Proteomic analysis of Escherichia coli with experimentally induced resistance to piperacillin/tazobactam
The worldwide emergence of antibiotic-resistant bacteria poses a serious threat to human health. In addition to the difficulties in controlling infectious diseases, the phenotype of resistance can generate metabolic changes which, in turn, can interfere with host–pathogen interactions. The aim of th...
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Published in: | Research in microbiology Vol. 161; no. 4; pp. 268 - 275 |
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Abstract | The worldwide emergence of antibiotic-resistant bacteria poses a serious threat to human health. In addition to the difficulties in controlling infectious diseases, the phenotype of resistance can generate metabolic changes which, in turn, can interfere with host–pathogen interactions. The aim of the present study was to identify changes in the subproteome of a laboratory-derived piperacillin/tazobactam-resistant strain of
Escherichia coli (minimal inhibitory concentration [MIC] = 128 mg/L) as compared with its susceptible wild-type strain
E. coli ATCC 25922 (MIC = 2 mg/L) using 2-D fluorescence difference gel electrophoresis (2D-DIGE) followed by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF MS). In the resistant strain, a total of 12 protein species were increased in abundance relative to the wild-type strain, including those related to bacterial virulence, antibiotic resistance and DNA protection during stress. Fourteen proteins were increased in abundance in the wild-type strain compared to the resistant strain, including those involved in glycolysis, protein biosynthesis, pentose-phosphate shunt, amino acid transport, cell division and oxidative stress response. In conclusion, our data show overall changes in the subproteome of the piperacillin/tazobactam-resistant strain, reporting for the first time the potential role of a multidrug efflux pump system in
E. coli resistance to piperacillin/tazobactam. |
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AbstractList | The worldwide emergence of antibiotic-resistant bacteria poses a serious threat to human health. In addition to the difficulties in controlling infectious diseases, the phenotype of resistance can generate metabolic changes which, in turn, can interfere with host–pathogen interactions. The aim of the present study was to identify changes in the subproteome of a laboratory-derived piperacillin/tazobactam-resistant strain of
Escherichia coli (minimal inhibitory concentration [MIC] = 128 mg/L) as compared with its susceptible wild-type strain
E. coli ATCC 25922 (MIC = 2 mg/L) using 2-D fluorescence difference gel electrophoresis (2D-DIGE) followed by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF MS). In the resistant strain, a total of 12 protein species were increased in abundance relative to the wild-type strain, including those related to bacterial virulence, antibiotic resistance and DNA protection during stress. Fourteen proteins were increased in abundance in the wild-type strain compared to the resistant strain, including those involved in glycolysis, protein biosynthesis, pentose-phosphate shunt, amino acid transport, cell division and oxidative stress response. In conclusion, our data show overall changes in the subproteome of the piperacillin/tazobactam-resistant strain, reporting for the first time the potential role of a multidrug efflux pump system in
E. coli resistance to piperacillin/tazobactam. The worldwide emergence of antibiotic-resistant bacteria poses a serious threat to human health. In addition to the difficulties in controlling infectious diseases, the phenotype of resistance can generate metabolic changes which, in turn, can interfere with host-pathogen interactions. The aim of the present study was to identify changes in the subproteome of a laboratory-derived piperacillin/tazobactam-resistant strain of Escherichia coli (minimal inhibitory concentration [MIC] = 128 mg/L) as compared with its susceptible wild-type strain E. coli ATCC 25922 (MIC = 2 mg/L) using 2-D fluorescence difference gel electrophoresis (2D-DIGE) followed by matrix-assisted laser desorption/ionization time-of-flight/time-of-flight (MALDI-TOF/TOF MS). In the resistant strain, a total of 12 protein species were increased in abundance relative to the wild-type strain, including those related to bacterial virulence, antibiotic resistance and DNA protection during stress. Fourteen proteins were increased in abundance in the wild-type strain compared to the resistant strain, including those involved in glycolysis, protein biosynthesis, pentose-phosphate shunt, amino acid transport, cell division and oxidative stress response. In conclusion, our data show overall changes in the subproteome of the piperacillin/tazobactam-resistant strain, reporting for the first time the potential role of a multidrug efflux pump system in E. coli resistance to piperacillin/tazobactam. |
