6%), and 30 following the return to France (attack rate of 5.2%). The following results only concern the 30 imported cases, which occurred between February 13 and May 14, 2006 (Figure 1). The median interval between return date and diagnosis was 21 days (range = 0–88d). Twenty of the episodes (66.6%) occurred within 4 weeks after returning home. Mean age of the cases was 28 years (range = 21–45 y). A large majority of these imported cases

was due to P. falciparum (83.3%). Other cases were due to Plasmodium ovale (two cases), Plasmodium Malariae (two cases), and Plasmodium Vivax (one case). No case with co-parasitism was observed. The average interval between onset of symptoms and the initial consultation was 3.5 days and reached 10 days for two subjects. Three subjects presented a serious form according to World Health Organization Antiinfection Compound Library in vitro criteria.1 The episode with

the most serious complications involved a man aged 30 who had been Venetoclax presented a cerebral malaria 18 days after return, and had been developed sequelae with poor prognosis. Exposure to the risk of developing a malaria episode was estimated at 2,012 person-months (PM) (575 × 3.5 mo) in Ivory Coast and at 575 PM after returning home, or a total of 2,587 PM. Incidence rate was 4.5 per 1,000 PM during the period spent in Ivory Coast and 34.8 per 1,000 PM during the month following the return. Post-return incidence rate was particularly higher among subjects who served in the Man–Danane–Daloa triangle (65.8 per 1,000 PM vs 28.6 in Abidjan and 24.0 in Bouake). Therefore,

the risk of malaria episode during the month following the return was higher than during the period spent in Ivory Coast [hazard ratio (HR) = 7.7, P < 10−5], and particularly among subjects who had been served in the Man–Danane–Daloa triangle (HR = 14.6, p < 10−5). Hence, these soldiers seemed to be particularly exposed to risk due to some field missions conducted in January and February, Leukocyte receptor tyrosine kinase during which prophylactic measures appeared to had been insufficiently applied (some nights without net, lack of supervision of chemoprophylaxis) given the operational context. The two last months of stay in Ivory Coast were yet marked by low rainfall. According to the data on the declaration forms, 55% (11/20) of subjects who developed a malaria episode during the first 4 weeks following return at home admitted to not having taken their chemoprophylaxis regularly (forgotten more than once) in the 8 days preceding diagnosis; that is, the minimal incubation period of malaria. Information concerning compliance with vector control measures in the operation theater was available for 20 subjects: 95% had used insecticide-treated combat uniforms, 85% had used bed nets, and 60% had used skin repellents. This investigation raised the clear predominance of P.

However, unlike Gsp and Exe, a pilotin, OutS, is required for secretion (Condemine et al., 1992), as well as stability and efficient outer membrane localization of OutD (Shevchik et al., 1997; Shevchik & Condemine, 1998). selleck Shigella flexneri MxiD similarly requires both a pilotin, MxiM, and accessory protein, MxiJ. However, MxiJ has no sequence similarity to GspB. Expression of either MxiM or MxiJ prevents MxiD from degradation (Schuch & Maurelli, 2001). Secretins in Class 4 are able to reach the outer membrane but are unable to form stable assemblies in the absence of their accessory proteins. BfpB from E. coli T4bP falls into this

category, as multimers of BfpB cannot form without BfpG (Schmidt et al., 2001). Despite being part of a T4bP system, TcpC in V. cholerae behaves differently. TcpC and its accessory protein, TcpQ, are mutually stabilizing, and each is completely degraded in the absence of the other (Bose & Taylor, 2005). Another example of a Class 4 secretin is PilQ from N. meningitidis T4aP. In the absence of PilW, PilQ remains monomeric in the outer membrane – or does not form stable multimers – and does not support T4P activity (Carbonnelle

et al., 2005). The inner membrane protein PilP has been reported to affect PilQ stability in Neisseria, but published results are inconsistent (Drake et al., 1997; Carbonnelle et al., 2005, 2006; Balasingham et al., 2007). Pilotins are required for both proper localization and assembly of Class learn more 5 secretins. PilQ in P. aeruginosa, unlike its homolog in N. meningitidis, is retained in the inner membrane without the PilF pilotin (Koo et al., 2008). Untethering of PilF from the membrane by mutation of its lipidation site causes PilQ assembly in both membranes and shows that secretin assembly mediated by PilF is a separate function from localization. Given the variation in the requirements for secretin assembly, the mode of interaction between pilotins and accessory proteins with their cognate secretin has Branched chain aminotransferase been the focus of much study. Biophysical techniques and functional characterization of mutants have begun

