NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B
NMR structure of a fungal virulence factor reveals structural homology with mammalian saposin B
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DOI：
10.1111/j.1365-2958.2009.06647.x
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发表时间：
2009-04-01
影响因子：
3.6
通讯作者：
Goldman, William E.
中科院分区：
文献类型：
--
作者：
Beck, Moriah R.;DeKoster, Gregory T.;Goldman, William E.
真菌蛋白CBP（钙结合蛋白）是一种已知的毒力因子，其毒力机制尚不清楚。基于其结合钙的能力及其作为荚膜组织胞浆菌最丰富的分泌蛋白的普遍性来鉴定该蛋白。然而，CBP与其他CBP没有序列同源性，并且不包含已知的钙结合基序。在这里，CBP的NMR结构揭示了一个高度交织的同源二聚体，并代表了任何真菌毒力因子的第一个原子水平的NMR模型。每个CBP单体由四个α-螺旋组成，采用saposin折叠，这是结合膜和脂质的蛋白质家族的特征。这种结构同源性表明CBP作为脂质结合蛋白发挥功能，可能与宿主细胞吞噬溶酶体中的宿主糖脂相互作用。
The fungal protein CBP (calcium binding protein) is a known virulence factor with an unknown virulence mechanism. The protein was identified based on its ability to bind calcium and its prevalence as Histoplasma capsulatum's most abundant secreted protein. However, CBP has no sequence homology with other CBPs and contains no known calcium binding motifs. Here, the NMR structure of CBP reveals a highly intertwined homodimer and represents the first atomic level NMR model of any fungal virulence factor. Each CBP monomer is comprised of four alpha-helices that adopt the saposin fold, characteristic of a protein family that binds to membranes and lipids. This structural homology suggests that CBP functions as a lipid binding protein, potentially interacting with host glycolipids in the phagolysosome of host cells.