4.6 Article

Acetylome and Succinylome Profiling of Edwardsiella tarda Reveals Key Roles of Both Lysine Acylations in Bacterial Antibiotic Resistance

Journal

ANTIBIOTICS-BASEL
Volume 11, Issue 7, Pages -

Publisher

MDPI
DOI: 10.3390/antibiotics11070841

Keywords

Edwardsiella tarda; acetylome; succinylome; antibiotic resistance

Funding

  1. Youth Project of Fujian Provincial Education Department [JAT210724]
  2. doctoral research project [20220105]
  3. Open Project Program of Fujian Provincial Key Laboratory of Agroecological Processing and Safety Monitoring (Fujian Agriculture and Forestry University) [NYST-2021-02]
  4. Science and Education Development Fund Project of Fujian Chuanzheng Communications College [20200202]
  5. program for the Key Laboratory of Marine Biotechnology of Fujian Province [2020MB04]
  6. Fujian-Taiwan Joint Innovative Center for Germplasm Resources and Cultivation of Crop (FJ 2011 Program, China) [2015-75]

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This study investigates the role of lysine acetylation and succinylation in the antibiotic resistance mechanism of Edwardsiella tarda. The results demonstrate that these post-translational modifications play important roles in bacterial antibiotic resistance and are enriched in various metabolic pathways. The findings provide insights into the mechanism of antibiotic resistance and may aid future research on the pathogenesis of this bacterium.
The antibiotic resistance of Edwardsiella tarda is becoming increasingly prevalent, and thus novel antimicrobial strategies are being sought. Lysine acylation has been demonstrated to play an important role in bacterial physiological functions, while its role in bacterial antibiotic resistance remains largely unclear. In this study, we investigated the lysine acetylation and succinylation profiles of E. tarda strain EIB202 using affinity antibody purification combined with LC-MS/MS. A total of 1511 lysine-acetylation sites were identified on 589 proteins, and 2346 lysine-succinylation sites were further identified on 692 proteins of this pathogen. Further bioinformatic analysis showed that both post-translational modifications (PTMs) were enriched in the tricarboxylic acid (TCA) cycle, pyruvate metabolism, biosynthesis, and carbon metabolism. In addition, 948 peptides of 437 proteins had overlapping associations with multiple metabolic pathways. Moreover, both acetylation and succinylation were found in many antimicrobial resistance (AMR) proteins, suggesting their potentially vital roles in antibiotic resistance. In general, our work provides insights into the acetylome and succinylome features responsible for the antibiotic resistance mechanism of E. tarda, and the results may facilitate future investigations into the pathogenesis of this bacterium.

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