A link between STK signalling and capsular polysaccharide synthesis in Streptococcus suis
文献类型： 外文期刊
作者： Tang, Jinsheng 1 ; Guo, Mengru 1 ; Chen, Min 1 ; Xu, Bin 2 ; Ran, Tingting 3 ; Wang, Weiwu 3 ; Ma, Zhe 1 ; Lin, Huixing 1 ; Fan, Hongjie 1 ;
作者机构： 1.Nanjing Agr Univ, Coll Vet Med, MOE Joint Int Res Lab Anim Hlth & Food Safety, Nanjing 210095, Peoples R China
2.Jiangsu Acad Agr Sci, Natl Res Ctr Vet Biol Engn & Technol, Nanjing 210000, Peoples R China
3.Nanjing Agr Univ, Dept Microbiol, Coll Life Sci, Nanjing 210095, Peoples R China
4.Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou 225009, Jiangsu, Peoples R China
期刊名称：NATURE COMMUNICATIONS （ 影响因子：16.6； 五年影响因子：17.0 ）
ISSN：
年卷期： 2023 年 14 卷 1 期
页码：
收录情况： SCI
摘要： Synthesis of capsular polysaccharide (CPS), an important virulence factor of pathogenic bacteria, is modulated by the CpsBCD phosphoregulatory system in Streptococcus. Serine/threonine kinases (STKs, e.g. Stk1) can also regulate CPS synthesis, but the underlyingmechanisms are unclear. Here, we identify a protein (CcpS) that is phosphorylated by Stk1 and modulates the activity of phosphatase CpsB in Streptococcus suis, thus linking Stk1 to CPS synthesis. The crystal structure of CcpS shows an intrinsically disordered region at its N-terminus, including two threonine residues that are phosphorylated by Stk1. The activity of phosphatase CpsB is inhibited when bound to non-phosphorylated CcpS. Thus, CcpS modulates the activity of phosphatase CpsB thereby altering CpsD phosphorylation, which in turn modulates the expression of the Wzx-Wzy pathway and thus CPS production.
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