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Objective The aim of this study was to investigate whether the use of modified ultrafiltration at the end of cardiopulmonary bypass for cardiac surgical procedures significantly changes vancomycin serum concentrations. Design Prospective study. Setting Single tertiary cardiac center. Participants Twenty-six elective adult patients undergoing cardiac surgery with cardiopulmonary bypass from April 2014 to April 2015. Interventions Serum vancomycin concentrations were measured just before cardiopulmonary bypass; during cardiopulmonary bypass at 5, 30, 60 minutes and then every 60 minutes; after completion of cardiopulmonary bypass before initiation of modified ultrafiltration; and at the end of modified ultrafiltration. Measurements and Main Results Seventeen patients received modified ultrafiltration at the end of cardiopulmonary bypass. Serum vancomycin concentrations prior to cardiopulmonary bypass (45.9 ± 17.3 μg/mL) were significantly higher (P < 0.0001) than each time point following cardiopulmonary bypass (5 min 20.4 ± 6.4 μg/mL, 30 min 18.8 ± 5.4 μg/mL, 60 min 16.6 ± 4.9 μg/mL, and 120 min 14.3 ± 4.7 μg/mL). In the modified ultrafiltration group, serum vancomycin concentrations were 14.7 ± 4.6 μg/mL prior to modified ultrafiltration and 13.9 ± 4.3 μg/mL after ultrafiltration; this difference was statistically significant (P = 0.0288). The mean modified ultrafiltration volume was 465 ± 158 mL. Conclusions Using modified ultrafiltration at the end of cardiopulmonary bypass significantly decreases serum vancomycin levels, but not by a clinically relevant amount. The decrease is to a concentration that is still significantly higher than the minimum inhibitory concentration for Staphylococcus epidermidis and Staphylococcus aureus ; thus additional vancomycin administration is not recommended. [ABSTRACT FROM AUTHOR]

Similar to animal viruses, the abundant plant positive-strand RNA viruses replicate in infected cells by exploiting the vast resources of the host. This review focuses on virus–host interactions during tombusvirus replication. The multifunctional tombusvirus p33 replication protein not only interacts with itself, the viral p92pol polymerase, and viral RNA, but also with approximately 100 cellular proteins and subcellular membranes. Several negative regulatory host proteins, such as cyclophilins and WW motif containing proteins, also bind to p33 and interfere with p33''s functions. To explain how p33 can perform multiple functions, we propose that a variety of interactions involving p33 result in the commitment of p33 molecules to specific tasks. This facilitates tight spatial and temporal organization of viral replication in infected cells. [Copyright &y& Elsevier]