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Protective activity of habekacin and four other aminoglycosides in mouse septicaemia caused by Enterobacteriaceae.

The in vivo efficacy of habekacin, an aminoglycoside antibiotic obtained by chemical derivation from dibekacin, was compared to that of gentamicin (GEN), tobramycin (TOB), kanamycin (KAN) and amikacin (AMI) in a protection test in mice. The 50% effective dose (ED50) was determined in groups of animals challenged with bacterial suspensions injected intraperitoneally together with mucin, and treated subcutaneously 1 h and 6 h later. The bacterial strains used were: Escherichia coli (three GEN sensitive strains and one GEN-KAN-TOB resistant strain), Enterobacter cloacae (one GEN-KAN resistant strain), Serratia marcescens and Klebsiella pneumoniae (one GEN sensitive strain and one GEN resistant strain). In this model, habekacin was found to be as active as GEN against GEN sensitive strains and more active than AMI on GEN, GEN-KAN and GEN-KAN-TOB resistant strains.

Amikacin↗

The numerous common antigens of enterobacteriaceae.

A mosaic of proteins is synthesized by each of the Enterobacterial species grown on artificial media (tryptose-agar, Difco). Their existence was proven with the help of sera prepared in rabbits with proteins from: S. enteritidis, S. typhi, S. typhimurium, S. paratyphi C, E. coli, and Sh. sonnei. The induced antibodies, strongly precipitated numerous heterologous Enterobacterial proteins. The proteins of Sh. dysenteriae 4, although reacting against the heterologous sera, were poor immunogens and induced, mainly, homologous antibodies. Comparative agar-gel diffusions of the same proteins against the antiproteinic sera and corresponding antibacterial sera proved that the bacteria induced fewer antibodies against a reduced number of heterologous antigens. Thus, it is evident that a competition among the numerous antigens of a bacterium takes place when whole bacteria are used for immunizations. The differences in the degree of relatedness of Salmonellae, Shigellae, and E. coli are illustrated by their reactions in agar-gel against homologous and heterologous sera. The serological activity of heated proteins (1 hr at 100 degrees C) against the antiproteinic sera differed according to the intrinsic qualities of the analysed materials.

Animals↗