Results 21 to 30 of about 14,068 (191)

Distribution of β-lactamases and emergence of carbapenemases co-occurring Enterobacterales isolates with high-level antibiotic resistance identified from patients with intra-abdominal infection in the Asia–Pacific region, 2015–2018

Journal of Microbiology, Immunology and Infection, 2022
Purpose: In this study, we aimed to assess the geographic distribution and molecular characteristics of β-lactamases among Enterobacterales isolates causing intra-abdominal infections (IAIs) from 2015 to 2018 in the Asia–Pacific region.
Yu-Chin Chen, Wei-Yu Chen, Wei-Yun Hsu, Hung-Jen Tang, Yun Chou, Yi-Hsin Chang, Chi-Chung Chen, Yin-Ching Chuang, Tu-Hsuan Chang   +8 more
doaj   +1 more source

Comparision of Three Laboratory Tests for Detection of AmpC β Lactamases in Klebsiella Species and E. Coli [PDF]

Journal of Clinical and Diagnostic Research, 2014
Background and objective: AmpC β lactamases are one of the important causes of drug resistance in gram negative bacteria. Failure to detect these enzymes in the laboratory has contributed to therapeutic failures but there are till date no standard ...
D.L. Maraskolhe, V.S. Deotale, D.K. Mendiratta, P. Narang   +3 more
doaj   +1 more source

Broad-spectrum β-lactamases among Enterobacteriaceae of animal origin: molecular aspects, mobility and impact on public health [PDF]

, 2010
Broad-spectrum β-lactamase genes (coding for extended-spectrum β-lactamases (ESBLs) and AmpC β-lactamases) have been frequently demonstrated in the microbiota of food-producing animals. This may pose a human health hazard since these genes may be present
Butaye, Patrick, Dewulf, Jeroen, Haesebrouck, Freddy, Herman, Lieve, Heyndrickx, Marc, Martel, An, Persoons, Davy, Smet, Annemieke   +7 more
core   +1 more source

Clonal Relationship and Resistance Profiles Among ESBL-Producing Escherichia coli

Frontiers in Cellular and Infection Microbiology, 2021
AmpC β-lactamases hydrolyze all β-lactams except cefepime and carbapenems. The study of AmpC-producing E. coli has high priority for the infection control committee. This research is aimed to investigate the resistant urinary AmpC-generating E.
Alireza Dolatyar Dehkharghani, Setareh Haghighat, Marjan Rahnamaye Farzami, Mohammad Rahbar, Masoumeh Douraghi   +4 more
doaj   +1 more source

Assessing the occurrence and transfer dynamics of ESBL/pAmpC-producing Escherichia coli across the broiler production pyramid [PDF]

, 2019
Extended-spectrum \u3b2-lactamase (ESBL)- and plasmid mediated AmpC-type cephalosporinase (pAmpC)-producing Escherichia coli (ESBL/pAmpC E. coli) in food-producing animals is a major public health concern.
APOSTOLAKOS, ILIAS, Fasolato, L., MUGHINI GRAS, LAPO, Piccirillo, A.   +3 more
core   +1 more source

Effect of β-lactamase inhibitors on in vitro activity of β-lactam antibiotics against Burkholderia cepacia complex species [PDF]

, 2016
Background: Bacteria belonging to the Burkholderia cepacia complex (Bcc) are an important cause of chronic respiratory tract infections in cystic fibrosis patients. Intrinsic resistance to a wide range of antimicrobial agents, including a variety of beta-
Coenye, Tom, Everaert, Annelien
core   +2 more sources

Bicyclic Boronates as Potent Inhibitors of AmpC, the Class C β-Lactamase from Escherichia coli

Biomolecules, 2020
Resistance to β-lactam antibacterials, importantly via production of β-lactamases, threatens their widespread use. Bicyclic boronates show promise as clinically useful, dual-action inhibitors of both serine- (SBL) and metallo- (MBL) β-lactamases.
Pauline A. Lang, Anete Parkova, Thomas M. Leissing, Karina Calvopiña, Ricky Cain, Alen Krajnc, Tharindi D. Panduwawala, Jules Philippe, Colin W. G. Fishwick, Peteris Trapencieris, Malcolm G. P. Page, Christopher J. Schofield, Jürgen Brem   +12 more
doaj   +1 more source

The functional repertoire of AmpR in the AmpC β-lactamase high expression and decreasing β-lactam and aminoglycosides resistance in ESBL Citrobacter freundii

Heliyon, 2023
Citrobacter freundii is characterized by AmpC β-lactamases that develop resistance to β-lactam antibiotics. The production of extended-spectrum β-lactamase (ESBL) is substantially high in Escherichia coli, C.
Falak Naz Tariq, Mehreen Shafiq, Nadeem Khawar, Gul Habib, Haji Gul, Azam Hayat, Mujaddad Ur Rehman, Ihab Mohamed Moussa, Eman A. Mahmoud, Hosam O. Elansary   +9 more
doaj   +1 more source

Identification of DHA-23, a Novel Plasmid-mediated and Inducible AmpC beta-Lactamase from Enterobacteriaceae in Northern Taiwan

Frontiers in Microbiology, 2015
Objectives: AmpC β-lactamases are classified as Amber Class C and Bush Group 1. AmpC β-lactamases can hydrolyze broad and extended-spectrum cephalosporins, and are not inhibited by β-lactamase inhibitors such as clavulanic acid.
Wen-Shyang eHsieh, Wen-Shyang eHsieh, Wen-Shyang eHsieh, Nai-yu eWang, Jou-an eFeng, Li-chuan eWeng, Hsueh-Hsia eWu, Hsueh-Hsia eWu   +7 more
doaj   +1 more source

Crystal structure of AmpC BER and molecular docking lead to the discovery of broad inhibition activities of halisulfates against β-lactamases

Computational and Structural Biotechnology Journal, 2021
AmpC BER is an extended-spectrum (ES) class C β-lactamase with a two-amino-acid insertion in the H10 helix region located at the boundary of the active site compared with its narrow spectrum progenitor.
Bo-Gyeong Jeong, Jung-Hyun Na, Da-Woon Bae, Soo-Bong Park, Hyi-Seung Lee, Sun-Shin Cha   +5 more
doaj   +1 more source