نتایج جستجو برای: β lactam resistance

تعداد نتایج: 546701  

2017
Yuji OHASHI Tomohiko FUJISAWA

Antibiotic resistance genes in the feces of healthy young adult Japanese were analyzed with polymerase chain reaction using specific primers. Antibiotic resistance genes against macrolides (ermB, ermF, ermX, and mefA/E), tetracyclines (tetW, tetQ, tetO, and tetX), β-lactam antibiotics (blaTEM ), and streptomycin (aadE) were detected in more than 50% of subjects. These antibiotic resistance gene...

Journal: :Asian Pacific journal of allergy and immunology 2016
Wiparat Manuyakorn Prapasiri Singvijarn Suwat Benjaponpitak Wasu Kamchaisatian Ticha Rerkpattanapipat Cherapat Sasisakulporn Wanlapa Jotikasthira

OBJECTIVE Skin testing with penicilloyl-polylysine (PPL) and a minor determinant mixture (MDM) were previously recommended for evaluating β-lactam hypersensitivity. However, PPL and MDM have not been commercially available. This study was to determine the negative predictive value (NPV) of skin testing with β-lactam antibiotics for the diagnosis of β-lactam hypersensitivity. METHOD Patients a...

Journal: :The Journal of antimicrobial chemotherapy 2013
H Jacquier G Marcadé E Raffoux H Dombret P L Woerther J L Donay G Arlet E Cambau

OBJECTIVES A relapse from Escherichia coli bloodstream infection was observed in a patient with acute leukaemia treated with ceftazidime for 7 days for febrile neutropenia. Whereas the original E. coli isolate was resistant to β-lactam/β-lactamase inhibitor combinations (EC1), the relapse E. coli isolate showed a similar phenotype but with resistance extended to ceftazidime (EC2). We investigat...

2016
Young-Sik Choe Ji-Hoon Lee Soo-Geun Jo Kwan Ha Park

As a novel strategy to remove β-lactam antibiotic residues from fish tissues, utilization of β-lactamase, enzyme that normally degrades β-lactam structure-containing drugs, was explored. The enzyme (TEM-52) selectively degraded β-lactam antibiotics but was completely inactive against tetracycline-, quinolone-, macrolide-, or aminoglycosidestructured antibacterials. After simultaneous administra...

Journal: :The Veterinary record 2014
C Dias C R Serra L C Simões M Simões A Martinez-Murcia M J Saavedra

AeromonAs are Gram-negative, facultative-anaerobic, non-sporeforming, glucose-fermenting, oxidaseand catalase-positive rods (Martin-Carnahan and Joseph 2005). Apart from fish, which are widely reported hosts for Aeromonads, insects, crustaceans, reptiles, birds and mammals were also found to harbour Aeromonas species, both in healthy and disease state (Pearson and others 2000, Turutoglu and oth...

Journal: :Journal of anatolian environmental and animal sciences 2021

In this study, it was aimed to investigate the presence of Klebsiella pneumoniae and phenotypically carbapenemase, extended-spectrum β-lactamase (ESBL), acquired-AmpC beta-lactamase, multiple antibiotic resistance isolates in faeces budgerigars parrots. A total 96 faecal samples belonging 54 42 parrots were used study. Cultivation performed on various media for identification pneuomiae from col...

2013
Avneet Saini Rohit Bansal A. Saini

New Delhi metallo-β-lactamase (NDM-1) has created a medical storm ever since it was first reported; as it is active on virtually all clinically used β-lactam antibiotics. NDM-1 rampancy worldwide is now considered a nightmare scenario, particularly due to its rapid dissemination. An underlying theme in the majority of recent studies is structural characterization as knowledge of the three-dimen...

Journal: :Enfermedades infecciosas y microbiologia clinica 2017
Inmaculada López-Hernández Noemí Alonso Marta Fernández-Martínez Laura Zamorano Alba Rivera Antonio Oliver M Carmen Conejo Luis Martínez-Martínez Ferrán Navarro Alvaro Pascual

INTRODUCTION Antimicrobial resistance in Enterobacteriaceae is increasing worldwide and is making treating infections caused by multidrug-resistant Enterobacteriaceae a challenge. The use of β-lactam agents is compromised by microorganisms harboring extended-spectrum β-lactamases (ESBLs) and other mechanisms of resistance. Avibactam is a non β-lactam agent that inhibits clinically relevant β-la...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2011
Narisara Chantratita Drew A Rholl Bernice Sim Vanaporn Wuthiekanun Direk Limmathurotsakul Premjit Amornchai Aunchalee Thanwisai Hui Hoon Chua Wen Fong Ooi Matthew T G Holden Nicholas P Day Patrick Tan Herbert P Schweizer Sharon J Peacock

Known mechanisms of resistance to β-lactam antibiotics include β-lactamase expression, altered drug target, decreased bacterial permeability, and increased drug efflux. Here, we describe a unique mechanism of β-lactam resistance in the biothreat organism Burkholderia pseudomallei (the cause of melioidosis), associated with treatment failure during prolonged ceftazidime therapy of natural infect...

2012
Ana Amoroso Julien Boudet Stéphanie Berzigotti Valérie Duval Nathalie Teller Dominique Mengin-Lecreulx André Luxen Jean-Pierre Simorre Bernard Joris

To resist to β-lactam antibiotics Eubacteria either constitutively synthesize a β-lactamase or a low affinity penicillin-binding protein target, or induce its synthesis in response to the presence of antibiotic outside the cell. In Bacillus licheniformis and Staphylococcus aureus, a membrane-bound penicillin receptor (BlaR/MecR) detects the presence of β-lactam and launches a cytoplasmic signal...

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