Title | The enzyme activity of sortase A is regulated by phosphorylation in Staphylococcus aureus |
Author | |
Publication Years | 2023-12-01
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DOI | |
Source Title | |
ISSN | 2150-5594
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EISSN | 2150-5608
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Volume | 14Issue:1 |
Abstract | 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. |
Keywords | |
URL | [Source Record] |
Indexed By | |
Language | English
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SUSTech Authorship | Others
|
Funding Project | National Natural Science Foundation of China["31870127","32270184"]
; Science and Technology Commission of Shanghai Municipality[19JC1416400]
; State Key Laboratory of Drug Research["SIMM2205KF-07","SIMM2003ZZ-03"]
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WOS Research Area | Immunology
; Infectious Diseases
; Microbiology
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WOS Subject | Immunology
; Infectious Diseases
; Microbiology
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WOS Accession No | WOS:000931939300001
|
Publisher | |
Scopus EID | 2-s2.0-85147895163
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Data Source | Scopus
|
Citation statistics |
Cited Times [WOS]:1
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Document Type | Journal Article |
Identifier | http://kc.sustech.edu.cn/handle/2SGJ60CL/475068 |
Department | School of Medicine |
Affiliation | 1.College of Life Science,Northwest University,Xi'an,China 2.State Key Laboratory of Drug Research,Shanghai Institute of Materia Medica,Chinese Academy of Sciences,China 3.Hangzhou Institute for Advanced Study,University of Chinese Academy of Sciences,Hangzhou,China 4.University of Chinese Academy of Sciences,China 5.National Facility for Protein Science in Shanghai,Zhangjiang Lab,Shanghai Advanced Research Institute,Chinese Academy of Science,China 6.School of Medicine,Southern University of Science and Technology,Shenzhen,China |
Recommended Citation 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).
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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).
|
MLA |
Chen,Feifei,et al."The enzyme activity of sortase A is regulated by phosphorylation in Staphylococcus aureus".Virulence 14.1(2023).
|
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