Identification of the Actin and Plasminogen Binding Regions of Group B Streptococcal Phosphoglycerate Kinase
Identification of the Actin and Plasminogen Binding Regions of Group B Streptococcal Phosphoglycerate Kinase
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DOI：
10.1074/jbc.m112.361261
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发表时间：
2012-08-17
影响因子：
4.8
通讯作者：
Tyrrell, Gregory J.
中科院分区：
文献类型：
--
作者：
Boone, Tyler J.;Tyrrell, Gregory J.
存在于B族链球菌（GBS）表面的磷酸甘油酸激酶（PGK）先前已被证明与宿主蛋白肌动蛋白和纤溶酶原结合。使用截短的GBS-PGK分子鉴定GBS-PGK的肌动蛋白和纤溶酶原结合位点，随后进行肽图谱分析。这些实验鉴定了位于398个氨基酸长的GBS-PGK分子的氨基酸126-134和204-208之间的两个肌动蛋白和纤溶酶原结合位点。用丙氨酸取代这些区域内的赖氨酸残基导致与肌动蛋白和纤溶酶原的结合显著降低。此外，氨基酸133处的谷氨酸残基转化为脯氨酸（在肺炎链球菌PGK蛋白的该位置处发现的氨基酸）也导致与肌动蛋白和纤溶酶原的结合显著降低。这些结果表明，在氨基酸位置126、127、130、204和208处的赖氨酸残基沿着在氨基酸位置133处的谷氨酸残基对于通过GBS-PGK结合肌动蛋白和纤溶酶原是必需的。
Phosphoglycerate kinase (PGK), present on the surface of group B streptococcus (GBS), has previously been demonstrated to bind the host proteins actin and plasminogen. The actin and plasminogen binding sites of GBS-PGK were identified using truncated GBS-PGK molecules, followed by peptide mapping. These experiments identified two actin and plasminogen binding sites located between amino acids 126-134 and 204-208 of the 398-amino acid-long GBS-PGK molecule. Substitution of the lysine residues within these regions with alanine resulted in significantly reduced binding to both actin and plasminogen. In addition, conversion of the glutamic acid residue at amino acid 133 to proline, the amino acid found at this position for the PGK protein of Streptococcus pneumoniae, also resulted in significantly reduced binding to actin and plasminogen. These results demonstrate that the lysine residues at amino acid positions 126, 127, 130, 204, and 208 along with the glutamic acid residue at amino acid position 133 are necessary for actin and plasminogen binding by GBS-PGK.