The use of antibiotic-impregnated fibrin sealant for the prevention of surgical site infection associated with spinal instrumentation.

PURPOSE: The purpose of this study was to determine if the use of antibiotic-impregnated fibrin sealant (AFS) was effective in preventing surgical site infections (SSI) associated with spinal instrumentation. METHODS: In a preliminary study, five pieces of vancomycin-impregnated fibrin sealant, five nuts that were not treated with the sealant, and five nuts that were treated with the sealant were subjected to agar diffusion testing. In a clinical study, the rates of deep SSI were compared between 188 patients who underwent procedures involving spinal instrumentation without AFS (group 1) and 196 patients who underwent procedures involving spinal instrumentation with AFS (group 2). RESULTS: All five pieces of vancomycin-impregnated fibrin sealant and the five nuts treated with the sealant exhibited antimicrobial efficacy, while the five untreated nuts did not exhibit antimicrobial efficacy in the agar diffusion test. In the clinical study, 11 (5.8 %) of the 188 patients in group 1 acquired a deep SSI, while none (0 %) of the 196 patients in group 2 acquired a deep SSI. CONCLUSION: The present study demonstrated that the application of AFS to spinal instrumentation yielded good clinical outcomes in terms of the prevention of postoperative spinal infections. It is hoped that limiting AFS use to patients requiring spinal instrumentation and those with risk factors for SSI will reduce the overall costs while preventing SSIs.

Studies of interaction of homo-dimeric ferredoxin-NAD(P)+ oxidoreductases of Bacillus subtilis and Rhodopseudomonas palustris, that are closely related to thioredoxin reductases in amino acid sequence, with ferredoxins and pyridine nucleotide coenzymes.

Ferredoxin-NADP(+) oxidoreductases (FNRs) of Bacillus subtilis (YumC) and Rhodopseudomonas palustris CGA009 (RPA3954) belong to a novel homo-dimeric type of FNR with high amino acid sequence homology to NADPH-thioredoxin reductases. These FNRs were purified from expression constructs in Escherichia coli cells, and their steady-state reactions with [2Fe-2S] type ferredoxins (Fds) from spinach and R. palustris, [4Fe-4S] type Fd from B. subtilis, NAD(P)(+)/NAD(P)H and ferricyanide were studied. From the K(m) and k(cat) values for the diaphorase activity with ferricyanide, it is demonstrated that both FNRs are far more specific for NADPH than for NADH. The UV-visible spectral changes induced by NADP(+) and B. subtilis Fd indicated that both FNRs form a ternary complex with NADP(+) and Fd, and that each of the two ligands decreases the affinities of the others. The steady-state kinetics of NADPH-cytochrome c reduction activity of YumC is consistent with formation of a ternary complex of NADPH and Fd during catalysis. These results indicate that despite their low sequence homology to other FNRs, these enzymes possess high FNR activity but with measurable differences in affinity for different types of Fds as compared to other more conventional FNRs.