to pinpoint the region(s) of the secretin subunit involved and the stoichiometry of the interaction. The majority of pilotins have been found to interact with the C-terminus of the secretin subunit, whereas accessory proteins bind in the N-terminal region. Protein chimeras between secretin C-termini and several different proteins have been used to show an interaction between the secretin and pilotin. Attachment of the C-terminal 65 amino acids of PulD or 43 amino acids of InvG to the filamentous phage protein pIV rendered the chimeras dependent on the pilotins, PulS and InvH, respectively, for phage assembly and allowed the chimera–pilotin complex to be co-immunoprecipitated (Daefler et al., 1997; Daefler & Russel, 1998).

However, unlike Gsp and Exe, a pilotin, OutS, is required for secretion (Condemine et al., 1992), as well as stability and efficient outer membrane localization of OutD (Shevchik et al., 1997; Shevchik & Condemine, 1998). Selleck HDAC inhibitor Shigella flexneri MxiD similarly requires both a pilotin, MxiM, and accessory protein, MxiJ. However, MxiJ has no sequence similarity to GspB. Expression of either MxiM or MxiJ prevents MxiD from degradation (Schuch & Maurelli, 2001). Secretins in Class 4 are able to reach the outer membrane but are unable to form stable assemblies in the absence of their accessory proteins. BfpB from E. coli T4bP falls into this

category, as multimers of BfpB cannot form without BfpG (Schmidt et al., 2001). Despite being part of a T4bP system, TcpC in V. cholerae behaves differently. TcpC and its accessory protein, TcpQ, are mutually stabilizing, and each is completely degraded in the absence of the other (Bose & Taylor, 2005). Another example of a Class 4 secretin is PilQ from N. meningitidis T4aP. In the absence of PilW, PilQ remains monomeric in the outer membrane – or does not form stable multimers – and does not support T4P activity (Carbonnelle

et al., 2005). The inner membrane protein PilP has been reported to affect PilQ stability in Neisseria, but published results are inconsistent (Drake et al., 1997; Carbonnelle et al., 2005, 2006; Balasingham et al., 2007). Pilotins are required for both proper localization and assembly of Class http://www.selleckchem.com/products/erastin.html 5 secretins. PilQ in P. aeruginosa, unlike its homolog in N. meningitidis, is retained in the inner membrane without the PilF pilotin (Koo et al., 2008). Untethering of PilF from the membrane by mutation of its lipidation site causes PilQ assembly in both membranes and shows that secretin assembly mediated by PilF is a separate function from localization. Given the variation in the requirements for secretin assembly, the mode of interaction between pilotins and accessory proteins with their cognate secretin has from been the focus of much study. Biophysical techniques and functional characterization of mutants have begun

to pinpoint the region(s) of the secretin subunit involved and the stoichiometry of the interaction. The majority of pilotins have been found to interact with the C-terminus of the secretin subunit, whereas accessory proteins bind in the N-terminal region. Protein chimeras between secretin C-termini and several different proteins have been used to show an interaction between the secretin and pilotin. Attachment of the C-terminal 65 amino acids of PulD or 43 amino acids of InvG to the filamentous phage protein pIV rendered the chimeras dependent on the pilotins, PulS and InvH, respectively, for phage assembly and allowed the chimera–pilotin complex to be co-immunoprecipitated (Daefler et al., 1997; Daefler & Russel, 1998).

Finally, it is interesting to notice that of the five identified stress-related

heat shock proteins, GroES, GroEL1, GroEL2, grpE and DnaK2, only GroES is differentially more abundant (Fig. 2d). As GroES interacts with GroEL to form a complex, which assists in correcting misfolded proteins, this result is surprising, particularly when compared with MED4 subjected to high light Stress, whereby both GroES and GroEL12 proteins were more abundant (Pandhal et al., 2007). Another protein identified as being stress response related, a histone-like DNA-binding protein (PMM1321), was more abundant in the P-stressed phenotype (Fig. 2e). These proteins are known to wrap DNA and stabilize it from denaturation under extreme environmental conditions (Pettijohn, 1988). Indeed, a homologue of this protein (HU) was more abundant in Synechocystis sp. PCC6803 under P-deplete Romidepsin concentration conditions (Gan, 2006), but surprisingly, was not observed in MED4 under light stress (Pandhal et al., 2007). This observation suggests specificity in stress response for this protein, possibly nutrient starvation; however, a more detailed examination of the overall stress responses within this organism is required. It is clear that MED4 acclimates to long-term P starvation through activating and also suppressing a wide range of cellular processes. Important Selleckchem Sorafenib metabolic mechanisms such as glycolysis are depressed, while other systems, most notably P-acquisition

