Trauma score and the injury severity score. J Trauma 1987, 27:370–378.PubMedCrossRef 17. Rahbar E, Fox EE, del Junco DJ, Harvin JA, Holcomb JB, Wade CE, Schreiber MA, Rahbar MH, Bulger EM, Phelan

HA, Brasel KJ, Alarcon LH, Myers JG, Cohen MJ, Muskat P, Cotton BA, PROMMTT Study Group: Early resuscitation intensity as a surrogate for bleeding severity and early mortality in the PROMMTT study. J Trauma Acute Care CYT387 Surg 2013, 75:S16-S23.PubMedCrossRef 18. Zhang W-B, Li N, Wang P-F, Wang G-F, Li Y-S, Li J-S: Infections following damage control laparotomy with abdominal packing. Scand J Infect Dis 2008, 40:867–876.PubMedCrossRef 19. Miller RS, Morris JA, Diaz JJ, Herring MB, May AK: Complications after 344 damage-control open celiotomies. J Trauma 2005, 59:1365–1371. discussion 1371–4PubMedCrossRef 20. Kritayakirana K, Maggio PM, Brundage S, Purtill M-A, Staudenmayer K, Spain DA: Outcomes and complications of open abdomen

technique for managing non-trauma patients. J Emerg Trauma Shock 2010, 3:118–122.PubMedCentralPubMedCrossRef Competing interests Our co-authors report no personal conflicts of interest related to the study, and there was no funding from either the public or private sector related to the study. Authors’ contributions All authors have made substantive contributions to the study: Study conception and design: L-ML, S-HW, and C-YF. Acquisition of data: C-HL, I-MK, S-CK, and S-WC. Analysis and interpretation of data: S-YW,

C-HO, and Y-PH. Manuscript drafting: L-ML, S-HW, C-NY. Critical revision: S-HW and S-JY. All authors read and approved the final VX-680 manuscript.”
“Introduction Morel-Lavallee lesion (MLL) is a closed, soft-tissue degloving injury that is accompanied by disruption of Enzalutamide solubility dmso perforating vessels and lymphatics. It occurs as a result of blunt shearing or tangential forces that separate the mobile subcutaneous tissue from the immobile underlying fascia. In this disorder, hemolymphatic collection is formed in the closed space between the two detached layers [1, 2]. The diagnosis of MLL is routinely made based on clinical and radiological examination [3, 4]. In 1/3 of cases, there is a possibility that clinicians might fail to diagnose MLL due to its inconsistent clinical manifestations and because it often involves initial skin bruising due to underlying soft tissue injury [2, 5–7]. We present a case of delayed MLL arising from pelvic fracture caused by a motor vehicle accident. Based on the available literature, this case involves the youngest individual yet reported to suffer from delayed MLL. In addition, we provide a review of MLL and Cell Cycle inhibitor describe rare cases of the disorder in children. Presentation A 28-month-old child was presented to the department of emergency medicine of our medical institution following a traffic accident. The patient had no history of neonatal injury or developmental abnormality and had stable vital signs and no neurologic symptoms.

4 and 0.04 genome equivalent (ge) by reaction) of a known quantity of DNA extracted from four strains: M. avium, M. fortuitum, M. intracellulare and M. gordonae (identified from the national French reference laboratory collection). Specificity and sensitivity were estimated against 30 non-mycobacteria (negative) strains and 31 mycobacteria (positive), respectively. The collection contained reference and

environmental strains of mycobacteria, as well as, strains of the closely related CNM group, and other non-actinobacteria strains isolated from the environment [17]. Mycobacteria collection included MTC (n = 2) and leprae species (n = 1), as well as species of slow growing NTM (n = 13), and rapid growing NTM (n = 15). TaqMan® real-time PCR were performed in duplicate using an ABI7500 real-time PCR system (Applied

