Pack T D, Podbielski A, Boyle M D
Department of Microbiology, Medical College of Ohio, Toledo 43699-0008, USA.
Gene. 1996 May 24;171(1):65-70. doi: 10.1016/0378-1119(96)00102-3.
Sequence comparison of six known group-A streptococcal IgG-binding proteins, sharing the common property of protein G-inhibitable IgG3-binding-activity, identified a highly conserved 35-amino-acid (aa) sequence (74-100% similarity) within an EQ-rich central conserved core region of each protein. A search of aa sequence databases identified four additional proteins with > 50% similarity to this consensus sequence. All of these proteins demonstrated protein G-inhibitable IgG3-binding activity. Taken together, these results identify a signature sequence that predicts the presence of a protein G-inhibitable IgG3-binding domain(s) in group-A streptococcal IgG-binding proteins.
对六种已知的A组链球菌IgG结合蛋白进行序列比较,这些蛋白具有蛋白G可抑制的IgG3结合活性这一共同特性,结果发现在每种蛋白富含EQ的中央保守核心区域内有一个高度保守的35个氨基酸(aa)序列(相似度为74 - 100%)。对氨基酸序列数据库的搜索发现了另外四种与该共有序列相似度大于50%的蛋白。所有这些蛋白都表现出蛋白G可抑制的IgG3结合活性。综合这些结果,确定了一个特征序列,该序列可预测A组链球菌IgG结合蛋白中存在蛋白G可抑制的IgG3结合结构域。