A bacterial two-hybrid assay revealed that contrary to M. tuberculosis, Lnt1 of S. coelicolor does not interact with Ppm. The D2 catalytic domain of M. tuberculosisPpm was sufficient for complementation of an S. coelicolor double mutant lacking Lnt1 and Ppm, both for Apa glycosylation and for glycosylation of φC31 receptor. On the other hand, M. tuberculosisPmt was not active in S. coelicolor, even when correctly Stem Cells antagonist localized to the cytoplasmic membrane, showing fundamental differences in the requirements for Pmt activity in these two species. It is now well established that many bacteria are capable of carrying out different types of protein glycosylation, and recent studies have shown

the importance of this protein modification (Nothaft & Szymanski, 2010). In some bacteria of the ε subdivision of the proteobacteria, such as Campylobacter jejuni, N-glycosylation of proteins has been shown to be an important factor for pathogenicity (Nothaft & Szymanski, 2013). A system homologous to that of protein O-mannosylation in yeast has been described in actinomycetes, including Streptomyces coelicolor and Mycobacterium tuberculosis (Lommel & Strahl, 2009; Espitia et al., 2010), and the crucial role

buy Ion Channel Ligand Library of this protein modification in M. tuberculosis virulence has recently been demonstrated (Liu et al., 2013). This system involves polyprenyl phosphate mannose synthase (Ppm), homologous to dolichol phosphate mannose synthase of yeast; Ppm carries Interleukin-3 receptor the GDP-mannose-dependent

mannosylation of polyprenyl phosphate on the intracellular side of the cytoplasmic membrane. Mannosylated polyprenyl phosphate is then flipped to the extracytoplasmic side, and transfer of mannose to serine or threonine residues of protein substrates is then carried out by protein mannosyl transferase (Pmt), during secretion (VanderVen et al., 2005; Lommel & Strahl, 2009). In the case of M. tuberculosis, several mannoproteins important for pathogenesis have been identified (González-Zamorano et al., 2009), among them the 45- and 47-kDa antigen Apa, which is the best characterized mycobacterial glycoprotein in terms of the glycosylation sites and the configuration and number of sugar residues (Dobos et al., 1996; Espitia et al., 2010). However, there is little information on the specific proteins glycosylated by this system in S. coelicolor. Only the PstS protein has been shown to be a substrate for glycosylation (Wehmeier et al., 2009), and genetic evidence indicates that glycosylation of the phage φC31 receptor is required for infection by this phage (Cowlishaw & Smith, 2001, 2002). Streptomyces lividans, which is taxonomically closely related to S. coelicolor, has been shown to glycosylate the Apa antigenic protein of M. tuberculosis, and the resulting glycoprotein showed very similar antigenic properties to the native protein (Lara et al.

, 2007). The serogroup O:28 (formerly M) of the Kauffmann-White scheme (Grimont & Weill, 2007) consists

of 107 serovars of Salmonella, which have only the epitope O28 divided into three subfactors – O281, O282 and O283 – but without any differences identified (Lindberg & Le Minor, 1984). Salmonella Dakar (S. Dakar) has subfactors O281 and O283, whereas Salmonella Telaviv (S. Telaviv) possesses O281 and O282. Up till now, the structures of the repeating units of only two O-polysaccharides – S.  Dakar (Kumirska et al., 2007) and S. Telaviv (Kumirska et al., 2011) – have been established. Both O-antigens contain untypical sugar 3-acetamido-3,6-dideoxy-glucose (Quip3NAc), found also in other Gram-negative bacteria (Raff & Wheet, 1967; Raff & Wheat, 1968). In preparing O-antigen-immune sera for the identification of S. Telaviv and S. Dakar serovars, rabbits are immunized with these bacteria and the sera obtained are absorbed by Salmonella Cobimetinib mw Champaign (O:39) and Salmonella II 39:l,z28:e,n,x (39) (Lindberg & Le Minor, 1984). A control test should give a negative cross-reaction

with bacteria belonging to serogroups C1, C2, D (122+), SB431542 order O:30, O:35 and O:39. Literature data on the serological and immunological properties of this serogroup are very limited. Lüderitz et al. studied the cross-reactions of S. Dakar and S. Telaviv with Citrobacter freundii 8090 and Citrobacter freundii 869 using unabsorbed and absorbed test sera (Lüderitz et al., 1967; Keleti & Lüderitz, 1971). They observed that Citrobacter freundii 8090 cross-reacts only with sera containing antibodies against 283 factor, whereas Citrobacter freundii 869 behaves like S. Dakar, cross-reacting with those sera containing antibodies against factor either 281 or 283. The LPSs of both bacteria cross-react with S. Champaign (serogroup O:39) and Salmonella Frankfurt Atazanavir (serogroup O:16). Allen & Pazur (1984) analysed the interaction of S. Telaviv LPS with its lipid A free polysaccharide with polymeric McPC 870 and MOPC 384 mouse IgA myeloma proteins. Inhibition data suggest that this interaction can be mediated by galactose and/or glucose units

of cross-reactive antigens. A close relationship between Escherichia coli O71 and S. enterica O28 O-antigens (represented by S. Dakar) was found by Hu et al. (2010). The serogroup-specific genes of E. coli O71 and S. enterica O28 were established, and the structural similarity between the E. coli O71 and S. Dakar O-antigen structures was presented. Clark et al. (2010) reported that the O-antigen gene cluster of S. Dakar was quite different from that of Salmonella Pomona (O281, O282), although these serovars belonged to the same O-serogroup. This study describes the immunochemical investigations of the Salmonella Telaviv (S. Telaviv OPS) and S. Dakar (S. Dakar OPS) O-antigens using polyclonal sera and monoclonal antibodies (MAbs) against O281.

