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Molecular Pathogenesis

Acetylation of PhoP K88 Is Involved in Regulating Salmonella Virulence

Jianhui Li, Shuting Liu, Yang Su, Jie Ren, Yu Sang, Jinjing Ni, Jie Lu, Yu-Feng Yao
Denise Monack, Editor
Jianhui Li
aLaboratory of Bacterial Pathogenesis, Department of Microbiology and Immunology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, China
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Shuting Liu
aLaboratory of Bacterial Pathogenesis, Department of Microbiology and Immunology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, China
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Yang Su
aLaboratory of Bacterial Pathogenesis, Department of Microbiology and Immunology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, China
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Jie Ren
aLaboratory of Bacterial Pathogenesis, Department of Microbiology and Immunology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, China
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Yu Sang
aLaboratory of Bacterial Pathogenesis, Department of Microbiology and Immunology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, China
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Jinjing Ni
aLaboratory of Bacterial Pathogenesis, Department of Microbiology and Immunology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, China
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Jie Lu
bDepartment of Infectious Diseases, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China
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Yu-Feng Yao
aLaboratory of Bacterial Pathogenesis, Department of Microbiology and Immunology, Institutes of Medical Sciences, Shanghai Jiao Tong University School of Medicine, Shanghai, China
bDepartment of Infectious Diseases, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai, China
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Denise Monack
Stanford University
Roles: Editor
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DOI: 10.1128/IAI.00588-20
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ABSTRACT

The PhoP-PhoQ two-component regulation system of Salmonella enterica serovar Typhimurium is involved in the response to various environmental stresses and is essential for bacterial virulence. Our previous studies showed that acetylation plays an important role in regulating the activity of PhoP, which consequently mediates the change in virulence of S. Typhimurium. Here, we demonstrate that a conserved lysine residue, K88, is crucial for the function of PhoP and its acetylation-downregulated PhoP activities. K88 could be specifically acetylated by acetyl phosphate (AcP), and the acetylation level of K88 decreased significantly after phagocytosis of S. Typhimurium by macrophages. Acetylation of K88 inhibited PhoP dimerization and DNA-binding abilities. In addition, mutation of K88 to glutamine, mimicking the acetylated form, dramatically attenuated intestinal inflammation and systemic infection of S. Typhimurium in the mouse model. These findings indicate that nonenzymatic acetylation of PhoP by AcP is a fine-tuned mechanism for the virulence of S. Typhimurium and highlights that virulence and metabolism in the host are closely linked.

FOOTNOTES

    • Received 21 September 2020.
    • Returned for modification 15 October 2020.
    • Accepted 9 December 2020.
    • Accepted manuscript posted online 14 December 2020.
  • Supplemental material is available online only.

  • Copyright © 2021 American Society for Microbiology.

All Rights Reserved.

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Acetylation of PhoP K88 Is Involved in Regulating Salmonella Virulence
Jianhui Li, Shuting Liu, Yang Su, Jie Ren, Yu Sang, Jinjing Ni, Jie Lu, Yu-Feng Yao
Infection and Immunity Feb 2021, 89 (3) e00588-20; DOI: 10.1128/IAI.00588-20

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Acetylation of PhoP K88 Is Involved in Regulating Salmonella Virulence
Jianhui Li, Shuting Liu, Yang Su, Jie Ren, Yu Sang, Jinjing Ni, Jie Lu, Yu-Feng Yao
Infection and Immunity Feb 2021, 89 (3) e00588-20; DOI: 10.1128/IAI.00588-20
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KEYWORDS

PhoP
Salmonella enterica serovar Typhimurium
acetyl phosphate
Acetylation
virulence

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