AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesAnthropology, Education, Sociology and Social PhenomenaInformation ScienceHealth Care
beta-LactamasesCarbapenemsEnterobacteriaceaeSerineEnterobacteriaceae InfectionsAcinetobacter baumanniibeta-Lactam ResistanceKlebsiella pneumoniaeKlebsiella InfectionsAcinetobacter InfectionsAnti-Bacterial Agentsbeta-LactamsBacterial ProteinsMicrobial Sensitivity TestsThienamycinsImipenemAzabicyclo CompoundsEnterobacter cloacaeMultiplex Polymerase Chain ReactionDrug Resistance, Multiple, BacterialGram-Negative BacteriaSerine EndopeptidasesMultilocus Sequence TypingDrug Resistance, BacterialAcinetobacterHospitalsMinocyclineElectrophoresis, Gel, Pulsed-FieldGram-Negative Bacterial InfectionsBacteriological TechniquesMolecular TypingSerine ProteasesSerine Proteinase InhibitorsCross InfectionDNA, BacterialDNA FingerprintingSequence Analysis, DNAPolymerase Chain ReactionPseudomonas aeruginosaPlasmidsSensitivity and SpecificityGenotypeAmino Acid SequencePhosphorylationMolecular Sequence DataSerine C-PalmitoyltransferasePhosphoserineSerine O-AcetyltransferaseGlycine HydroxymethyltransferaseProtein-Serine-Threonine KinasesThreonineSubstrate SpecificityBase SequenceMutagenesis, Site-DirectedSequence Homology, Amino AcidBinding SitesCell LineMutationRecombinant ProteinsKineticsMannose-Binding Protein-Associated Serine ProteasesSerpinsCloning, MolecularEnzyme ActivationProtein BindingProtein KinasesSignal TransductionAmino AcidsL-Serine DehydrataseProtein Structure, TertiaryIsoflurophatePhosphoprotein PhosphatasesProtease InhibitorsPeptide MappingPhenylmethylsulfonyl FluorideTrypsinCathepsin GAmino Acid SubstitutionGlycineEndopeptidasesSequence AlignmentProtein Processing, Post-TranslationalElectrophoresis, Polyacrylamide GelCysteineRacemases and EpimerasesTransfectionPhosphothreonineChymotrypsinPhosphoglycerate DehydrogenaseModels, MolecularPhosphopeptidesAlaninePhosphoproteinsEscherichia coliCells, CulturedStructure-Activity RelationshipPhosphoamino AcidsEnzyme InhibitorsOkadaic AcidProtein Phosphatase 2
Produce serineMetallo-carbapenemasesBeta-lactamasesESBLsKlebsiellaCarbapenemsSusceptibleResistanceAvibactamClinicalResistantClassStudy
Produce serine1
  • and CRE that produce serine- and/or metallo-carbapenemases. (bvsalud.org)
Metallo-carbapenemases1
  • During our studies, we targeted several clinically relevant metallo-carbapenemases (VIM-2, NDM-1 and GIM-1) and a serine-carbapenemase (OXA-48) and aimed to develop potential inhibitors or fragments that can ultimately be used in combination therapy with antibiotics to prolong their lifetime thus restoring the antibiotic efficacy. (uit.no)
Beta-lactamases5
  • Classes A, C, and D have a serine residue at the active site, whereas class B enzymes have zinc at the active site, ie, metallo-beta-lactamases (MBLs). (merckmanuals.com)
  • While ceftazidime-avibactam is an important antimicrobial in many CRE infections caused by serine-beta-lactamases (KPC, OXA48), it lacks activity against metallo-beta-lactamase (MBL) producing carbapenemases. (contagionlive.com)
  • Aztreonam is known to be stable against hydrolysis by MBLs but is susceptible to hydrolysis by serine beta-lactamases. (contagionlive.com)
  • By combining aztreonam and avibactam, the result is enhanced activity and aztreonam is "protected" from inactivation by serine beta-lactamases. (contagionlive.com)
  • Only four clinical isolates with OmpK35 and OmpK36 porin defects and carrying multiple beta lactamases and carbapenemases had raised MICs against ceftaroline/avibactam, 86% were successfully inhibited despite the porin defects and β-lactamases. (biobanking.com)
ESBLs3
  • Class A includes extended-spectrum BLs (ESBLs) and Klebsiella pneumoniae carbapenemases (KPCs), class B includes the MBLs (NDM, IMP, and VIM), class C includes AmpC, and class D includes the oxacillinases (OXAs). (merckmanuals.com)
  • Klebsiella pneumoniae carbapenemases (KPCs) are similar to ESBLs except that they also hydrolyze carbapenems. (merckmanuals.com)
  • A total of 50 MDR-GNB, of which 29 carried multiple β-lactamases, underwent broth microdilution (BMD) and disk diffusion (DD) testing as well as confirmation tests for ESBLs and carbapenemases. (udayton.edu)
Klebsiella1
Carbapenems1
  • In addition to inactivating carbapenems, these carbapenemases can hydrolyze almost all groups of β-lactams. (uit.no)
Susceptible1
  • The gene ontology (GO) terms associated with monooxygenase, iron binding, and passive transmembrane transporter activities were significantly enriched in four out of six resistant vs. susceptible comparisons while serine protease activity was elevated in all insecticide-resistant groups relative to the susceptible strain. (cdc.gov)
Resistance2
  • Many carbapenemases are encoded on plasmids, facilitating the spread of resistance genes among organisms of the same species or even different bacterial species. (msdmanuals.com)
  • By virtue of its universal stability to serine or metallo β-lactamases, zidebactam synergizes with PBP 3-binding cefepime and overcomes nearly all the known enzymatic and non-enzymatic resistance mechanisms in Gram-negative pathogens. (wockhardt.com)
Avibactam1
  • In conclusion, the results of this study demonstrated that the combination of avibactam at 4µg/ml with ceftaroline exponentially expands its spectrum of activity to cover the highly resistant organisms with multiple β-lactamases and serine carbapenemases commonly present in porin defective clinical isolates of K. pneumoniae . (biobanking.com)
Clinical1
  • Enterobacteriaceae in 2 clinical suggestive of serine carbapenemase logical and immunhistochemical study. (cdc.gov)
Resistant1
  • The obtained results were statistically analyzed and correlated to the obtained resistant genotypes that were determined by using polymerase chain reactions (PCR) for the detection of the major carbapenemase-encoding genes covering the three classes (Class A, B, and D) of carbapenemases. (biomedcentral.com)
Class1
  • The carbapenemases in A. baumannii have belonged to the bla OXA-23- , bla OXA-24- , and bla OXA-58- type class D family of serine β-lactamases and IMP/VIM class B metallo-β-lactamases [ 3 , 4 ]. (biomedcentral.com)
Study1
  • Our inhibitors gave different levels of inhibition towards the carbapenemases tested during the course of the study. (uit.no)