Biosystems), a Lifetech 7500 software version 2.0.6 (Applied Biosystems) and TaqMan JAK inhibitor fast virus 1-STEP Master Mix with 6-carboxy-X-rhodamine (ROX) (Applied Biosystems). The TaqMan® probes were labeled (Eurogentec) with the fluorescent dyes 6-carboxyfluorescein (5′ end) and Black Hole Quencher (3′ end). All reactions were performed in a 25 μl reaction mixture volume (2.5 μl of DNA) with 500 nM of forward primer, 500 nM of reverse primer, 50 nM of probe and 5 mM of MgCl2. Reverse transcriptase was inactivated immediately (95 °C, 45 s) according

to the manufacturer instruction, Selleck MG132 and real-time PCR consisted in 40 cycles of denaturation (95°C for 3 s), annealing and extension (both steps at 60°C for 30 s). Determinations of cycle threshold were performed by setting the instrument’s threshold line at 0.02 many ∆Rn units (fluorescence gain above the baseline divided by the ROX channel signal). Environmental analyses In order to compare the new real-time PCR method to the culture method, 26 tap water distribution points in Paris (France) were Palbociclib sampled between April 2011 and July 2011, corresponding to 90 samples. Briefly, one liter of tap water was sampled in sterile plastic bottle, then centrifuged at 5000 × g for 2h and finally re-suspended in 1 ml of water. Mycobacteria density was estimated by culture (Method A) in all these samples following the procedure previously described by Le Dantec et al. [28]. In parallel, DNA was extracted using two different methods: i) a bacterial DNA extraction kit (QIAamp DNA mini kit, Qiagen) according to the manufacturer recommendations (Method B), and ii) a phenol-chloroform extraction procedure according to Radomski et al. [29] (Method C). Extracted DNA was 10 fold diluted and mycobacteria density was estimated in duplicate using the new real-time PCR method. Using environmental samples, the new atpE targeting method was also compared a previously described rrs targeting method [17].

Within this framework, creatine supplementation in young, post puberty athletes Cell Cycle inhibitor can be considered a high quality type of “food” that can offer additional benefits to optimise training outcomes. Dosing protocols applied in creatine supplementation A typical creatine supplementation protocol consists of a loading phase of 20 g CM/d or 0.3 g CM/kg/d split into 4 daily intakes of 5 g each, followed by a maintenance phase of 3-5 g CM/d or 0.03 g CM/kg/d for the duration of the supplementation period [5]. Other supplementation protocols are also used such as a daily

single dose of around 3 – 6 g or between 0.03 to 0.1 g/kg/d [15, 55] however this method takes longer (between 21 to 28 days) to produce ergogenic effects [5]. Sale et al [56] found that a moderate protocol consisting of 20 g CM taken in 1g doses (evenly ingested

at 30-min intervals) for 5 days resulted find more in reduced urinary creatine and methylamine excretion, leading to an estimated increase in whole body retention of creatine (+13%) when compared with a typical loading supplementation protocol of 4 x 5 g/d during 5 days (evenly ingested at 3 hour intervals). This enhancement in creatine retention would lead to a significantly higher weight gain when people follow a moderate protocol AP24534 mouse ingestion of several doses of small amounts of CM evenly spread along the day. Responders vs. non-responders Syrotuik and Bell [57] investigated the physical characteristics of responder and non-responder subjects to creatine supplementation in recreationally resistance trained men with no history of CM usage. The supplement group was asked to ingest a loading dosage of 0.3 g/kg/d for 5 days. The physiological characteristics of responders were classified using Greenhaff et al [58] criterion of >20 mmol/kg dry weight increase in total intramuscular creatine and phosphocreatine and non responders as <10 mmol/kg dry

weight increase, a third group labeled quasi responders were also used to classify participants who fell in between the previously mentioned groups (10-20 mmol/kg dry weight). Overall, the supplemented group showed a mean increase in total resting muscle creatine ID-8 and phosphocreatine of 14.5% (from 111.12 ± 8.87 mmol/kg dry weight to 127.30 ± 9.69 mmol/kg dry weight) whilst the placebo group remained relatively unaffected (from 115.70 ± 14.99 mmol/kg dry weight to 111.74 ± 12.95 mmol/kg dry weight). However when looking at individual cases from the creatine group the results showed a variance in response. From the 11 males in the supplemented group, 3 participants were responders (mean increase of 29.5 mmol/kg dry weight or 27%), 5 quasi responders (mean increase of 14.9 mmol/kg dry weight or 13.6%) and 3 non-responders (mean increase of 5.1 mmol/kg dry weight or 4.8%).

