1,721,157 research outputs found
Penicillin-binding proteins and the intrinsic resistance to beta-lactams in gram-positive cocci
No full textThe chemical composition of peptidoglycan of Klebsiella pneumoniae strain Mir A12 and ATCC 13883
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Characterization of a conditional mutant with altered envelope showing pH-dependent morphology and temperature-dependent division
No full textRole of PBSs and outer membrane permeability in determining susceptibility of Enterobacteriacee to carbapenems
No full textIn vitro activity and beta-lactamase stability of LY163892
No full textSusceptibility testing of clinical isolates of several gram-negative and gram-positive species showed LY163892 to be more active than cefaclor and cephalexin. OXA-2, TEM-1, TEM-2, PSE-1, CEP-1, CARB-3 and SHV-1 beta-lactamases showed similar activity against LY163892 and cefaclor, whereas OXA-1 hydrolyzed the latter more rapidly. Organisms producing these beta-lactamases, but not TEM-2 and CEP-1, appeared to be more susceptible to LY163892 than cephalexin, although cephalexin proved to be more resistant to beta-lactamase activity. Strains producing TEM-2 and CEP-1 were resistant to LY163892, cefaclor and cephalexin
Synergy and mechanism of interaction between pefloxacin and penicillin G against enterococci
No full textIn vitro synergy between penicillin and pefloxacin against Enterococcus hirae and Enterococcus faecium strains with different penicillin susceptibility was studied. The combination was synergistic against penicillin-resistant strains, E. hirae R40 and E. faecium 28R, but not against the penicillin-susceptible ones (E. hirae ATCC 9790 and E. faecium 28S). Analysis of PBPs of cells, grown in the presence of pefloxacin, showed that PBP5 of penicillin-resistant strains, the PBP responsible for the resistance of enterococci to beta-lactam antibiotics, is consistently reduced while it is almost unaffected in the penicillin-susceptible strains even at the highest concentrations of pefloxacin. These results indicate that pefloxacin interferes with the mechanism of synthesis of PBPs and particularly of PBP5, a protein whose production has already been modified in resistant strains, in some way rectifing the previous alteration
Cell division, macromolecular synthesis and morphology dependent on the state of the envelope in a mutant of Klebsiella pneumoniae
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Reliability of the MB/BacT system for testing susceptibility of Mycobacterium tuberculosis isolates to antituberculous drugs
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