen
白色念珠菌是皮肤、口腔和胃肠道真菌病的病原体。识别与白色念珠菌接触时免疫细胞所参与的受体及其各自的配体对于了解导致侵袭性念珠菌病的炎症反应至关重要。 Mincle 是最近发现的一种巨噬细胞表达的受体，对于宿主对白色念珠菌的反应非常重要。人类和小鼠 Mincle 的碳水化合物识别结构域在变性条件下得到表达、纯化，并成功重折叠。除了寡聚物之外，在两种不同的缓冲溶液中还存在可分离的蛋白质单体和二聚体形式。人类和小鼠同源物结合酵母提取物，分离的二聚体和单体物种也证明了对整个白色念珠菌酵母细胞的识别。这些数据表明了介导 Mincle 和酵母在巨噬细胞表面相互作用的几种功能状态。
Candida albicans is a causative agent in mycoses of the skin, oral cavity, and gastrointestinal tract. Identification of receptors, and their respective ligands, that are engaged by immune cells when in contact with C. albicans is crucial for understanding inflammatory responses leading to invasive candidiasis. Mincle is a recently identified macrophage-expressed receptor that is important for host responses to C. albicans. The carbohydrate-recognition domain of human and mouse Mincle were expressed, purified under denaturing conditions, and successfully refolded. In addition to oligomers, there are isolatable monomeric and dimeric forms of the protein that occur under two different buffer solutions. The human and mouse homologues bound yeast extract, and the isolated dimeric and monomeric species also demonstrated the recognition of whole C. albicans yeast cells. The data are indicative of several functional states mediating the interaction of Mincle and yeast at the surface of the macrophage.