The enzyme activity of sortase A is regulated by phosphorylation in Staphylococcus aureus
文献类型：期刊论文
| 作者 | Chen, Feifei4,5,6; Di, Hongxia3,5; Wang, Yanhui3,5; Peng, Chao2; Chen, Rongrong3,4; Pan, Huiwen3,4; Yang, Cai-Guang3,4,5 ; Liang, Haihua1,6; Lan, Lefu1,3,4,5,6
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| 刊名 | VIRULENCE
 |
| 出版日期 | 2023-12-31 |
| 卷号 | 14期号:1页码:2171641 |
| 关键词 | Staphylococcus aureus Sortase A protein phosphorylation virulence |
| DOI | 10.1080/21505594.2023.2171641 |
| 文献子类 | Article |
| 英文摘要 | In many Gram-positive bacteria, the transpeptidase enzyme sortase A (SrtA) anchors surface proteins to cell wall and plays a critical role in the bacterial pathogenesis. Here, we show that in Staphylococcus aureus, an important human pathogen, the SrtA is phosphorylated by serine/threonine protein kinase Stk1. S. aureus SrtA can also be phosphorylated by small-molecule phosphodonor acetyl phosphate (AcP) in vitro. We determined that various amino acid residues of S. aureus SrtA are subject to phosphorylation, primarily on its catalytic site residue cysteine-184 in the context of a bacterial cell lysate. Both Stk1 and AcP-mediated phosphorylation inhibited the enzyme activity of SrtA in vitro. Consequently, deletion of gene (i.e. stp1) encoding serine/threonine phosphatase Stp1, the corresponding phosphatase of Stk1, caused an increase in the phosphorylation level of SrtA. The stp1 deletion mutant mimicked the phenotypic traits of srtA deletion mutant (i.e. attenuated growth where either haemoglobin or haem as a sole iron source and reduced liver infections in a mouse model of systemic infection). Importantly, the phenotypic defects of the stp1 deletion mutant can be alleviated by overexpressing srtA. Taken together, our finding suggests that phosphorylation plays an important role in modulating the activity of SrtA in S. aureus. |
| WOS关键词 | SURFACE-PROTEINS ; CELL-WALL ; BACTERIAL VIRULENCE ; INDUCED PNEUMONIA ; IN-VITRO ; TRANSPEPTIDASE ; TARGET ; INHIBITOR ; MECHANISM ; SITE |
| WOS研究方向 | Immunology ; Infectious Diseases ; Microbiology |
| 语种 | 英语 |
| WOS记录号 | WOS:000931939300001 |
| 出版者 | TAYLOR & FRANCIS INC |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/309634]  |
| 专题 | 新药研究国家重点实验室 |
| 通讯作者 | Liang, Haihua; Lan, Lefu |
| 作者单位 | 1.Southern Univ Sci & Technol, Sch Med, Shenzhen, Peoples R China 2.Chinese Acad Sci, Shanghai Adv Res Inst, Zhangjiang Lab, Natl Facil Prot Sci Shanghai, Shanghai, Peoples R China; 3.Univ Chinese Acad Sci, Beijing, Peoples R China; 4.Univ Chinese Acad Sci, Hangzhou Inst Adv Study, Hangzhou, Peoples R China; 5.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai, Peoples R China; 6.Northwest Univ, Coll Life Sci, Xian, Peoples R China; |
| 推荐引用方式 GB/T 7714 | Chen, Feifei,Di, Hongxia,Wang, Yanhui,et al. The enzyme activity of sortase A is regulated by phosphorylation in Staphylococcus aureus[J]. VIRULENCE,2023,14(1):2171641. |
| APA | Chen, Feifei.,Di, Hongxia.,Wang, Yanhui.,Peng, Chao.,Chen, Rongrong.,...&Lan, Lefu.(2023).The enzyme activity of sortase A is regulated by phosphorylation in Staphylococcus aureus.VIRULENCE,14(1),2171641. |
| MLA | Chen, Feifei,et al."The enzyme activity of sortase A is regulated by phosphorylation in Staphylococcus aureus".VIRULENCE 14.1(2023):2171641. |
入库方式： OAI收割
来源：上海药物研究所
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