The beta-domain of cluster 2b streptokinase is a major determinant for the regulation of its plasminogen activation activity by cellular plasminogen receptors

文献类型： 外文期刊

第一作者： Zhang, Yueling

作者： Zhang, Yueling;Mayfield, Jeffrey A.;Ploplis, Victoria A.;Castellino, Francis J.;Zhang, Yueling;Mayfield, Jeffrey A.;Ploplis, Victoria A.;Castellino, Francis J.;Zhang, Yueling

作者机构：

关键词： Streptokinase;Streptococcus pyogenes;Bacterial virulence;Human plasminogen;Protein domains

期刊名称：BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS （ 影响因子：3.575； 五年影响因子：3.381 ）

ISSN： 0006-291X

年卷期： 2014 年 444 卷 4 期

页码：

收录情况： SCI

摘要： Cluster 2b streptokinase (SK2b), secreted by invasive skin-trophic strains of Streptococcus pyogenes (GAS), is a human plasminogen (hPg) activator that optimally functions when human plasma hPg is bound, via its kringle-2 domain, to cognizant bacterial cells through the a1a2 domain of the major cellular hPg receptor, Plasminogen-binding group A streptococcal M-like protein (PAM). Another class of streptokinases (SK1), secreted primarily by GAS strains that possess affinity for pharyngeal infections, does not require PAM-bound hPg for optimal activity. We find herein that replacement of the central beta-domain of SK2b with the same module from SKI reduces the dependency of SK2b on PAM, and the converse is true when the beta-domain of SKI is replaced with this same region of SK2b. These data suggest that simple evolutionary shuttling of protein domains in GAS can be employed by GAS to rapidly generate strains that differ in tissue tropism and invasive capability and allow the bacteria to survive different challenges by the host. (C) 2014 Elsevier Inc. All rights reserved.

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