Author | Diniz, Cláudio Galuppo Valéria dos Santos, Kênia de Macêdo Farias, Luiz de Castro Veloso, Luciano da Silva Giusta, Mario da Fonseca Pires, Simone Santos, Agenor Valadares Roque de Carvalho, Maria Auxiliadora Monteiro de Andrade, Hélida Morais Apolônio, Ana Carolina |
Author_xml | – sequence: 1 givenname: Kênia surname: Valéria dos Santos fullname: Valéria dos Santos, Kênia email: keniavaleria@gmail.com organization: Departamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Caixa Postal 486, 30.161-970 Belo Horizonte MG, Brazil – sequence: 2 givenname: Cláudio Galuppo surname: Diniz fullname: Diniz, Cláudio Galuppo email: cgdiniz@gmail.com organization: Departamento de Parasitologia, Microbiologia e Imunologia, Universidade Federal de Juiz de Fora, Bairro Martelos, Juiz de Fora CEP 36036-900 MG, Brazil – sequence: 3 givenname: Luciano surname: de Castro Veloso fullname: de Castro Veloso, Luciano email: lucianocvbio@gmail.com organization: Departamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Caixa Postal 486, 30.161-970 Belo Horizonte MG, Brazil – sequence: 4 givenname: Hélida surname: Monteiro de Andrade fullname: Monteiro de Andrade, Hélida email: helidandrade@gmail.com organization: Departamento de Parasitologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, Belo Horizonte MG, Brazil – sequence: 5 givenname: Mario surname: da Silva Giusta fullname: da Silva Giusta, Mario email: mgiusta@yahoo.com.br organization: Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, Belo Horizonte MG, Brazil – sequence: 6 givenname: Simone surname: da Fonseca Pires fullname: da Fonseca Pires, Simone email: simonefpires@gmail.com organization: Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, Belo Horizonte MG, Brazil – sequence: 7 givenname: Agenor Valadares surname: Santos fullname: Santos, Agenor Valadares email: agvaladares@gmail.com organization: Departamento de Bioquímica e Imunologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Av. Antônio Carlos, 6627, Belo Horizonte MG, Brazil – sequence: 8 givenname: Ana Carolina surname: Morais Apolônio fullname: Morais Apolônio, Ana Carolina email: carolinaapolonio@gmail.com organization: Departamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Caixa Postal 486, 30.161-970 Belo Horizonte MG, Brazil – sequence: 9 givenname: Maria Auxiliadora surname: Roque de Carvalho fullname: Roque de Carvalho, Maria Auxiliadora email: marc@icb.ufmg.br organization: Departamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Caixa Postal 486, 30.161-970 Belo Horizonte MG, Brazil – sequence: 10 givenname: Luiz surname: de Macêdo Farias fullname: de Macêdo Farias, Luiz email: macedo@icb.ufmg.br organization: Departamento de Microbiologia, Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, Caixa Postal 486, 30.161-970 Belo Horizonte MG, Brazil |
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Keywords | Resistance 2-D DIGE Comparative proteome Escherichia coli Piperacillin/tazobactam Enzyme β-Lactams Enzyme inhibitor Proteome β-Lactamase Induced resistance Penicillin derivatives Antibiotic Tazobactam Piperacillin Proteomics Bacteria Hydrolases Antibacterial agent Enterobacteriaceae |
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SubjectTerms | 2-D DIGE Amino acids Analytical, structural and metabolic biochemistry Anti-Bacterial Agents - pharmacology Bacteriology Biological and medical sciences Comparative proteome Drug Resistance, Multiple, Bacterial Electrophoresis, Gel, Two-Dimensional Escherichia coli Escherichia coli - chemistry Escherichia coli - drug effects Escherichia coli - genetics Escherichia coli - metabolism Escherichia coli Proteins - chemistry Escherichia coli Proteins - genetics Escherichia coli Proteins - metabolism Fundamental and applied biological sciences. Psychology Mass Spectrometry Microbiology Miscellaneous Molecular Sequence Data Penicillanic Acid - analogs & derivatives Penicillanic Acid - pharmacology Piperacillin - pharmacology Piperacillin/tazobactam Proteins Proteomics Resistance |
Title | Proteomic analysis of Escherichia coli with experimentally induced resistance to piperacillin/tazobactam |
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