نتایج جستجو برای: carbapenemases

تعداد نتایج: 913  

Journal: :Journal of clinical microbiology 2015
Baixing Ding Fupin Hu Yang Yang Qinglan Guo Jinwei Huang Minggui Wang

Carbapenem-resistant Escherichia coli, Klebsiella pneumoniae, Enterobacter aerogenes, and Acinetobacter baumannii were isolated from a single patient, each producing different carbapenemases (NDM-1, KPC-2, IMP, and OXA-23, respectively). The NDM-1-producing E. coli strain was preceded by a clonally related carbapenem-susceptible strain a month earlier, suggesting in vivo acquisition of blaNDM-1.

Journal: :Chemical communications 2014
Ewa I Chudyk Michael A L Limb Charlotte Jones James Spencer Marc W van der Kamp Adrian J Mulholland

Carbapenems, 'last resort' antibiotics for many bacterial infections, can now be broken down by several class A β-lactamases (i.e. carbapenemases). Here, carbapenemase activity is predicted through QM/MM dynamics simulations of acyl-enzyme deacylation, requiring only the 3D structure of the apo-enzyme. This may assist in anticipating resistance and future antibiotic design.

Journal: :Antimicrobial agents and chemotherapy 2015
Romney M Humphries Shangxin Yang Peera Hemarajata Kevin W Ward Janet A Hindler Shelley A Miller Aric Gregson

Ceftazidime-avibactam is the first antimicrobial approved by the U.S. FDA for the treatment of carbapenem-resistant Enterobacteriaceae. Avibactam, a non-β-lactam β-lactamase inhibitor, inactivates class A serine carbapenemases, including Klebsiella pneumoniae carbapenemase (KPC). We report a KPC-producing K. pneumoniae isolate resistant to ceftazidime-avibactam (MIC, 32/4 μg/ml) from a patient ...

Journal: :The Journal of antimicrobial chemotherapy 2012
Laurent Poirel Anaïs Potron Patrice Nordmann

OXA-48-type carbapenem-hydrolysing class D β-lactamases are increasingly reported in enterobacterial species. To date, six OXA-48-like variants have been identified, with OXA-48 being the most widespread. They differ by a few amino acid substitutions or deletions (one to five amino acids). The enzymes hydrolyse penicillins at a high level and carbapenems at a low level, sparing broad-spectrum c...

Journal: :The Journal of antimicrobial chemotherapy 2010
David M Livermore Shazad Mushtaq Marina Warner

BACKGROUND BAL30376 combines the siderophore monobactam BAL19764 (Syn/PTX 2416) with the bridged monobactam BAL29880 to inhibit AmpC enzymes and with clavulanate to inhibit extended-spectrum β-lactamases (ESBLs). We tested BAL30376 and its components versus isolates and laboratory strains of Enterobacteriaceae and non-fermenters. METHODS MICs were determined on Mueller-Hinton agar supplemente...

2016
Dereje D. Gudeta Valeria Bortolaia Simona Pollini Jean-Denis Docquier Gian M. Rossolini Gregory C. A. Amos Elizabeth M. H. Wellington Luca Guardabassi

Carbapenemases are bacterial enzymes that hydrolyze carbapenems, a group of last-resort β-lactam antibiotics used for treatment of severe bacterial infections. They belong to three β-lactamase classes based amino acid sequence (A, B, and D). The aim of this study was to elucidate occurrence, diversity and functionality of carbapenemase-encoding genes in soil microbiota by functional metagenomic...

2015
Fereshteh Eftekhar Ziaeldin Naseh

BACKGROUND AND OBJECTIVES Klebsiella pneumoniae is an opportunistic pathogen responsible for up to 10% of nosocomial infections. The emergence and spread of multidrug resistant K. pneumoniae, mostly due to the production of extended-spectrum β-lactamases (ESBL) and carbapenemases, is often responsible for antibiotic treatment failure of these infections. We compared the antibiotic resistance pr...

Journal: :Antimicrobial Agents and Chemotherapy 2014

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