Abstract: Operational since 1988, the Great Lakes Regional Water Use Database provides information on water uses to fulfill to state and provincial commitments under the 1985 Great Lakes Charter. Aggregated water use information is available for 9 water use categories (e.g., public supply and self-supply domestic, irrigation, livestock, industrial, thermoelectric fossil fuel, thermoelectric nuclear, hydroelectric and other), the 5 Great Lakes basins, 10 Great Lakes states and provinces. This database was designed to be a crude tool to track of water withdrawals, diversions and consumptive use. The most recent year for which water use data was collected is 2004. In total, water withdrawals for the year 2004 were approximately 850 billion gallons per day, or about 3,219 billion liters per day. Self-supplied hydroelectric is the largest single category of withdrawal and represents 95 percent of the total amount of water ?withdrawn? in 2004. This presentation will highlight 2004 regional water use trends, setting the stage for the sessions timely focus on the valuation of Great Lakes waters.

Abstract: Rickettsiae grow only intracellularly. The antibiotic susceptibility is assessed by plaque,dye uptake or IF assays. Rickettsiae are susceptible to doxycycline, thiamphenicol and fluroquinolones. Betalactams, aminoglycosides and cotrimoxazole are not active. Typhus group rickettsiae are susceptible to all macrolides,whereas the spotted fever are more resistant to rifampicin than the other rickettsiae. Rickettsiae felis is not susceptible to gentamicin, erythromycine, amoxicilline or cotrimoxazole. we present an overview of susceptibility of rickettsiae to antimicrobials

Abstract: Polycationic antimicrobial peptides are an important component of the innate defence of all species of life. These compounds are active against a broad range of bacterial strains, including antibiotic resistant isolates, and are synergistic with conventional antibiotics. The therapeutic use of a cationic antibiotic polymyxin B (PMB) was abandoned for a long time due to its undesirable side effects. However, the spread of resistance to currently used antibiotics has forced the reevaluation of PMB for clinical use. Using different substrates and inhibitors of energy metabolism we obtained information on the mechanism of PMB interaction with bacterial outer membrane (OM) as well as with the plasma membrane (PM). Methods: An electrochemical monitoring of K+, Ca2+, H+, tetraphenylphosphonium (TPP+), and phenyldicarbaundecaborane (PCB-) ion fluxes across envelopes of E. coli and Pseudoalteromonas spp. cells was performed. In parallel, the cell binding of fluorescent compound dansylpolymyxin, OD of bacterial suspensions, ATP content of cells, and bactericidal activity of PMB were studied. Results: Using different conditions of cell incubation, the OM permeabilizing activity of PMB was dissected from the PM depolarizing effects. These two stages were easily distinguishable in the presence of high concentrations of divalent cations and can be separated in time by 1-5 min interval. PMB-induced pores in bacterial envelope were registered, but the pore formation and depolarization of the PM were not obligatory for the dissipation of cell K+ gradient or the bactericidal action of this antibiotic. At conditions of increased ionic strength the dependence of membranotropic activity of PMB on metabolic state of the cells was discovered. Energization of the cells by glucose stimulated the binding of PMB to bacteria and the depolarizing activity of this antibiotic. Membranotropic effects of PMB were considerably stronger when all amount of the drug was added to the cell suspension at one stroke. Conclusions: 1. At low concentrations PMB compromises the barrier of the OM, while at higher concentrations it also depolarizes the PM by forming ion-permeable pores. 2. High ionic strength prevents the self-promoted entry of PMB into bacterial cells, though the ability to bind to the OM surface is not affected. 3. Suppression of energy metabolism of bacteria makes them more resistant to PMB.