In vitro investigation of BK-218, a new oral and parenteral cephalosporin

  title={In vitro investigation of BK-218, a new oral and parenteral cephalosporin},
  author={Istv{\'a}n J Szab{\'o} and Judit Barab{\'a}s and A K Tar and L{\'a}szl{\'o} Kiss and M. Y. Filep and Tim Schmidt and K{\'a}lm{\'a}n Marossy and Bela L. Toth-Martinez and Gy{\"o}rgy Barab{\'a}s and Ferenc Hern{\'a}di},
  journal={Antimicrobial Agents and Chemotherapy},
  pages={349 - 354}
The antibacterial activity of BK-218 was similar to that of cefamandole when it was tested against several laboratory strains. The inhibiting effect of BK-218 was greater than that of cephalexin and cefoxitin on penicillin-binding proteins of Escherichia coli HB101. This result was in close correlation with the relative inhibition of radiolabeled glucosamine incorporation (greatest with BK-218) and with the lytic effect (most intensive with BK-218). BK-218 proved to be a good inhibitor for all… Expand
Antimicrobial activity of three investigational oral cephalosporins (BK-218, cefdinir, and RU29246) against Legionella.
Three new, orally administered cephalosporins (BK-218, cefdinir, RU29246) were tested against 13 representative strains of Legionella and appear poorly suited by activity assays for Legionellosis therapy. Expand
Antibacterial activity of the investigational oral and parenteral cephalosporin BK-218
  • D. M. Johnson, R. Jones
  • Biology, Medicine
  • European Journal of Clinical Microbiology and Infectious Diseases
  • 2005
BK-218 was active against Streptococcus pneumoniae, Haemophilus influenzae andMoraxella catarrhalis but strains resistant to penicillins had higher MICs and BK- 218 had greater activity than cefuroxime or cefaclor against oxacillin-susceptibleStaphylococcus spp. Expand
New cephalosporins in development pipelines
One of the most commercially successful classes of human antibacterials is the cephalosporins, intially introduced in the 1960s, commanding a major market share worldwide and many in development, many seeking a niche position to gain a foothold in a mature therapy area. Expand


Cefaclor: In Vitro Spectrum of Activity and Beta-Lactamase Stability
  • H. Neu, K. Fu
  • Medicine, Chemistry
  • Antimicrobial Agents and Chemotherapy
  • 1978
Cefaclor was more active than cephalexin or cephalothin against Escherichia coli, Salmonella, and Shigella isolates but did not act against Serratia, Acinetobacter, indole-positive Proteus, or Bacteroides isolates. Expand
Cefatrizine Activity Compared with That of Other Cephalosporins
  • H. Neu, K. Fu
  • Biology, Medicine
  • Antimicrobial Agents and Chemotherapy
  • 1979
Cefatrizine had excellent activity against gram-positive cocci, inhibiting all except enterococci at minimal inhibitory concentrations below 1 μg/ml, and was more active than cephalothin or cephalexin against E. coli, Klebsiella, Enterobacter, Citrobacter, Salmonella, and Shigella. Expand
CGP 9000: a new orally active, broad-spectrum cephalosporin.
Upon oral administration to mice infected with various bacteria, CGP 9000 is, in general, 2 to 7 times more effective than either cephalexin or cephradine. Expand
Identification of the lethal target of benzylpenicillin in Streptococcus faecalis by in vivo penicillin binding studies
It is shown that in Streptococcus faecalis ATCC 9790 changes in conditions of growth are accompanied by changes in PBPs, and in the presence of the minimal dose of 14C-benzylpenicillin causing complete inhibition of cell growth, 100% of the total radioactivity is bound to a single protein (PBP 3). Expand
beta-Lactamase inhibitors.
In summary, Table XVI shows the inhibition profiles of representative beta-lactamases from each major class of Richmond and Sykes. Either resistance (R) or sensitivity (S) is given as a general guideExpand
Trapping of nonhydrolyzable cephalosporins by cephalosporinases in Enterobacter cloacae and Pseudomonas aeruginosa as a possible resistance mechanism.
Findings corroborate the assumption that binding of nonhydrolyzable cephalosporins, rather than hydrolysis by cep Halosporinases, may play an important role in resistance to these agents and other newer cep HALsporins in Enterobacteriaceae, as well as in other gram-negative bacteria. Expand
Novel Method for Detection of β-Lactamases by Using a Chromogenic Cephalosporin Substrate
A new cephalosporin with a highly reactive β-lactam ring was found to give an immediate color change in the presence of β-lactamases from many bacteria, including staphylococci, Bacillus species,Expand
Beta-Lactamases Produced by a Pseudomonas aeruginosa Strain Highly Resistant to Carbenicillin
It is clearly demonstrated that two β-lactamases were synthetized: one of them, constitutive, has its enzymatic activity directed mainly toward penicillins, and carbenicillin appears to be its best substrate (higher Vmax); thus, this β- lactamase is a “carbeniillinase” that differs from the well-known “TEM-like” enzymes. Expand
Interactions between beta-lactam antibiotics and isolated membranes of Streptococcus faecalis ATCC 9790.
The DD-carboxypeptidase-exchange membrane-bound enzyme in Streptococcus faecalis ATCC 9790 reacts with beta-lactam antibiotics to form complexes with rather long half-lives. Depending upon theExpand
A spectrophotometric assay of beta-lactamase action on penicillins.
A new method for measuring the enzymic hydrolysis of the beta-lactam ring in penicillins is described. The change in extinction in the u.v. region is determined. The method is sensitiveExpand