The typical Ricolinostat device size was 2 × 2 μm. The high-resolution transmission electron microscopy (HRTEM) image taken inside the via-hole (Figure  2c) reveals the formation of two layers; one is TaOx and the other one is WOx, which is formed by the surface oxidation of the W BE because of the ex situ fabrication process. To confirm the thickness of the deposited TaOx layer, a HRTEM image was acquired from the area outside the via-hole, i.e., on the SiO2 (Figure  2b). The amorphous TaOx layer was approximately 9nm thick, confirming that the thickness of the polycrystalline WOx layer inside the

via-hole was approximately 5 nm (Figure  2c). This kind of bilayer structure (high-κ/WOx) was observed in all of the fabricated resistive memory stacks investigated (TEM images not shown here). Figure 1 AFM image of the W surface of an S1 device. The RMS surface roughness

is 1.18 nm. Figure 2 TEM and HRTEM images of IrO x /TaO x /W stack with via-hole structure and size of 2 × 2 μm. (a) TEM image. (b) HRTEM image outside of active region. The TaOx film is approximately 9 nm thick and amorphous. (c) HRTEM image in the active region. A WOx layer with a thickness of approximately 5 nm is formed inside the hole region. To obtain high-density memory, W films with a thickness approximately 100 nm were deposited on the SiO2 (200 nm)/Si substrates by sputtering to form IrOx/AlOx/W cross-point structures Galunisertib ic50 (Device: S2), which were patterned using photolithography and wet Adenosine see more etching techniques to form W BE stripes. Cross-point memory with different sizes ranging from 4 × 4 to 50 × 50 μm was fabricated by another

lithography step to pattern the TE stripes using a lift-off method. To obtain forming-free cross-point memory, the thickness of the AlOx layer was 7 nm. Figure  3a shows a typical optical microscope (OM) image of a fabricated resistive memory device with an IrOx/AlOx/W cross-point structure (Device: S2) with a size of 4 × 4 μm. The AlOx layer sandwiched between the IrOx TE and W BE is clearly seen in a cross-sectional HRTEM image of this device (Figure  3b). The surface of the W BE is rough. The energy-dispersive X-ray spectra shown in Figure  3c confirm that the respective layers contain Ir, Al, O, and W. To further examine the roughness and surface morphology of the W BE, an AFM image of the W BE surface was obtained, as shown Figure  4. The average and RMS surface roughness of the W BE were 1.05 and 1.35 nm, respectively, which are higher than those of the W BE in the devices with via-hole structures (S1, as shown in Figure  1). This morphological difference is also found to be important to improve the resistive switching behavior of cross-point memory devices, which will be discussed later. However, we first designed the via-hole PF devices (S1) and then the cross-point structure (S2) to improve memory characteristics.

Approximately 50-75 mg of muscle was obtained from the lateral portion of the vastus lateralis midway between the patella and iliac crest of the

leg using a 5-mm Bergstrom style biopsy needle. Muscle samples were taken on 3 separate occasions at each of the two resistance exercise 4SC-202 nmr sessions; 1) 30 min prior to exercise and ingestion of the supplement, 2) 15 min post-exercise, and 3) 120 min post-exercise. Participants were instructed to refrain from exercise 48 hr prior to each muscle biopsy. After removal, adipose tissue was trimmed from the muscle specimens and immediately frozen in liquid nitrogen and then check details stored at -80°C for later analysis. Serum IGF and insulin The concentrations of serum insulin and IGF-1 were determined in duplicate and the average concentrations reported using commercially available enzyme-linked immunoabsorbent assay (ELISA) kits (Diagnostic Systems Laboratories, Webster, TX; Biosource, Camarillo, CA). Standard Lenvatinib manufacturer curves were generated using specific control peptides. Concentrations were determined at an optical density of 450 nm with a microplate reader (Wallac

Victor 1420, Perkin Elmer, Boston, MA, USA). The overall intra-assay percent coefficient of variation was 4.6% and 2.9% for insulin and IGF-1, respectively. IRS-1 and Akt/mTOR signaling pathway protein expression Approximately 20 mg of each muscle sample was homogenized using a commercial cell extraction buffer (Biosource, Camarillo, CA, USA) and a tissue homogenizer. The cell extraction buffer was supplemented with