, 2007). The serogroup O:28 (formerly M) of the Kauffmann-White scheme (Grimont & Weill, 2007) consists

of 107 serovars of Salmonella, which have only the epitope O28 divided into three subfactors – O281, O282 and O283 – but without any differences identified (Lindberg & Le Minor, 1984). Salmonella Dakar (S. Dakar) has subfactors O281 and O283, whereas Salmonella Telaviv (S. Telaviv) possesses O281 and O282. Up till now, the structures of the repeating units of only two O-polysaccharides – S.  Dakar (Kumirska et al., 2007) and S. Telaviv (Kumirska et al., 2011) – have been established. Both O-antigens contain untypical sugar 3-acetamido-3,6-dideoxy-glucose (Quip3NAc), found also in other Gram-negative bacteria (Raff & Wheet, 1967; Raff & Wheat, 1968). In preparing O-antigen-immune sera for the identification of S. Telaviv and S. Dakar serovars, rabbits are immunized with these bacteria and the sera obtained are absorbed by Salmonella RG7420 molecular weight Champaign (O:39) and Salmonella II 39:l,z28:e,n,x (39) (Lindberg & Le Minor, 1984). A control test should give a negative cross-reaction

with bacteria belonging to serogroups C1, C2, D (122+), Ipilimumab clinical trial O:30, O:35 and O:39. Literature data on the serological and immunological properties of this serogroup are very limited. Lüderitz et al. studied the cross-reactions of S. Dakar and S. Telaviv with Citrobacter freundii 8090 and Citrobacter freundii 869 using unabsorbed and absorbed test sera (Lüderitz et al., 1967; Keleti & Lüderitz, 1971). They observed that Citrobacter freundii 8090 cross-reacts only with sera containing antibodies against 283 factor, whereas Citrobacter freundii 869 behaves like S. Dakar, cross-reacting with those sera containing antibodies against factor either 281 or 283. The LPSs of both bacteria cross-react with S. Champaign (serogroup O:39) and Salmonella Frankfurt HSP90 (serogroup O:16). Allen & Pazur (1984) analysed the interaction of S. Telaviv LPS with its lipid A free polysaccharide with polymeric McPC 870 and MOPC 384 mouse IgA myeloma proteins. Inhibition data suggest that this interaction can be mediated by galactose and/or glucose units

of cross-reactive antigens. A close relationship between Escherichia coli O71 and S. enterica O28 O-antigens (represented by S. Dakar) was found by Hu et al. (2010). The serogroup-specific genes of E. coli O71 and S. enterica O28 were established, and the structural similarity between the E. coli O71 and S. Dakar O-antigen structures was presented. Clark et al. (2010) reported that the O-antigen gene cluster of S. Dakar was quite different from that of Salmonella Pomona (O281, O282), although these serovars belonged to the same O-serogroup. This study describes the immunochemical investigations of the Salmonella Telaviv (S. Telaviv OPS) and S. Dakar (S. Dakar OPS) O-antigens using polyclonal sera and monoclonal antibodies (MAbs) against O281.

Congenital infections in the neonate have been described for a variety of opportunistic pathogens affecting the mother. These include Mycobacterium tuberculosis [14,15], cryptococcal infection [16,17], cytomegalovirus (CMV) [18], Pneumocystis jirovecii (PCP) [19,20] and toxoplasmosis

[21,22]. Vertical transmission is generally assumed to be the route of selleck inhibitor infection, although in some cases it may not be clear whether the neonate acquired the infection in utero or during the perinatal or postnatal period. Neonates born to HIV-seropositive women should be assessed by a paediatrician, and where necessary actively screened, for congenital opportunistic infections. The placenta should also be examined histologically ABT-737 for signs of infection or disease (category IV recommendation).

(Letters in parentheses denote US Food and Drug Administration-assigned pregnancy categories [23].) Therapeutic options are identical to non-pregnant patients. Trimethoprim-sulphamethoxazole (C/D) is the treatment of choice in pregnancy. Alternative options are limited to: clindamycin (B) with primaquine (C); dapsone (C) with trimethoprim (C); or atovaquone (C) suspension. Clindamycin is generally considered safe in pregnancy, but primaquine can cause haemolysis. There are limited data on the use of dapsone in pregnancy; however, one review identified mild degrees of haemolysis [24]. Intravenous pentamidine is embryotoxic much but not teratogenic, so should be used only if other options are not tolerated. Steroids should be administered as per standard guidelines for the treatment of PCP in non-pregnant women. Chemoprophylaxis for PCP should be prescribed to HIV-seropositive pregnant women as per guidelines for non-pregnant individuals. As for most drugs, avoidance of prescribing in the first trimester should be adhered to, other than in exceptional circumstances. It is important to remember that there is a false reduction in absolute CD4 cell counts during pregnancy, especially during the third trimester, and in such circumstances

