ArticleMolecular & cellular proteomics : MCP2016
Comparative Phosphoproteomics Reveals the Role of AmpC β-lactamase Phosphorylation in the Clinical Imipenem-resistant Strain Acinetobacter baumannii SK17.
Article in Molecular & cellular proteomics : MCP, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Antechokinetics, the kinetics of antimicrobial resistance molecules.Frontiers in pharmacology · 2026Review
- Phosphomimetic mutations near active sites of proteins in Thermus thermophilus suggest a widespread regulatory mechanism.FEBS open bio · 2025Article
- Phosphorylation of Staphylococcus aureus β-lactamase, a prerequisite to its sequestration on the cytoplasmic membrane.Protein science : a publication of the Protein Society · 2025Article
- Exploration of Phosphoproteins inPathogens (Basel, Switzerland) · 2025Article
- Carbapenem-induced β-lactamase-isoform expression trends in Acinetobacter baumannii.Scientific reports · 2024Article
- A Review of the Bacterial Phosphoproteomes of Beneficial Microbes.Microorganisms · 2023Review
- Colistin Resistance inAntibiotics (Basel, Switzerland) · 2023Review
- The deficiency of poly-β-1,6-N-acetyl-glucosamine deacetylase trigger A. baumannii to convert to biofilm-independent colistin-tolerant cells.Scientific reports · 2023Article
- Review
- Addressing the Possibility of a Histone-Like Code in Bacteria.Journal of proteome research · 2021Review
- Phosphorylation of Extracellular Proteins inFrontiers in microbiology · 2021Article
- Bacterial Protein Kinases.Advances in experimental medicine and biology · 2021Article
- Effect of membrane fusion protein AdeT1 on the antimicrobial resistance of Escherichia coli.Scientific reports · 2020Article
- Phosphoproteomics and Bioinformatics Analyses Reveal Key Roles of GSK-3 and AKAP4 in Mouse Sperm Capacitation.International journal of molecular sciences · 2020Article
- Bacterial Genome Wide Association Studies (bGWAS) and Transcriptomics Identifies Cryptic Antimicrobial Resistance Mechanisms inFrontiers in public health · 2020Article
- Goals and Challenges in Bacterial Phosphoproteomics.International journal of molecular sciences · 2019Review
- Site-specific His/Asp phosphoproteomic analysis of prokaryotes reveals putative targets for drug resistance.BMC microbiology · 2017Article
- Acetylome ofFrontiers in molecular biosciences · 2017Article
- Mass Spectrometry Targeted Assays as a Tool to Improve Our Understanding of Post-translational Modifications in Pathogenic Bacteria.Frontiers in microbiology · 2016Article
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Authors and funding
10 authors at 6 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nosocomial infectious outbreaks caused by multidrug-resistant Acinetobacter baumannii have emerged as a serious threat to human health. Phosphoproteomics of pathogenic bacteria has been used to identify the mechanisms of bacterial virulence and antimicrobial resistance. In this study, we used a shotgun strategy combined with high-accuracy mass spectrometry to analyze the phosphoproteomics of the imipenem-susceptible strain SK17-S and -resistant strain SK17-R. We identified 410 phosphosites on 248 unique phosphoproteins in SK17-S and 285 phosphosites on 211 unique phosphoproteins in SK17-R. The distributions of the Ser/Thr/Tyr/Asp/His phosphosites in SK17-S and SK17-R were 47.0%/27.6%/12.4%/8.0%/4.9% versus 41.4%/29.5%/17.5%/6.7%/4.9%, respectively. The Ser-90 phosphosite, located on the catalytic motif S(88)VS(90)K of the AmpC β-lactamase, was first identified in SK17-S. Based on site-directed mutagenesis, the nonphosphorylatable mutant S90A was found to be more resistant to imipenem, whereas the phosphorylation-simulated mutant S90D was sensitive to imipenem. Additionally, the S90A mutant protein exhibited higher β-lactamase activity and conferred greater bacterial protection against imipenem in SK17-S compared with the wild-type. In sum, our results revealed that in A. baumannii, Ser-90 phosphorylation of AmpC negatively regulates both β-lactamase activity and the ability to counteract the antibiotic effects of imipenem. These findings highlight the impact of phosphorylation-mediated regulation in antibiotic-resistant bacteria on future drug design and new therapies.
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