Disease relevance of ECs2333

• Cytosolic intermediates for cell wall biosynthesis and degradation control inducible beta-lactam resistance in gram-negative bacteria [1].
• This observation might be important for designing inhibitors of NagZ that could prevent the establishment of beta-lactam resistance of Enterobacteria possessing inducible beta-lactamases [2].
• Balance between two transpeptidation mechanisms determines the expression of beta-lactam resistance in Enterococcus faecium [3].
• In this study, the roles of the drug exporters of E. coli in beta-lactam resistance were examined [4].
• Both ampicillin and cefuroxime therapy of neonates selected drug- and species-dependent beta-lactam resistance patterns in fecal strains of Escherichia coli and Klebsiella spp [5].

High impact information on ECs2333

• Escherichia coli CF349 exhibited a complex beta-lactam resistance phenotype, including resistance to amoxicillin and ticarcillin alone and in combination with clavulanate and to some extended-spectrum cephalosporins [6].
• We found that five of five resistance-nodulation-cell division-type drug exporters confer beta-lactam antibiotic resistance, while no other drug exporters confer any beta-lactam resistance even when they cooperate with TolC [4].
• Desulfovibrio desulfuricans clinical isolate D3 had a clavulanic acid-inhibited beta-lactam resistance profile and was resistant to some expanded-spectrum cephalosporins [7].
• The outer membrane of gram-negative bacteria plays a major role in beta-lactam resistance as it slows down antibiotic entry into the periplasm and therefore acts in synergy with beta-lactamases and efflux systems [8].
• Transconjugants in Escherichia coli were obtained at low levels (10(-7) per donor cell) and exhibited a similar beta-lactam resistance pattern (resistant to ampicillin, ticarcillin, and ceftazidime at 64 microg/ml) [9].

Chemical compound and disease context of ECs2333

• Bacteroides fragilis CS30 is a clinical isolate resistant to high concentrations of benzylpenicillin and cephaloridine but not to cephamycin or penem antibiotics. beta-Lactam resistance is mediated by a chromosomally encoded cephalosporinase produced at a high level [10].
• A clinical isolate of Bacteroides vulgatus was resistant to tetracycline, clindamycin, ampicillin, cephaloridine, cefoxitin, and other beta-lactam antibiotics except imipenem. beta-Lactam resistance was mediated by a membrane-associated, clavulanate-sensitive cephalosporinase capable of degrading cephalosporins and penicillins [11].
• Ampicillin-sulbactam and amoxicillin-clavulanate susceptibility testing of Escherichia coli isolates with different beta-lactam resistance phenotypes [12].
• Thirty-seven of 42 TMPR isolates from six species of gram-negative bacilli conjugally transferred TMP resistance to K12 E. coli. beta-Lactam resistance cotransferred from 21 of the 37 donors, and sulfamethoxazole (SMZ) resistance cotransferred from five of the 37 donors [13].
• When co-amoxiclav-resistant E. coli was detected in the stools after diagnosis of E. coli UTI, isolates were compared with urinary E. coli isolates in terms of clonal relatedness, beta-lactam susceptibility and mechanisms of beta-lactam resistance [14].

Biological context of ECs2333

• Although conferring a narrow-spectrum beta-lactam resistance phenotype, OXA-55 had carbapenem-hydrolyzing activity that mirrored the reduced susceptibility to imipenem observed in S. algae KB-1 [15].
• Molecular genetic analysis of cephalosporinase production and its role in beta-lactam resistance in clinical isolates of Enterobacter cloacae [16].
• A Haemophilus influenzae strain (T-1,3) possessing clinical beta-lactam resistance due to altered penicillin-binding protein 3 was used to construct a recombinant cosmid gene bank in Escherichia coli [17].
• All isolates transferred beta-lactam resistance to Escherichia coli through conjugative, IncN plasmids that exhibited differences in the RFLP and hybridization patterns with bla(VIM)- and IS26-specific probes [18].
• Production of extended-spectrum beta-lactamases (ESBLs) is an important mechanism of beta-lactam resistance in Enterobacteriaceae: Identification of ESBLs based on phenotypic tests is the strategy most commonly used in clinical microbiology laboratories [19].

Associations of ECs2333 with chemical compounds

• This was in contrast to our previous findings that ampicillin, but not cefuroxime, contributed to the emergence of beta-lactam resistance also by the promotion of nosocomial spread of resistant strains [5].
• Compared with SHV-5, the mutant beta-lactamases conferred lower levels of beta-lactam resistance and were less efficient in hydrolyzing ampicillin, cephalothin, and cefotaxime [20].
• A study has been conducted to identify the beta-lactamases most likely to contribute to beta-lactam resistance in clinical populations and to investigate their interactions with cefuroxime and newer cephalosporins [21].
• There was a very high incidence of beta-lactam resistance (ampicillin resistance greater than 80% and cephaloridine resistance greater than 65%) amongst these isolates [22].
• When a mutant disrupted in pcbR was constructed by gene replacement, the resulting pcbR mutant exhibited a significant decrease in its resistance to benzylpenicillin and cephalosporins, indicating that pcbR is involved in beta-lactam resistance in this organism [23].

Analytical, diagnostic and therapeutic context of ECs2333

• We developed 2 variants, A and B, of a multiplex polymerase chain reaction method for detecting the beta-lactam resistance genes bla(TEM), bla(SHV), and bla(OXA) in 122 uropathogenic Escherichia coli animal strains [24].

References