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PubMed1996

[In vitro activity of a new fluoroquinolone, marbofloxacin (RO 09-1168) against strictly anaerobic bacteria and some bacteria from human fecal flora].

As recommended by the EEC, the in vitro activity of a veterinary quinolone has to be evaluated on human strains isolated from the gut and especially against anaerobes. Thus, the MICs for Marbofloxacin were determined by the reference agar method (Norma NCCLS M11 A3) using Wilkins Chalgren medium for the 124 anaerobic strains and Mueller Hinton agar for E. coli, Proteus, Enterococcus and Lactobacillus. On the whole aerobes, the activity of Marbofloxacin was equal or slightly greater to that of ofloxacin. The modal MIC was 0.03 mg/l for Enterobacteriaceae, 2 mg/l and 16 mg/l for Enterococcus and Lactobacillus strains, respectively. Considering the anti-anaerobic activity of this new drug, in comparison with that of ofloxacin, MICs for ofloxacin were generally one log2 higher for Gram negative bacilli and two log2 higher for Gram positive bacilli. Modal MICs for marbofloxacin were 0.12 mg/l for Clostridium perfringens, 0.5 mg/l for Bacteroides fragilis, Fusobacterium, Prevotella, and Peptostreptococcus strains, 1 mg/l for Bifidobacteria, 2 mg/l for non-fragilis members of the B. fragilis group, and 4 mg/l for C. difficile strains, respectively. It appears in vitro that Marbofloxacin was a more potent agent than ofloxacin on the whole anaerobes.

Anti-Infective Agents↗
PubMed1998

Activity of cefepime compared with other antibiotics against gram-positive bacteria and cefuroxime-resistant gram-negative bacteria.

BACKGROUND: Cefepime is a new, parenteral, fourth-generation antibiotic that is stable in the presence of Bush group 1 beta-lactamases. In vitro activity of cefepime, cefuroxime, ceftazidime, ciprofloxacin and imipenem against Gram-positive cocci and cefuroxime-resistant Gram-negative bacilli was studied. METHODS: The agar dilution method described by the US National Committee for Clinical Laboratory Standards was used to determine the minimum inhibitory concentrations of antibiotics tested. These included cefepime, cefuroxime, ceftazidime, ciprofloxacin and imipenem. The tested clinical isolates included Gram-positive cocci (methicillin-sensitive coagulase-negative staphylococci, methicillin-resistant coagulase-negative staphylococci, methicillin-sensitive Staphylococcus aureus, methicillin-resistant S aureus, Streptococcus pyogenes, viridans streptococci, Streptococcus pneumoniae, group D enterococci) and cefuroxime-resistant Gram-negative bacilli (Escherichia coli, Klebsiella pneumoniae, Acinetobacter spp, Pseudomonas aeruginosa, Enterobacter cloacae, Serratia marcescens, Burkholderia cepacia and Xanthomonas maltophilia). RESULTS: The activity of cefepime against most Gram-negative bacilli other than B cepacia and X maltophilia is better than that of ceftazidime. However, cefepime is less active against these Gram-negative bacilli than ciprofloxacin and imipenem. The activity of cefepime against B cepacia and X maltophilia is less than that of ceftazidime or ciprofloxacin. Among Gram-positive cocci, cefepime was active against most isolates of methicillin-sensitive staphylococci, S pyogenes, viridans streptococci and S pneumoniae. However, cefepime has poor activity against methicillin-resistant S aureus and enterococci. CONCLUSIONS: Due to its extended spectrum of activity, cefepime has potential use as suitable empiric monotherapy for the treatment of a variety of community- and hospital-acquired infections.

Cefepime↗
PubMed1990

Protein secretion in gram-negative bacteria: transport across the outer membrane involves common mechanisms in different bacteria.

The xcp genes are required for protein secretion by Pseudomonas aeruginosa. They are involved in the second step of the process, i.e. the translocation across the outer membrane, after the exoproteins have reached the periplasm in a signal peptide dependent fashion. The nucleotide sequence of a 2.5 kb DNA fragment containing xcp genes showed at least two complete open reading frames, potentially encoding proteins with molecular weights of 41 and 19 kd. Products with these apparent molecular weights were identified after expression of the DNA fragment in vitro and in vivo. Subcloning and complementation experiments showed that both proteins are required for secretion. The two products are located in the inner membrane and share highly significant homologies with the PulL and PulM proteins which are required for the specific secretion of pullulanase in Klebsiella pneumoniae. These homologies reveal the existence of a common mechanism for protein secretion in Pseudomonas aeruginosa and Klebsiella pneumoniae.

Amino Acid Sequence↗
PubMed2001

Bacteria as workers in the living factory: metal-accumulating bacteria and their potential for materials science.

Metal micro-/nano-particles with suitable chemical modification can be organized into new ceramic-metal (cermet) or organic-metal (orgmet) composites or structured materials. These materials are attracting significant attention because of their unique structures and highly optimized properties. However, the synthesis of composite materials with inhomogeneities on the nanometer or sub-micrometer scale is a continuing challenge in materials science. Many industrial physical and chemical surface-coating processes using conventional techniques are both energy and cost inefficient and require sophisticated instrumentation. In the future, biology might offer a superior option.

Bacterial Physiological Phenomena↗