In vitro activity of LJC10,627, a new carbapenem antibiotic with high stability to dehydropeptidase I
| Autor: | Katsuyuki Nishiki, M Yoshida, M Hikida, Kimiko Ubukata, Y Furukawa, K Tashiro, Masatoshi Konno, S Mitsuhashi |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Carbapenem
Imipenem Dipeptidases Swine Ceftazidime Microbial Sensitivity Tests Muramoylpentapeptide Carboxypeptidase medicine.disease_cause Gram-Positive Bacteria Kidney beta-Lactamases Microbiology Bacterial Proteins Staphylococcus epidermidis Gram-Negative Bacteria medicine polycyclic compounds Animals Penicillin-Binding Proteins Pharmacology (medical) Microscopy Phase-Contrast Biapenem Pharmacology biology Pseudomonas aeruginosa Hydrolysis biochemical phenomena metabolism and nutrition biology.organism_classification bacterial infections and mycoses Kinetics Infectious Diseases Carbapenems Hexosyltransferases Staphylococcus aureus Peptidyl Transferases Thienamycins Bacteroides fragilis Carrier Proteins medicine.drug Protein Binding Research Article |
| Zdroj: | Antimicrobial agents and chemotherapy. 34(6) |
| ISSN: | 0066-4804 |
| Popis: | The in vitro activity of LJC10,627, a new carbapenem, was compared with those of imipenem and ceftazidime. LJC10,627 had broad-spectrum activity against gram-positive and gram-negative clinical isolates. The MICs of this compound for 90% of members of the family Enterobacteriaceae tested (MIC90s), including strains resistant to ceftazidime, ranged from 0.1 to 25 micrograms/ml. LJC10,627 inhibited Pseudomonas aeruginosa at an MIC90 of 3.13 micrograms/ml; it thus was twofold more active than imipenem. This compound inhibited Haemophilus, Neisseria, and Branhamella species at MIC90s of 3.13, 0.1, and 0.1 micrograms/ml, respectively. LJC10,627 was two- to fourfold less active than imipenem against methicillin-susceptible Staphylococcus aureus and Staphylococcus epidermidis at MIC90s of 0.1 and 0.39 microgram/ml. However, the compound was found to be twofold more active than imipenem against Bacteroides fragilis at an MIC90 of 1.56 microgram/ml. LJC10,627 was very stable to various beta-lactamases except for Xanthomonas maltophilia oxyiminocephalosporinase type II. LJC10,627 was minimally hydrolyzed by swine renal dehydropeptidase I; its residual activity was 93.0% after 2 h. Killing kinetics of this compound for Escherichia coli and Pseudomonas aeruginosa showed that bactericidal action occurred at concentrations above the MIC (0.05 and 0.39 microgram/ml, respectively). LJC10,627 had a high affinity for penicillin-binding proteins 2, 4, and 1B(s) of Escherichia coli and Pseudomonas aeruginosa and penicillin-binding proteins 1 and 4 of Staphylococcus aureus. |
| Databáze: | OpenAIRE |
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