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Structural and bioc...
Structural and biochemical characterization of the environmental MBLs MYO-1, ECV-1 and SHD-1.
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- Fröhlich, Christopher (author)
- Universitetet i Tromsø – Norges arktiske universitet,University of Tromsø – The Arctic University of Norway
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- Sørum, Vidar (author)
- Universitetet i Tromsø – Norges arktiske universitet,University of Tromsø – The Arctic University of Norway
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Huber, Sandra (author)
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- Samuelsen, Ørjan (author)
- Universitetet i Tromsø – Norges arktiske universitet,University of Tromsø – The Arctic University of Norway
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- Berglund, Fanny (author)
- Gothenburg University,Göteborgs universitet,Institutionen för biomedicin, avdelningen för infektionssjukdomar,CARe - Centrum för antibiotikaresistensforskning,Institutionen för matematiska vetenskaper,Institute of Biomedicine, Department of Infectious Medicine,Centre for antibiotic resistance research, CARe,Department of Mathematical Sciences,University of Gothenburg,Chalmers tekniska högskola,Chalmers University of Technology
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- Kristiansson, Erik, 1978 (author)
- Gothenburg University,Göteborgs universitet,Institutionen för matematiska vetenskaper,CARe - Centrum för antibiotikaresistensforskning,Department of Mathematical Sciences,Centre for antibiotic resistance research, CARe,University of Gothenburg,Chalmers tekniska högskola,Chalmers University of Technology
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- Kotsakis, Stathis, 1982 (author)
- Gothenburg University,Göteborgs universitet,CARe - Centrum för antibiotikaresistensforskning,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Centre for antibiotic resistance research, CARe,Institute of Biomedicine, Department of Infectious Medicine,University of Gothenburg
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- Marathe, Nachiket (author)
- Gothenburg University,Göteborgs universitet,CARe - Centrum för antibiotikaresistensforskning,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Centre for antibiotic resistance research, CARe,Institute of Biomedicine, Department of Infectious Medicine,Havforskningsinstituttet,Norwegian Institute of Marine Research,Chalmers tekniska högskola,Chalmers University of Technology,University of Gothenburg
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- Larsson, D. G. Joakim, 1969 (author)
- Gothenburg University,Göteborgs universitet,CARe - Centrum för antibiotikaresistensforskning,Institutionen för biomedicin, avdelningen för infektionssjukdomar,Centre for antibiotic resistance research, CARe,Institute of Biomedicine, Department of Infectious Medicine,University of Gothenburg
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- Leiros, Hanna-Kirsti S (author)
- Universitetet i Tromsø – Norges arktiske universitet,University of Tromsø – The Arctic University of Norway
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(creator_code:org_t)
- 2020-05-28
- 2020
- English.
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In: The Journal of antimicrobial chemotherapy. - : Oxford University Press (OUP). - 1460-2091 .- 0305-7453. ; 75:9, s. 2554-2563
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Abstract
Subject headings
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- MBLs form a large and heterogeneous group of bacterial enzymes conferring resistance to β-lactam antibiotics, including carbapenems. A large environmental reservoir of MBLs has been identified, which can act as a source for transfer into human pathogens. Therefore, structural investigation of environmental and clinically rare MBLs can give new insights into structure-activity relationships to explore the role of catalytic and second shell residues, which are under selective pressure.To investigate the structure and activity of the environmental subclass B1 MBLs MYO-1, SHD-1 and ECV-1.The respective genes of these MBLs were cloned into vectors and expressed in Escherichia coli. Purified enzymes were characterized with respect to their catalytic efficiency (kcat/Km). The enzymatic activities and MICs were determined for a panel of different β-lactams, including penicillins, cephalosporins and carbapenems. Thermostability was measured and structures were solved using X-ray crystallography (MYO-1 and ECV-1) or generated by homology modelling (SHD-1).Expression of the environmental MBLs in E. coli resulted in the characteristic MBL profile, not affecting aztreonam susceptibility and decreasing susceptibility to carbapenems, cephalosporins and penicillins. The purified enzymes showed variable catalytic activity in the order of <5% to ∼70% compared with the clinically widespread NDM-1. The thermostability of ECV-1 and SHD-1 was up to 8°C higher than that of MYO-1 and NDM-1. Using solved structures and molecular modelling, we identified differences in their second shell composition, possibly responsible for their relatively low hydrolytic activity.These results show the importance of environmental species acting as reservoirs for MBL-encoding genes.
Subject headings
- MEDICIN OCH HÄLSOVETENSKAP -- Medicinska och farmaceutiska grundvetenskaper -- Mikrobiologi inom det medicinska området (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Basic Medicine -- Microbiology in the medical area (hsv//eng)
- NATURVETENSKAP -- Biologi -- Mikrobiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Microbiology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Bioinformatik och systembiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Bioinformatics and Systems Biology (hsv//eng)
- NATURVETENSKAP -- Biologi -- Strukturbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Structural Biology (hsv//eng)
Keyword
- antibiotics
Publication and Content Type
- ref (subject category)
- art (subject category)
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Fröhlich, Christ ...
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Sørum, Vidar
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Huber, Sandra
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Samuelsen, Ørjan
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Berglund, Fanny
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Kristiansson, Er ...
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Kotsakis, Stathi ...
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Marathe, Nachike ...
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Larsson, D. G. J ...
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Leiros, Hanna-Ki ...
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MEDICAL AND HEAL ...
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and Basic Medicine
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NATURAL SCIENCES
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and Biological Scien ...
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and Microbiology
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NATURAL SCIENCES
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and Biological Scien ...
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and Biochemistry and ...
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NATURAL SCIENCES
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NATURAL SCIENCES
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University of Gothenburg
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Chalmers University of Technology