Effect of Plate Configuration in the Primary Stability of Osteotomies and Biological Reconstructions of Femoral Defects: Finite-Element Study.

BACKGROUND/OBJECTIVE: Osteosynthesis is an alternative treatment for stabilizing femur-bone traumas. The initial stability of the fixation systems is one of the biomechanical parameters affecting implant failure and bone union, especially in surgeries of intercalary reconstructions after the removal of bone tumors. This study aimed to investigate the initial biomechanical effect of using one or two osteosynthesis plate configurations for femoral fixation and the effect of fastening the allograft to the osteosynthesis plate in the case of femoral allograft reconstructions. METHODS: Three finite-element models of a femur with three different fixation conditions for a transverse osteotomy in the middle of the diaphysis, i.e., using one and two osteosynthesis plates and an intercalary allograft, were constructed. An eight-hole compression plate and a six-hole second plate were used to simulate osteosynthesis plates. The plate screws were tightened previously to the loading, and the tightening sequences simulate the bolt-tightening procedure in a surgical environment. The models were imported into the ADINA System for nonlinear analysis, using compression loads applied over the femur head. RESULTS: Models with the dual fixation systems had the most outstanding compression stiffness. The femur head movement in the dual plate system was 24.8% smaller than in the single plate system. A statistical analysis of a region of interest (VOI) placed in the femur diaphysis showed that the biomechanical effect of using the dual plate system is smaller in the osteotomy region than at the femur head, e.g., a displacement average decrease of only 5% between the two systems, while the maximum value decreases by 26.8%. The allograft fixation to the second osteosynthesis plate leads to an improvement in the system stability. CONCLUSIONS: The results presented in this work show that including the bolt analysis in the femoral diaphysis osteotomy fixation will allow for capturing the nonlinear behavior of the osteotomy region more realistically. The stability of the intercalary reconstruction of the femoral diaphysis was higher when the allograft was fastened to the second osteosynthesis plate.

Comparison of the antibacterial effect of modified 3-mix paste versus Ultrapex over anaerobic microorganisms from infected root canals of primary teeth: an in vitro study.

OBJECTIVE: The aim of this study was to evaluate in vitro the antimicrobial efficacy of a modified 3-mix paste and to compare it with an iodoform paste (Ultrapex) against anaerobic microorganisms isolated from root canals of infected or necrotic primary teeth. STUDY DESIGN: An in vitro experimental assay was performed over isolated and identified anaerobic microorganisms of 21 samples, in order to compare the antimicrobial ability of both root canal filling materials, using a disc-diffusion method. RESULTS: A total of 21 microbial samples (15 polymicrobial and 6 monomicrobial) were obtained, from which 19 different strains were identified. Modified 3-mix paste showed an excellent antimicrobial effect against most of both kinds of microbial samples, although some of them exhibited resistance; on the other hand, Ultrapex showed only minimal antimicrobial ability (null or low categories). Clostridium ramosum exhibited the most resistance to both materials. CONCLUSION: The bactericidal effect of the modified 3-mix paste was superior to Ultrapex, with a statistically significant difference, against anaerobic microorganisms isolated from infected root canals of primary teeth.

Reduction in bacterial loading using 2% chlorhexidine gluconate as an irrigant in pulpectomized primary teeth: a preliminary report.

OBJECTIVE: The aim of this study was to evaluate the reduction in bacterial loading using 2% chlorhexidine gluconate as an irrigating solution in pulpectomized primary teeth. STUDY DESIGN: A randomized, controlled clinical trial was performed that included primary teeth with pulp necrosis. Forty necrotic teeth were included, 20 irrigated with 2% chlorhexidine gluconate (experimental group) and 20 with sterile saline solution (control group); in all cases, 2 microbiological samples from within the canals were taken with sterile paper points, the first after the canal opening and before the first irrigation, and the second after instrumentation and final irrigation, before filling. All samples were evaluated by McFarlands scale. RESULTS: The results were statistically analyzed by the Mann-Whitney U test. After analyzing samples before and after irrigation in the control group (saline), we found a significant decrease of bacterial load (P < 0.0002). The same occurred in the chlorhexidine group samples (P < 0.0001). When both groups were compared post-irrigation, a statistically significant difference was observed in favor of 2% chlorhexidine gluconate. CONCLUSION: Two percent chlorhexidine gluconate showed a greater reduction of intracanal bacterial loading compared with that observed with sterile saline solution. This irrigating solution is suggested as an alternative for pulpectomy of necrotic primary teeth.

An immunological assay for detection and enumeration of thermophilic biomining microorganisms.

A specific, fast, and sensitive nonradioactive immunobinding assay for the detection and enumeration of the moderate thermophile Thiobacillus caldus and the thermophilic archaeon Sulfolobus acidocaldarius was developed. It employs enhanced chemiluminescence or peroxidase-conjugated immunoglobulins in a dot or slot blotting system and is very convenient for monitoring thermophilic bioleaching microorganisms in effluents from industrial bioleaching processes.

Phosphate starvation affects the synthesis of outer membrane proteins in Thiobacillus ferrooxidans.

