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Comparative phosphoproteomics reveals the role of AmpC β-lactamase phosphorylation in the clinical imipenem-resistant strain Acinetobacter baumannii SK17 (MaxQuant 1.3 and 1.4)

ABSTRACT: Nosocomial outbreaks of infections caused by multidrug-resistant Acinetobacter baumannii have emerged as a serious threat to human health. The phosphoproteomics of pathogenic bacteria have been investigated for their role in virulence regulation networks. In this study, we analyzed the phosphoproteomics of two clinical isolates of A. baumannii: imipenem-sensitive strain SK17-S and -resistant strain SK17-R.

INSTRUMENT(S):

ORGANISM(S): Acinetobacter Baumannii

TISSUE(S): Prokaryotic Cell, Cell Culture

SUBMITTER: Juo-hsin Lai

LAB HEAD: Juohsin Lai

PROVIDER: PXD002033 | Pride | 2015-10-27

REPOSITORIES: Pride

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			Action	DRS
	17R-1.RAW	Raw
	17R-3.RAW	Raw
	17R-5.RAW	Raw
	17R-7.RAW	Raw
	17R-FT-1.RAW	Raw

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Publications

Comparative Phosphoproteomics Reveals the Role of AmpC β-lactamase Phosphorylation in the Clinical Imipenem-resistant Strain Acinetobacter baumannii SK17.

Lai Juo-Hsin JH Yang Jhih-Tian JT Chern Jeffy J Chen Te-Li TL Wu Wan-Ling WL Liao Jiahn-Haur JH Tsai Shih-Feng SF Liang Suh-Yuen SY Chou Chi-Chi CC Wu Shih-Hsiung SH

Molecular & cellular proteomics : MCP 20151023 1

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 24 ...[more]

PMID: 26499836

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Mutation of the RNA polymerase β-subunit gene promotes hetero-to-homo conversion of ß-lactam resistance of methicillin-resistant Staphylococcus aureus

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Project description:Infections caused by carbapenem-resistant Acinetobacter baumannii (CRAb) are associated with high patient morbidity and mortality. The serious threat for human health imposed by CRAb was recently underscored by identification of close-to-untouchable carbapenem- and tetracycline-resistant isolates. Since outer membrane vesicles (OMVs) of Gram-negative bacteria may contribute to antimicrobial resistance, our present study was aimed at investigating OMVs produced by the first two carbapenem- and tetracycline-resistant CRAb isolates in Europe. These isolates, denoted CRAb1 and CRAb2 contain large, nearly identical plasmids that specify multiple resistances. Both isolates produce OMVs that were analyzed by differential light scattering, transmission electron microscopy and proteomics. By comparison with OMVs from the plasmid-free non-carbapenem-resistant A. baumannii isolate Ab1, which is an isogenic ancestor of the CRAb1 isolate, we show that plasmid carriage by the CRAb1 and CRAb2 isolates leads to an increased OMV size that is accompanied by increased diversity of the OMV proteome. Our analyses show that OMVs from CRAb1 and CRAb2 are major reservoirs of proteins involved in antimicrobial resistance, including the plasmid-encoded carbapenemases BlaNDM-1, and BlaOXA-97. We also show that these OMV-borne carbapenemases hydrolyze imipenem and protect otherwise carbapenem-sensitive A. baumannii and Escherichia coli isolates against this antibiotic. Altogether, our observations show that OMVs from highly drug-resistant CRAb confer tolerance against last-resort antibiotics to non-resistant bacterial pathogens.

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