mechanisms, are considerably elevated. Photosynthesis and carbon fixation are reduced, while the structures of the photosystems are reinforced. This, in particular, is an indication of the stressed cell reducing its metabolic activities while simultaneously maintaining cellular integrity. Specific Thymidylate synthase amino acid biosynthesis mechanisms are either reinforced or reduced. This may be an indication of individual amino acid requirements, which could well be linked to intracellular recycling efficiency and/or specificity. Indeed, translation, indicated through ribosome levels, appears

to be increased, indicating an active, ongoing response. Specific chaperonins and protein-folding proteins, particularly membrane-associated ones, are more abundant, while DNA integrity is reinforced. Interestingly, there does appear to be a specificity of the stress response to P starvation, whereby under conditions of nitrogen deprivation, ribosomal genes as well as the carboxysome shell protein genes csoS12 and photosystem genes were all repressed, whereas Rubisco is repressed under both N starvation (Tolonen et al., 2006) and P starvation (this study). However, the response to N deprivation was measured over a 48-h period and may not reflect longer term acclimation. The environmental conditions that MED4 are exposed to in situ are considered to be consistent and unchanging; however, these results appear to suggest that MED4 exhibits a capability to withstand long periods of P starvation and recover.

[43] While a number of pharmacists

expressed negative personal attitudes towards CPD, the majority of the research participants within the various studies seemed beset by the compound interaction of barriers apparently outside of their control, such as time and resource issues. A number of theories have been developed to examine the process by which people attribute behaviour (including their own) to internal or external causes and there is now a large body of Ixazomib evidence showing that people’s judgements about the causes of behaviour are not completely rational but biased.[44] A common observation is that people attribute successes internally, as within their control, whereas failures are attributed externally to others or to the circumstances, www.selleckchem.com/products/PLX-4720.html a concept captured by the term ‘self-serving attribution bias’.[44] A self-serving bias is therefore said to exist where an individual’s assignment of responsibility affects his or her beliefs in an optimistic way, a way that

makes things appear better than they are from the individual’s point of view. We believe there may be an element of self-serving attribution bias at play in terms of pharmacy professionals’ stated barriers to CPD. That is, pharmacy professionals’ own explanations for lack of participation in CPD could stem from their erroneous perception that it is mainly factors external to their control that pose the real barriers, and that ultimately external factors are helping to drive participation in CPD. This would indicate that making CPD a statutory requirement could compel pharmacy professionals to engage with the process at some level, and indeed the personal correspondence referred to above seems to indicate the same. Nonetheless, if CPD is to RANTES be truly successful and useful for revalidation, it seems that people’s beliefs and attitudes must be addressed through the modification

of the various other external barriers perceived to be impacting on CPD behaviour. The implications of the current findings can be considered as follows. If CPD is to succeed and be useful as part of revalidation, pharmacy professionals’ beliefs and attitudes must be addressed by recognising and modifying barriers through a combination of four main categories of regulatory, professional, work-related and personal channels (see Figure 2). We believe it is possible to draw on the current findings to suggest a number of remedial steps in relation to these categories so as to ultimately impact on pharmacy professionals’ personal motivations and therefore participation in CPD.