1 mM phenylmethanesulphonylfluoride (PMSF) and a protease inhibitor cocktail Non-specific serine/threonine protein kinase (Sigma Chemical Company, St. Louis, MO, USA) with broad specificity for the inhibition of serine, cysteine, and metallo-proteases. Muscle homogenates were analyzed for phosphorylated IRS-1 (Ser312), Akt (Ser473), 4E-BP1 (Thr46) and p70S6K (Thr389) using commercially-available phosphoELISA kits (Invitrogen, Carlsbad, CA, USA). This sensitivity of these particular assays is reported by the manufacturer to be less than 1 U⁄mL. The absorbances, which are directly proportional to the concentration in the samples, were determined at 450 nm with a microplate reader (Wallac Victor 1420, Perkin Elmer, Boston MA, USA). A set of standards of known concentrations for each phosphorylated muscle variable were utilized to construct standard curves by plotting the net absorbance values of the standards against their respective protein concentrations. By applying a four part parameter curve using MikroWin microplate data reduction software (Microtek Lab Systems, Germany), the concentrations in the muscle samples were appropriately calculated. Protein concentrations were expressed relative to muscle wet-weight. The overall intra-assay percent coefficient of variation for all assays was less than 7% Phosphorylated mTOR was assessed through the use of ELISA used by methods previously described [29].

Methods The multiwalled CNTs were grown at 700°C via a thermal chemical vapor deposition system under the acetylene, nitrogen, and hydrogen ambience. The as-grown CNTs were scraped off from the substrate, and then the derived 0.03-g CNTs were suspended in a mixture of concentrated H2SO4 (95%), HNO3 (70%), and deionized water for 15 min at 140°C to enhance the solubility of CNTs in the following solvents. The filtered CNTs were rinsed by deionized water to remove the acidic residues. Afterwards, these Selleck Lazertinib acid-treated CNTs were dissolved in a mixture of ethanol and ethylene PF-04929113 concentration glycol and then ultrasonicated in ice bath for 3 h. After centrifugalizing,

a homogeneous CNT solution with an approximate 0.5-mg/ml concentration of CNTs was sprayed onto glass substrates (Eagle 2000, Corning Display Technologies Taiwan Co., Ltd, Taipei, Taiwan) at 200°C to form the CNTFs. The thickness of CNTF could be adjusted by varying the spray times, and therefore, the 110-nm-thick and 230-nm-thick CNTFs on the glass substrates were obtained, respectively. Subsequently, two glass substrates, one was deposited with CNTF and the other was a bare glass substrate, were face-to-face compressed with a force of 100 N. The thermal

compression temperature was varied from room temperature to 400°C, and the compression duration changed from 0 to 50 min. Results and discussion The field emission scanning electron microscopy (FE-SEM) images of the morphological variations see more for the as-sprayed CNTF and thermally compressed ones are shown in Figure 1. The CNTs in the as-sprayed CNTF can be recognized individually and distributed arbitrarily with the wire shape, as exhibited in Figure 1a.

After the thermal compression with the compression force of 100 N at 200°C for 50 min, the neighbor CNTs seem to be intertwined with each other and each CNT is hard to be distinguished, as shown in Figure 1b. Once the compression temperature SDHB reaches to 400°C, the wire-shaped CNTs no longer exist and the CNTs merge into a continuous film, as shown in Figure 1c. Moreover, from the color contrast in Figure 1c, the surface of CNTF compressed at 400°C becomes much smoother than others. To further realize the effect of the thermal compression on the structure of CNT, the high-resolution transmission electron microscopy (TEM) is executed to analyze the as-sprayed CNTs and thermally compressed ones. For the as-sprayed CNTs shown in Figure 2a, two stacked CNTs are exhibited with the regular and coaxial multiwalled structures, as indicated by the dashed lines. Furthermore, it is easy to distinguish each wall structure even though one CNT stacks on the other.

Interestingly, the closest variants to the homB predominant check details allele AI were the selleck chemicals llc rarest variants AV and AVI, all three exclusive of homB gene. The closest variants to the homA predominant allele AII were AIII and

AIV (data not shown). Concerning the most prevalent homB and homA allele types, no geographical predominance of any allele was observed, and no correlation was found between any allelic variant and gastric disease as well (data not shown). In order to test the in vivo expression of homB and homA allelic variants, human sera were tested with a recombinant purified HomB protein, allele type AI [9]. All sera (n = 24) showed an immunoreaction against this protein, suggesting that all homB and homA allelic variants are expressed during infection and are antigenic in humans. However, it should be noted that only one serum could be tested for the rarest allelic variants, AIII, AIV, AV and AVI. Discussion In the present study, the distribution and diversity of two putative H. pylori OMP-coding genes, homB and homA, was evaluated in clinical strains with different geographical origins. Both genes displayed a varied worldwide distribution, with a marked difference between East Asian and Western countries, in accordance with other studies reporting such differences in the frequency of H. pylori virulence factors [16–19]. At least one copy of either homB

