[Experience of using the antibacterial drug Fosfomycin Esparma for the treatment of acute uncomplicated cystitis in women].

AIM: To evaluate the efficacy and safety of the antibacterial drug fosfomycin trometamol (Fosfomycin Esparma) in women of reproductive age with acute uncomplicated cystitis. MATERIALS AND METHODS: In order to assess the efficacy and safety of using fosfomycin trometamol (Fosfomycin Esparma), a prospective, non-randomized, uncontrolled study involving 32 women with acute uncomplicated cystitis was carried out. The average patients age was 27.3+/-3.1 years. Before the study, all women underwent a general clinical, bacteriological, and ultrasound examination. Inclusion criteria was the presence of pathognomonic symptoms of acute uncomplicated cystitis. Exclusion criteria were as following: complicated urinary tract infection, anatomical and functional disorders of the urinary tract, comorbidities. All patients were prescribed a study drug at a dose of 3 g, once. The efficiency of therapy was evaluated on days 3 and 14 after administration of Fosfomycin Esparma based on clinical and microbiological cure and safety. RESULTS: The only bacterial pathogen isolated from the urine was E. coli. In 4 cases (12.5%) strains produced extended-spectrum -lactamase. The sensitivity of E. coli to fosfomycin, piperacillin/tazobactam, amikacin and meropenem was 100%. A resistance to ampicillin was 15.6%, compared to 9.4% for levofloxacin and norfloxacin and 12% for cefotaxime, ceftazidime, cefpoxin. By the 3rd day after receiving fosfomycin, the symptoms of cystitis were resolved in all patients. On day 14, according to the results of the urine culture, there was no growth of bacteria. During the follow-up period, no significant side effects was detected. CONCLUSION: Our study showed that antibacterial drug Fosfomycin Esparma in women of reproductive age with acute uncomplicated cystitis is effective and safe. Maintaining a high sensitivity to fosfomycin allows us to recommend this drug as an empirical antibiotic therapy in this cohort of patients.

[Problems in the diagnosis of ornithosis].

The paper describes 3 cases of ornithosis that could be detected by clinical and laboratory studies using immunological assays. In one case, its diagnosis was made late when the infection occurred in a woman working in a travel agency in Cyprus. The two other cases having an occupational contact (pet shop workers) were observed to have its acute form. All the described cases showed lung involvement characterized by external respiratory failure, one of the most common manifestations of ornithosis (psittacosis). Among the practically used laboratory tests, the indirect hemagglutination reaction is an accessible and effective serological assay for the diagnosis of ornithosis.

Effect of E20D substitution in the active site of Escherichia coli inorganic pyrophosphatase on its quaternary structure and catalytic properties.

Glutamic acid 20 is an evolutionarily conserved residue found within the active site of the inorganic pyrophosphatase of Escherichia coli (E-PPase). Here we determine the effect of E20D substitution on the quaternary structure and catalytic properties of E-PPase. In contrast to wild-type enzyme, which is hexameric under a variety of conditions, E20D-PPase can be dissociated by dilution into nearly inactive trimers, as shown by electrophoresis of cross-linked enzyme, analytical ultracentrifugation, and measurement of catalytic activity as a function of enzyme concentration. Hexamer stability is increased in the presence of both substrate and Mg2+, is maximal at pH 6.5, and falls off sharply as the pH is lowered or raised from this value. Measured at saturating substrate, 20 mM Mg2+ and pH 7.2, E20D substitution (a) decreases activity towards inorganic pyrophosphate (PPi) hydrolysis and oxygen exchange between water and inorganic phosphate (P1), (b) increases the rate of net PPi synthesis, and (c) decreases the amount of enzyme-bound PPi in equilibrium with Pi in solution. Measurements of PPi hydrolysis rate as a function of both Mg2+ concentration and pH for the E20D variant show that its decreased activity is largely accounted for on the basis of an increased pKa of the catalytically essential base at the active site, and the need for a Mg2+ stoichiometry of 5 in the enzyme-substrate complex, similar to what is seen for the D97E variant. By contrast, wild-type PPase catalysis over a wide range of Mg2+ concentration and pH is dominated by an enzyme-substrate complex having a total of four Mg2+ ions. These results are consistent with a supporting role for Glu20 in PPase catalysis and demostrate that even conservative mutation at the active site can perturb the quaternary structure of the enzyme.