The outer membrane protein (omp40) component from the chemolithoautotrophic acidophilic Thiobacillus ferrooxidans is apparently regulated by the external pH and the concentration of phosphorus. Its amino-terminal sequence showed little identity with the Escherichia coli OmpC, OmpF or PhoE porins, but was 38.5% identical to the outer membrane channel-forming protein NosA from Pseudomonas stutzeri, whose expression is also regulated environmentally. In addition, the partial amino acid sequence of T. ferrooxidans omp40 showed between 34 and 38% identity with the amino-terminal end of the small outer membrane proteins Rck and PagC from Salmonella typhimurium and OmpX from Enterobacter cloacae.

Chemotaxis of Leptospirillum ferrooxidans and other acidophilic chemolithotrophs: comparison with the Escherichia coli chemosensory system.

Ni2+, Fe2+ and Cu2+ were attractants and aspartate was an apparent repellent for Leptospirillum ferrooxidans, a behaviour opposite to that for Escherichia coli. Membranes from L. ferrooxidans contained proteins with a molecular mass in the range of 80 kDa which were methylated in vitro. Methylation was stimulated in the presence of a membrane-free extract from E. coli, showing the response pattern expected for L. ferrooxidans, increased methylation by Ni2+, and demethylation by aspartate. This suggests the existence of sensory transducers having a common methylation domain with the E. coli methyl-accepting chemotaxis proteins. Total chromosomal DNA digests from L. ferrooxidans, Thiobacillus ferrooxidans and T. thiooxidans hybridized with probes containing different domains of the tar gene from E. coli, implying the presence of tar type genes in the acidophilic bacteria studied.

Effect of external pH perturbations on in vivo protein synthesis by the acidophilic bacterium Thiobacillus ferrooxidans.

The response of the obligate acidophilic bacterium Thiobacillus ferrooxidans to external pH changes is reported. When T. ferrooxidans cells grown at pH 1.5 were shifted to pH 3.5, there were several changes in the general protein synthesis pattern, including a large stimulation of the synthesis of a 36-kDa protein (p36). The apparent low isoelectric point of p36, its location in the membrane fraction, and its cross-reaction with anti-OmpC from Salmonella typhi suggested that it may be a porin whose expression is regulated by extracellular pH.

Methylation of proteins from the translational apparatus: an overview.

Several of the translational apparatus proteins are methylated in all kinds of organisms. Although most of the modified proteins play key roles during protein biosynthesis, the biological function of these chemical modifications still remains elusive. Our recent data indicate a highly conserved pattern of ribosomal protein methylation in eubacteria, with methylated proteins being both structurally and functionally homologous in several microorganisms. Chloroplast ribosomes also appear to have a rather eubacterial pattern of ribosomal protein methylation. On the other hand, there is an apparently ubiquitous methylation of some of the translational factors in several organisms. These findings suggest an important, albeit unknown role for the post-synthetic methylation of the translational machinery. The analysis of the sequences of known methylation target sites and the search of similar sites in other proteins of known sequence, allows to predict those ribosomal proteins or translational factors that may be subjected to post-translational modifications with one or more methyl groups. Although a definitive answer with respect to the biological role of these N-methylations is still missing, a direct correlation between the methylation of some proteins and their biological activity is just beginning to emerge.

Methylation of ribosomal proteins in bacteria: evidence of conserved modification of the eubacterial 50S subunit.

Methylation of the 50S ribosomal proteins from Bacillus stearothermophilus, Bacillus subtilis, Alteromonas espejiana, and Halobacterium cutirubrum was measured after the cells were grown in the presence of [1-14C]methionine or [methyl-3H]methionine or both. Two-dimensional polyacrylamide gel electrophoretic analysis revealed, in general, similar relative electrophoretic mobilities of the methylated proteins from each eubacterium studied. Proteins known to be structurally and functionally homologous in several microorganisms were all methylated. Thus, the following group of proteins, which appear to be involved in peptidyltransferase or in polyphenylalanine-synthesizing activity in B. stearothermophilus (P.E. Auron and S. R. Fahnestock, J. Biol. Chem. 256:10105-10110, 1981), were methylated (possible Escherichia coli methylated homologs are indicated in parentheses): BTL5(EL5), BTL6(EL3), BTL8(EL10), BTL11(EL11), BTL13(EL7L12) and BTL20b(EL16). In addition, the pentameric ribosomal complex BTL13 X BTL8, analogous to the complex EL7L12 X EL10 of E. coli, contained methylated proteins. Analysis of the methylated amino acids in the most heavily methylated proteins, BSL11 from B. subtilis and BTL11 from B. stearothermophilus, showed the presence of epsilon-N-trimethyllysine as the major methylated amino acid in both proteins, in agreement with known data for E. coli. In addition, BSL11 appeared to contain trimethylalanine, a characteristic, modified amino acid previously described only in EL11 from E. coli. These results and those previously obtained from other bacteria indicate a high degree of conservation for ribosomal protein methylation and suggest an important, albeit unknown, role for the modification of these components in eubacterial ribosomes.

Methylation of ribosomal proteins in Bacillus subtilis.

We measured the methylation of ribosomal proteins from the 30S and 50S subunits of Bacillus subtilis after growing the cells in the presence of [1-14C]methionine and [methyl-3H]methionine. Two-dimensional polyacrylamide gel electrophoretic analysis revealed a preferential methylation of the 50S ribosomal proteins. Proteins L11 and L16, and possibly L9, L10, L18, and L20, were methylated. On the other hand, only two possibly methylated proteins were found on the 30S subunit. A comparison of these results with those for Escherichia coli suggests a common methylation pattern for the bacterial ribosomal proteins.