or homA genes was found to be present in the genome of the H. pylori strains suggesting that these OMP-coding genes are under selective BMS202 cell line pressure to be maintained in the bacterium,

as was reported for other H. pylori OMP-coding genes such as babA/babB, sabA and (-)-p-Bromotetramisole Oxalate oipA [5–7]. Analysis of homB and homA genes revealed diversity regarding the number of copies and their genomic localization, regardless of the clinical origin of the strain, but with geographical specificity. Both the homB/homA single-copy and the double-copy genotypes were observed in Western strains while the East Asian strains presented the single-copy genotype only, suggesting that, if gene duplication had occurred, it did not seem to be a random event. Variation in copy number of OMP-encoding genes can help the bacterium adapting to a particular host, which is essential to promote a chronic infection [5, 11, 20]. The fact that homB and homA genes display a high level of similarity, especially at the 5′and 3′ ends, suggests that intra or intergenomic recombination events can occur, leading to gene duplication, deletion or homB/homA conversion, as a response to environmental changes. The presence of an intergenic region at the empty locus with high identity with both homB and homA suggests that the gene was lost, leaving short remnant sequences which will enable the gene to be integrated again by genomic recombination, in response to environmental changes, as has been hypothesized for other H.

The regulation of transcription, which maybe also affects the expression of VCA0518 in the sorbitol fast-fermenting and slow-fermenting strains, should also be considered MtlD catalyses the transformation of selleck inhibitor mannitol-1-P to fructose-6-P, the later enters

the fructose metabolism pathway. Mannitol and sorbitol are very similar in molecular structure. In Pseudomonas fluorescens, sorbitol is transported by the mannitol PTS system and transformed by polyol dehydrogenase, A-769662 concentration which has a broad substrate spectrum [14, 15]. In a previous study we confirmed the transcriptions of the N16961 VCA1046 gene in sorbitol and mannitol fermentation media [16]. Here, our results indicate that two non-sorbitol specific PTSs are involved in the V. cholerae sorbitol utilization process. This may be similar to the uptake of L-sorbose in Lactobacillus casei where L-sorbose RepSox is mainly taken up via EIISor and EIIMan plays a secondary role [17]. In Bacillus subtilis, MtlD is required for sorbitol assimilation in addition to the gut operon [18]. Interestingly, both of these PTSs are located on chromosome II of V. cholerae. Several studies indicate that the two chromosomes of V. cholerae are heterologous and that chromosome II may be a megaplasmid captured by an ancestral V. cholerae [7]. The ability to ferment sorbitol used to learn more differentiate V.

cholerae strains may provide clues as to both the origins and genetic variation of the toxigenic and nontoxigenic strains. The traditional sorbitol fermentation test is a phenotypic method using phenol red as the indicator. In our study, we showed that the observed differences in sorbitol fermentation rates were the

result of changes in the production rate of formate in the fast-fermenting and slow-fermenting strains. The fact that the ratio of formate to acetic acid was not consistent between the two strains also indicated that, besides the differences early in the metabolic pathway (including the transportation and transformation of sorbitol), pyruvate catabolism could be different in sorbitol fermentation in the toxigenic and nontoxigenic strains. Both pyruvate dehydrogenase and PFL can catalyze the transformation of pyruvate to acetyl-CoA, but they have different electron acceptors and outputs. Their activities affect the relative proportion of the end products [19]. Pyruvate dehydrogenase produces CO2 in addition to acetyl-CoA, while formate is the product of PFL. In the proteomic and qRT-PCR analyses of this study, the respective expression and transcription levels of these two genes were significantly different in the fast-fermenting JS32 and slow-fermenting N16961. Consistent with this fact was that formate was produced earlier in JS32 than in N16961.

These

were P. aeruginosa (PAO1, PA14, PA7 and LESB58), P. fluorescens (Pf0-1, Pf-5 and SBW25), P. putida (KT2440, F1 and W619) and P. syringae (B728a and DC3000). It was reasoned that if a gene is under direct Crc control, the binding site should be present in that gene in all representatives of a particular species. Accordingly, only genes with the A-rich motif (AAnAAnAA) in the upstream region of intraspecies orthologs for all strains of a given species were considered as candidates (Additional file 1). In total, 421 candidate TEW-7197 genes were identified, with an estimated false discovery rate of 27% (see materials and methods). P. aeruginosa has the highest number (215) of Crc candidates, P. syringae and P. putida had 143 and 133, respectively while P. fluorescens has the lowest number (84) (Figure 1). This difference in the number of possible CRC-AZD6094 solubility dmso regulated genes is likely to be a consequence of the taxonomic organisation within the genus, in particular the JNK-IN-8 nmr diversity of P. fluorescens species. A consequence of this diversity is that the core genome of P. fluorescens is significantly smaller than that of P. aeruginosa

