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Acquisition of resistance to extended-spectrum cephalosporins by Salmonella entirica subsp. enterica serovar Newport and Escherichia coli in the turkey poult intestinal tract

Article Abstract:

The mechanisms and frequency of transfer of resistance of the extended-spectrum cephalosporins (ESCs) by Escherichia coli and the acquisition of such resistance by antimicrobial-susceptible Salmonella serovar Newport bacteria in the turkey poult intestinal tract are examined. It is demonstrated that Salmonella serovar Newport can become resistant to ESCs and other antibiotics by acquiring a conjugative drug resistance plasmid from E. coli in the intestines.

Author: Poppe, C., Martin, L. C., Gyles, C. L., Reid-Smith, R., Boerlin, P., Forward, K. R., Prescott, J. F., McEwen, S. A.
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
Genetic aspects, Drug resistance in microorganisms, Microbial drug resistance, Escherichia coli, Salmonella enteritidis

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Cloning, overexpression, and characterization of a novel thermostable pencillin G acylase from achromobacter xylosoxidants: Probing the molecular basis for its high thermostability

Article Abstract:

The gene encoding a novel pencillin G acylase (PGA), designed pgaW, is cloned from Achromobacter xylosoxidans and overexpressed in Escherichia coli. The results suggest that the increased number of buried ion pair networks, lower in N and Q contents, excessive arginine residues and remarkably high content of proline residues in the structure of PGA650 could contribute to its high thermostability.

Author: Gang Cai, Songcheng Zhu, Sheng Yang, Guoping Zhao, Weihing Jiang
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2004
Oxidases, Microbiology, Acylation

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Improving the activity and stability of GL-7-ACA acylase CA130 by site-directed mutagenesis

Article Abstract:

Glutaryl-7-amino cephalosporanic acid acylase from Pseudomonas sp. strain 130 (CA130) was mutated to improve its enzymatic activity and stability. Based on the crystal structure of CA130, two series of amino acid residues, one from those directly involved in catalytic function and another from those putatively involved in surface charge, were selected as targets for site-directed mutagenesis.

Author: Wei Zhang, Sheng Yang, Yuan Liu, Huabao Zheng, Weihong Jiang
Publisher: American Society for Microbiology
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2005
Gene mutations, Gene mutation, Bacterial genetics

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Subjects list: Research, Cephalosporins, Moxalactam, Cephaloridine
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