e., Escherichia coli) (Blattner et al., 1997; Dippel & Boos, 2005). Based on the sequence

annotation, the genetic information encoded on pPag3 corresponds with the previously described phenotypic characteristics of nonpigmented variants http://www.selleckchem.com/products/KU-60019.html of P. agglomerans (i.e., thiamine deficiency, lack of maltose utilization, no pigmentation) (Chatterjee & Gibbins, 1971; Gantotti & Beer, 1982; Lindh et al., 1991), indicating that the plasmids in both species likely have similar features. In addition, when multiplying the size of pPag3 (530 kb) with the average molecular weight of a base pair (660 Da), the molecular weight of pPag3 obtained is in agreement with the observed 350 MDa plasmid reported from P. agglomerans (ex E. herbicola) Eh112Y (Gantotti & Beer, 1982). A nonpigmented variant of P. vagans C9-1, designated C9-1W, was obtained (Fig. 1). The identity of C9-1W as a derivative rather than as a contaminant was confirmed with 100%gyrB sequence identity compared with C9-1. The distinctive white colony color is attributable to loss

of the carotenoid biosynthetic gene cluster located on pPag3. Genotyping with multiple primer pairs targeting parts of the three plasmids in P. vagans C9-1 mTOR inhibitor confirmed the absence of pPag3 and the presence of pPag1 and pPag2. The plasmid sequence data identified a thiamine biosynthetic cluster (thiOSGF). Whether these are required for thiamine biosynthesis was unclear because several other genes (thiBCDEIJKLMPQ) known from pathways in prokaryotes (Begley et al., 1999; Settembre et al., 2003) are found scattered on the P. vagans C9-1 chromosome (Smits et al., 2009). When tested

on glucose-amended minimal media, C9-1W only grew with a thiamine supplement. This confirms that plasmid-borne Florfenicol thiOSGF are essential for thiamine autotrophy in P. vagans C9-1, and may explain thiamine auxotrophy reported for the nonpigmented variant, plasmid-cured P. agglomerans (Chatterjee & Gibbins, 1971; Gantotti & Beer, 1982). Substitution of glucose with maltose in the minimal medium resulted in no growth regardless of the presence/absence of thiamine. This further demonstrates that maltose utilization (Dippel & Boos, 2005) is conferred by genes located on pPag3 (Pvag_pPag30206–Pvag_pPag30215). When P. vagans C9-1W was grown with sucrose or sorbitol as the sole carbon sources, thiamine was again found to be the critical parameter for growth. This confirms the thiamine auxotrophy of P. vagans C9-1W, and also the retention of pPag1 (containing sucrose metabolic genes) and pPag2 (containing sorbitol metabolic genes) in the variant. Plasmid pPag3 also contains two genes with high sequence identity to a β-lactamase bla and its cognate regulator ampR (Pvag_pPag30395–Pvag_pPag30396). Ampicillin resistance has been reported to occur commonly in P. agglomerans clinical isolates (Cruz et al., 2007). Unlike the wild-type strain P.

Thus, SgII is present in LDCV and non-LDCV compartments of various neural cells. The wide subcellular Ganetespib cost localization of SgII may reflect diverse release sites of neuropeptides and secretorneurin, or suggests its role in the sorting and packaging of molecules other than neuropeptides in non-LDCV compartments. “
“Neurons in the visual cortex

exhibit heterogeneity in feature selectivity and the tendency to generate action potentials synchronously with other nearby neurons. By examining visual responses from cat area 17 we found that, during gamma oscillations, there was a positive correlation between each unit’s sharpness of orientation tuning, strength of oscillations, and propensity towards synchronisation with other units. Using a computational

Epacadostat model, we demonstrated that heterogeneity in the strength of rhythmic inhibitory inputs can account for the correlations between these three properties. Neurons subject to strong inhibition tend to oscillate strongly in response to both optimal and suboptimal stimuli and synchronise promiscuously with other neurons, even if they have different orientation preferences. Moreover, these strongly inhibited neurons can exhibit sharp orientation selectivity provided that the inhibition they receive is broadly tuned relative to their excitatory inputs. These results predict that the strength and orientation tuning of synaptic inhibition are heterogeneous across area 17 neurons, which could have important implications for these neurons’ sensory processing capabilities. Furthermore, although our experimental recordings were conducted in the visual cortex, our model and simulation results can apply more generally to any brain region with analogous neuron types in which heterogeneity in the strength of rhythmic

inhibition can arise during gamma oscillations. Branched chain aminotransferase “
“Hypoglossal motoneurons (HMs) are known to be under ‘permanent’ bicuculline-sensitive inhibition and to show ‘transient’ synaptic γ-aminobutyric acid (GABA)A and glycine inhibitory responses. The present paper describes a permanent bicuculline-sensitive current that should contribute to their tonic inhibition. This current was recorded in brainstem slices superfused without any exogenous agonist and remained detectable with tetrodotoxin. It could also be blocked by the other GABAA antagonists picrotoxin (PTX) and 2-(3-carboxypropyl)-3-amino-6-(4 methoxyphenyl)pyridazinium bromide) (SR95531; gabazine), but persisted in the presence of a specific blocker of α5-containing GABAA receptors. Addition of 2 μm 4,5,6,7-tetrahydroisoxazolo[5,4-c]pyridin-3-ol hydrochloride (THIP), known to preferentially activate GABAA receptors devoid of a γ-subunit, induced a sustained anionic current that could be further enhanced by neurosteroids such as allopregnanolone (100 nm).

