MICROBIOLOGICAL EVALUATION OF PANIPENEM/BETAMIPRON, A NEW PARENTERALLY ACTIVE CARBAPENEM II. MECHANISM OF ANTIBACTERIAL ACTIVITY OF PANIPENEM

• Published in: CHEMOTHERAPY Vol. 39; no. Supplement3; pp. 102 - 110
• Main Authors: Ohya, Satoshi, Utsui, Yukio, Yajima, Tsutomu, Domon, Haruki, Takenouchi, Takashi, Fukuoka, Takashi, Ajiki, Yoko, Sekine, Naoko, Kawada, Harumi, Yasuda, Hiroshi, Kuwahara, Shogo
• Format: Journal Article
• Language: Japanese
• Published: Japanese Society of Chemotherapy 1991
• Subjects: Panipenem/betamipron; Penicillin-binding proteins; Postantibiotic effect; β-Lactamase
• ISSN: 0009-3165; 1884-5894
• DOI: 10.11250/chemotherapy1953.39.Supplement3_102

Mechanism of antibacterial activity of panipenem (PAPM), a new carbapenem antibiotic, was studied. PAPM showed a high stability against hydrolysis by β-lactamases of various classes, including penicillinases, cephalosporinases and cefuroximases. This antibiotic strongly inhibited cephalosporinases and cefuroximases of gram-negative species. It also inhibited penicillinases of gram negative species, whereas it did not inhibit a penicillinase of gram-positive origanisms. It showed a high affinity for penicillin-binding protein (PBP) 1A, 1B, 2, 4, 5, and 6 of Escherichia coli. It induced spherical cells from E. coli treated with 1/8 MIC or higher concentrations, and at the MIC or higher concentrations it immediately lysed cells. Affinity for PBPs and influence on the morphology of PAPM in Pseudomonas aeruginosa was similar to those of E. coli. PAPM showed postanti-biotic effect not only against gram-positive organisms but also against gram-negative organisms. PAPM showed a cooperative bactericidal activity with human serum and white blood cells on E. coli.