and so the pool of orthologous genes that are potentially regulated by Crc is lower [41–45]. Twelve Crc candidates are common to all four Pseudomonas species while a further 28 Crc candidates are present in three out of the four species BCKDHA examined (Figure 1). Taken together, these 40 Crc candidates represent the predicted core Crc regulon of Pseudomonas (Table 1). Many

of these Crc candidates are annotated as having roles in nutrient transport and metabolism, fitting with the idea of CRC as a means of controlling hierarchical assimilation of nutrients from the environment. Most putative Crc targets are not part of the core regulon and are confined to a single or two species. These include the three Crc target genes (alkS, benR of P. putida and amiE of P. aeruginosa) that have been experimentally shown to bind Crc in the 5′ region of the mRNA [17, 18, 33]. No orthologues of benR or amiE were detected outside of P. putida or P. aeruginosa species, respectively, and so these are species-specific targets. The absence of alkS in our dataset is due to its location on a mobile element (the P. putida OCT plasmid) that is only present in some strains of P. putida. In summation, the Pseudomonas regulatory network controlled by Crc ranges from genes that are regulated at a genus-wide level, down to genes that may only be regulated in certain strains within a particular species. Figure 1 Interspecific variations of the Crc regulon. Venn diagram showing a four way comparison of Crc candidates in P. aeruginosa, P. fluorescens, P. putida and P. syringae.

This observation is consistent with the oberserved low level expression of other stress responses [14,

16]. There was no significant difference in the growth rate or physical characteristics, such as clumping or pigmentation between M. smegmatis and M. tuberculosis strains expressing ssd and control strains. The primary distinguishing physical feature between the M. smegmatis and M. tuberculosis ssd expressing merodiploid strains in comparison to control bacteria was increased cell lengths and a smooth ultrastructural characteristic (Figure 2ABCD). The observed smooth ultrastructure devoid of concentric rings along the bacterial filament is important because this observation is consistent with inhibition of FtsZ polymerization and Z-ring formation as Temozolomide molecular weight previously reported [6, 7, 17, 18]. The M. smegmatis wild type control strain exhibited cell lengths of 2.1 check details ± 0.11 μm (Figure 2AF) and the M. smegmatis

ssd merodiploid strain had increased cell lengths of 3.2 ± 0.42 μm (Figure 2BF). Similarly, M. tuberculosis H37Rv control cells had lengths of 1.73 ± 0.43 μm (Figure 2CF) and expression of ssd resulted in increased cell lengths of 2.53 ± 0.76 Apoptosis inhibitor μm (Figure 2DF). In contrast, a ssd::Tn M. tuberculosis mutant strain had decreased cell lengths of 1.35 ± 0.51 μm (Figure 2EF). This experimental data demonstrates a causal relationship between the expression levels of ssd and altered bacterial cell lengths, confirming the bioinformatics analysis and further substantiating Ssd as a septum regulation protein as annotated (http://​genolist.​pasteur.​fr/​TubercuList[19]) and indicated by transcriptional mapping [6]. Figure 2 Ultrastructure Analysis (SEM) and Length distributions. Bacterial morphology.

(A) M. smegmatis control strain, (B) M. smegmatis ssd merodiploid (C) M. tuberculosis control, (D) M. tuberculosis ssd merodiploid and (E) ssd::Tn mutant M. tuberculosis strain were visualized by scanning electron microscopy. Images are representative of different fields of bacteria from exponentially growing cultures at 37°C. (F) Lengths of the bacterial cells were calculated from the coordinates of Carnitine palmitoyltransferase II both ends of the cell as measured from representative fields as visualized by scanning electron microscopy. Multiple fields were examined and values calculated in 0.5-1 mm increments from multiple fields of over 100 cells. Whole-genome expression profiling of ssd merodiploid and mutant strains To assess the effect of ssd expression on M. tuberculosis metabolism, global gene expression profiling was performed on the ssd overexpression M. tuberculosis merodiploid strain. A total of 2,274 ORFs were transcriptionally active with 432 of these ORFs being differentially expressed 1.5-fold or greater change (p values ≤ 0.05).