Through neuronal apoptosis induction by shifting mature cerebellar granule neurons to low-potassium medium, we have demonstrated that nuclear liver activator protein 1 expression decreases and its phosphorylation disappears, whereas liver inhibitory protein levels

increase in the nuclear fraction, suggesting a pro-survival role for liver activator protein transcriptional activation and a pro-apoptotic role for liver inhibitory protein transcriptional inhibition. To confirm this, we transfected cerebellar granule neurons with plasmids expressing CFTR activator liver activator protein 1, liver activator protein 2, or liver inhibitory protein respectively, and observed that both liver activator proteins, which increase PARP activity CCAAT-dependent transcription, but not liver inhibitory protein, counteracted apoptosis, thus demonstrating the pro-survival role of liver activator proteins. These data significantly improve our current understanding of the role of CCAAT enhancer-binding protein β in neuronal survival/apoptosis. CCAAT enhancer binding protein

(C/EBP) β belongs to a transcription factor family (C/EBP α–ζ) whose members contain a basic leucine-zipper domain for DNA binding and dimerization (Nerlov, 2008). Homodimeric and heterodimeric interactions occur among members of this family. C/EBP β exists in three isoforms generated from a single mRNA by leaky ribosome scanning: 38-kDa liver activator protein (LAP) 1 (LAP1), 35-kDa LAP2, and 21-kDa liver inhibitory protein (LIP). LAP1 and LAP2 contain both the transactivation and basic leucine-zipper domains, whereas LIP lacks the transactivation domain and forms non-functional heterodimers with LAP1 and LAP2 (Descombes

& Schibler, 1991; Ossipow et al., 1993). These transcription factors undergo post-translational modifications such as phosphorylation and sumoylation, as well Epothilone B (EPO906, Patupilone) as subcellular translocation, which regulate transcriptional function (Nerlov, 2008; Kowenz-Leutz et al., 2010). C/EBPs have been extensively studied, owing to their importance in several cellular processes and in various diseases, including cancer. C/EBP β has multiple roles: it may inhibit or promote cell proliferation or differentiation, as well as survival or apoptosis, depending on the cell context and expressed isoforms (Sebastian & Johnson, 2006; Nerlov, 2007; Li et al., 2008; Ramathal et al., 2010). In the liver, LAP arrests cell cycle progression, whereas LIP induces hepatocyte proliferation (Buck et al., 1994). Moreover, LAP Thr217 phosphorylation in the mouse protein (Ser105 in rat) is required for hepatocyte proliferation and blocks apoptosis, determining cell survival (Buck et al., 1999, 2001; Buck & Chojkier, 2003). Furthermore, the LAP/LIP ratio is critical in C/EBP β-mediated gene transcription, and modulates the cell response to endoplasmic reticulum (ER) stress (Li et al., 2008).

(2009). Participants performed one block of 60 trials, comprising 40 ‘money trials’ and 20 ‘blank trials’, presented in randomized order. Money trials included 20 repetitions of a $5 bill and 20 repetitions of a 10 cents coin. Each trial began with a cue (a picture of a $5 bill or a 10 cents coin within a white rectangle; or an empty rectangle for blank trials) for 2 s, followed by a blank screen for 1 s (Fig. 2A). TMS was delivered

at only one time-point – this was 500 ms before the choice screen (like the ‘late’ period of Experiment 1). This was motivated by the finding in Experiment 1 (see below) that this time-point was the optimal one for eliciting an effect. After this, a choice screen appeared (as for Experiment 1) learn more and the participant selected the response. Some trials included a yellow border around the white rectangle during money stimulus presentation; on these trials, the participant was required

to say ‘yellow’ (see Experiment 2b below). Participants were informed that, at the end of the experiment, one of the money trials would be randomly selected and honored (i.e. participants get the money if they selected Yes). Participants were instructed to select Yes on both types of find more money trials (optimal choice for participants), as well as on the blank trials. Having the same response on all three types of trials ensured that any resulting differences in motor-evoked Rho potentials (MEPs) across these trials were dependent only on the monetary value of the trials, and not independently driven by differences in the required responses. The task structure was similar to

