Results 21 to 30 of about 54,914 (224)

Extended-spectrum β-lactamase Enterobacteriaceae from patients in Jeddah, Saudi Arabia: Antibiotic susceptibility and molecular approaches

Journal of Contemporary Medical Sciences, 2021
Objectives: This study aimed to determine the Enterobacteriaceae strains among patients who suffering diarrhea, phenotypic and genotypic characterization of ESBL-producing isolates in Jeddah, Saudi Arabia. Methods: Stool samples were collected and cultured to determine the different Enterobacteriaceae strains, PCR was done for the isolates to detect ...
Wafa A. Alshehri, Tarek A. A. Moussa
openaire   +2 more sources

Clinical Significance of Extended-spectrum β-lactamase-producing Bacteria in First Pediatric Febrile Urinary Tract Infections and Differences between Age Groups [PDF]

Childhood Kidney Diseases, 2017
Purpose Extended-spectrum β-lactamase-producing bacteria-induced urinary tract infections are increasing and require more potent antibiotics such as carbapenems.
Sun Yeong Park, Ji Hong Kim
doaj   +1 more source

β-Lactamase is encoded on plasmid pACK3 inStaphylococcus simulansbiovarstaphylolyticus [PDF]

FEMS Microbiology Letters, 1991
Abstract Staphylococcus simulans biovar staphylolyticus , the lysostaphin-producing organism, contains five plasmids designated pACK1 through pACK5. Hybridization analysis using cloned β-lactamase gene ( bla ) as probe and characterization of cured strains revealed that bla resides on pACK3 rather than on the lysostaphin endopeptidase plasmid ...
Harry E. Heath, Lucie S. Heath, Karen E. Rose, Gary L. Sloan   +3 more
openaire   +1 more source

In Vitro Susceptibility of Aztreonam-Vaborbactam, Aztreonam-Relebactam and Aztreonam-Avibactam Associations against Metallo-β-Lactamase-Producing Gram-Negative Bacteria

Antibiotics, 2023
Background: Despite the availability of new options (ceftazidime-avibactam, imipenem-relebactam, meropenem-vaborbactam and cefiderocol), it is still very difficult to treat infections caused by metallo-β-lactamase (MBLs)-producers resistant to aztreonam.
Cécile Emeraud, Sandrine Bernabeu, Laurent Dortet   +2 more
doaj   +1 more source

Hinge-shift mechanism as a protein design principle for the evolution of β-lactamases from substrate promiscuity to specificity

Nature Communications, 2021
TEM-1 β-lactamase evolved from ancestral enzymes that degraded a variety of β-lactam antibiotics with moderate efficiency and degrades β-lactam antibiotics with a strong preference for penicillins.
Tushar Modi, Valeria A. Risso, Sergio Martinez-Rodriguez, Jose A. Gavira, Mubark D. Mebrat, Wade D. Van Horn, Jose M. Sanchez-Ruiz, S. Banu Ozkan   +7 more
doaj   +1 more source

SUSCEPTIBILITY AND DETECTION OF EXTENDED SPECTRUM β-LACTAMASE ENZYMES FROM OTITIS MEDIA PATHOGENS [PDF]

American Journal of Infectious Diseases, 2013
Otitis media is the bacterial infection of the middle ear usually accompanied with inflammation, effusions and pain. It can present clinically in two major forms: Acute Otitis Media (AOM) and Otitis Media with Effusion (OME) and it is one of the leading cause of hospital visits and antibiotic prescriptions amongst children and even adults.
openaire   +1 more source

Detection of cfxA2, cfxA3, and cfxA6 genes in beta-lactamase producing oral anaerobes

Journal of Applied Oral Science, 2016
Purpose The aim of this study was to identify β-lactamase-producing oral anaerobic bacteria and screen them for the presence of cfxA and BlaTEM genes that are responsible for β-lactamase production and resistance to β-lactam antibiotics.
Buhle BINTA, Mrudula PATEL
doaj   +1 more source

Repression of Virulence in Staphylococcus aureus by 2‐Aminothiol‐Mediated Quorum Quenching

Angewandte Chemie, EarlyView.
Simple analogues of cysteine that can eliminate the native autoinducing peptides (AIPs) of staphylococci extracellularly, before they activate their receptor, and turn off quorum sensing in different Staphylococcus aureus. The elimination of AIPs occurs through a mechanism similar to native chemical ligation (NCL). Further, this strategy showed promise
Bengt H. Gless, Riccardo Milazzo, Martin S. Bojer, Benjamin S. Sereika‐Bejder, Hanne Ingmer, Christian A. Olsen   +5 more
wiley   +2 more sources

Nucleotide sequence of the gene encoding the active-site serine β-lactamase fromStreptomyces cacaoi [PDF]

FEMS Microbiology Letters, 1988
Abstract The gene encoding the extracellular active-site serine β-lactamase of Streptomyces cacaoi previously cloned into Streptomyces lividans , has the information for the synthesis of a 303 amino-acid precursor. The β-lactamase as excreted by the host S.
Mauro V. Lenzini, Hiroshi Ishihara, Jean Dusart, Hiroshi Ogawara, Bernard Joris, Jozef Beeumen, Jean-Marie Frère, Jean-Marie Ghuysen   +7 more
openaire   +1 more source

Effect of β-Lactamase inhibitors on in vitro activity of β-Lactam antibiotics against Burkholderia cepacia complex species

Antimicrobial Resistance and Infection Control, 2016
Background Bacteria belonging to the Burkholderia cepacia complex (Bcc) are an important cause of chronic respiratory tract infections in cystic fibrosis patients.
Annelien Everaert, Tom Coenye
doaj   +1 more source