Experiment 2a (Fig. 2A), the only differences being that the choice screen was not presented and the participants did not have to move their fingers to press keys. To minimize the possibility of participants not paying attention to the screen (as no hand responses were required in this experiment), each trial included, with a 10% probability, a yellow border on the white rectangle containing the money cue. On these trials, the participants had to say the word ‘yellow’ as soon as they saw the border; they were instructed that failure to do so more than once would result in the cancellation of any monetary rewards they might otherwise receive from the experiment. To keep Experiments 2a and 2b similar, this additional feature and requirement was also included in Experiment 2a. Note that Experiment 2b did not have any manual response requirement. The only motor requirement was to report the occurrence of the yellow border on the 10% of trials in which this occurred. Participants were seated 50 cm in front of an iMac (19-inch monitor). The experiments were run using Matlab (MathWorks, Natick, MA, USA) and the PsychToolBox3 (http://www.psychtoolbox.org).

5%), followed by Lutibacter maritimus (94.4%), Aestuariicola saemankumensis (92.5%), Lutimonas vermicola (92.2%) and

Actibacter sediminis (92.1%). The 16S rRNA gene sequence Dabrafenib manufacturer analyses indicated that strain JC2131T belonged to the family Flavobacteriaceae, phylum Bacteroidetes. This was confirmed by the phylogenetic tree (Fig. 1) that showed that strain JC2131T formed a monophyletic clade distantly associated with the aforementioned genera. Strain JC2131T was rod-shaped (0.8–1.0 μm wide and 2.4–3.0 μm long) and devoid of flagellar and gliding motility. Colonies on MA were circular with regular margins, smooth, convex and amber-pigmented. Growth occurred at 5–50 °C (optimum, 35 °C), at pH 5–8 (optimum, pH 6) and in the presence of 1–20% sea salts (optimum, 3%). Growth did not occur on R2A medium selleck kinase inhibitor in the absence of sea salts. The DNA G+C content of strain JC2131T was 43.7 mol%, which was significantly higher than those of the genus Lutibacter (33.9–34.6 mol%). Other biochemical and physiological properties are presented in Table 1 and in the genus and species descriptions. The cellular fatty acid profiles of strain JC2131T and related members of the family Flavobacteriaceae are shown in Table

2. A significantly higher proportion of iso-C13 : 0 and lower proportions of C15 : 1ω6c and iso-C16 : 0 3-OH clearly differentiated strain JC2131T from the L. litoralis KCCM 42118T. The major respiratory quinone was menaquinone-6 (MK-6), in line with these all other members of the family Flavobacteriaceae. Flexirubin-type pigments were not detected. Chromatograms of the total lipids of strain JC2131T and related members of the family Flavobacteriaceae are shown in Fig. 2. The results showed that each profile from different genera was distinct, although all strains displayed phosphatidylethanolamine and some unidentified aminolipids and phospholipids. As shown by the 16S rRNA gene sequence analysis, strain JC2131T belonged to the family Flavobacteriaceae and formed a distinct phyletic line with the clades of the related genera. Furthermore, strain JC2131T was differentiated from members of the genus Lutibacter by several phenotypic

characteristics, including DNA G+C content, fatty acid composition, pH range for growth, sea salt requirement, aesculin hydrolysis and carbon utilization (Tables 1 and 2). Based on the polyphasic data presented in this study, strain JC2131T represents a novel genus and species of the family Flavobacteriaceae, for which the name Marinitalea sucinacia gen. nov., sp. nov. is proposed. Marinitalea (Ma.ri.ni.ta’le.a. L. adj. marinus, of the sea, marine; L. fem. n. talea, a rod; N.L. fem. n. Marinitalea, rod of the sea). Gram-negative, aerobic, chemoheterotrophic and mesophilic. Catalase-positive and oxidase-negative. Cells are rod-shaped with rounded ends, nonflagellated and nongliding. Flexirubin type pigments are absent. The major isoprenoid quinone is MK-6.