more emphasis should be put on the CD4 percentage as an indicator for the need to commence PCP or indeed any prophylaxis. Trimethoprim-sulphamethoxazole (C/D) is the preferred prophylactic agent against PCP in pregnancy [25,26]. Concerns remain over the safety of this drug in the first trimester [27], and during this time an alternative agent could be used if indicated. Possible alternatives include once daily dapsone (C) or nebulised pentamidine (C). The dosing of these agents is the same as for non-pregnant individuals. Other alternatives to these agents include clindamycin (B) and primaquine (C) or atovaquone (C); however, data on their efficacy are not as clear as for the other agents, and data on their safety in pregnancy is not complete. First-line therapy should be with liposomal amphotericin B (B).

Indeed, the main goal of homeostatic plasticity INCB024360 cost studies is to control this directly by means of a ‘priming’ stimulus, as opposed to letting it vary normally, so as to optimize any effect of an intervention protocol (Fricke et al., 2011). The correlation between the change in the PPR and baseline state

was not evident in the measurement taken immediately after rTMS, although the average increase in the PPR even at that point was statistically significant. This is notable as it indicates that the influence of the baseline state of excitability on the response to rTMS is not present immediately after the stimulation has ended, but rather requires a time lapse to build up. This may indicate that the changes observed in the final measurement represent something closer to a ‘final’ size of response, before the effect begins to fade. However, this cannot be ascertained without a more prolonged period of post-stimulation testing. In the group that also received iHFS, this correlation between the baseline condition and the final measurement was not present, indicating that iHFS had a disruptive effect on the normal time course of the response to rTMS. It is important to note that, in the group that received rTMS alone (Group 2), the PPR

increased significantly after 25 min compared with the values obtained immediately after rTMS. This makes TSA HDAC cost it unlikely that the lack of further increase in the PPR after iHFS in Group 1 was from simply due to a ceiling effect, as after rTMS the PPR value was almost identical for both groups. Furthermore, in the group that received iHFS alone (Group 3), the baseline value of the PPR approximated

the value found in the other two groups after rTMS. This did not prevent iHFS from producing a significant increase in the PPR, suggesting that the lack of effect of iHFS in Group 1 depended on the previous history of activity rather than on the value of the PPR at the time of stimulation. In contrast to the results obtained for cortical excitability, rTMS and iHFS showed no significant interaction in their effect on tactile acuity. Both groups experienced a significant improvement in two-point discrimination immediately following rTMS, which remained unchanged in the last assessment, with or without iHFS. A previous report, in which a similar rTMS protocol was used, also showed that the induced change in tactile acuity was strongest immediately after stimulation, and slowly reverted to baseline values over the following hours (Tegenthoff et al., 2005). This represents a marked difference from the effect of rTMS on cortical excitability, which, as was shown above, is considerably stronger 25 min after the end of stimulation than immediately after. In addition, the effect on the PPR was highly sensitive to iHFS, whereas iHFS had almost no influence on the rTMS-induced change in tactile acuity.

28, 95% CI = 5.54–36.81). We found higher risk of resistance among patients with metastasis (OR = 8.42, 95% CI = 2.44–29.07), large tumor size (>3 cm) (OR = 7.73, 95% CI = 1.93–30.91), high β-hCG (>100 000 IU/L) (OR = 5.86, 95% CI = 1.07–32.02) and/or a diagnosis more than 4 months after pregnancy (OR = 3.30, 95% CI = 1.08–10.02), compared with their reference PFT�� chemical structure group. We found no priority for the different

chemotherapy regimens. Intermediate risk GTN patients had a higher risk of resistance to chemotherapy compared with low-risk patients. Clinical trials and cost-effectiveness studies are needed to suggest a better treatment program for the intermediate risk group. “
“Aim:  The aim of this study was to evaluate urine microscopy, dipstick analysis and urinary symptoms in screening for urinary tract infection (UTI) in hyperemesis gravidarum (HG). Materials and Methods:  A prospective cross-sectional study was performed on women at VX-765 mw first hospitalization for HG. A clean-catch mid-stream urine sample from each recruit was sent for microscopy (for bacteria, leucocytes and erythrocytes), dipstick analysis (for leukocyte esterase, nitrites, protein and hemoglobin) and microbiological culture. The presence of current

urinary symptoms was elicited by questionnaire. UTI is defined as at least 105 colony-forming units/mL of a single uropathogen on culture.

Screening test parameters were analyzed Interleukin-2 receptor against UTI. Results:  UTI was diagnosed in 15/292 subjects (5.1%). Receiver–operator characteristic curve analysis of microscopic urine leucocytes revealed area under the curve = 0.64, 95% confidence interval (CI) 0.5–0.79, P = 0.063 and erythrocytes area under the curve = 0.53, 95%CI 0.39–0.67, P = 0.67 for UTI indicating the limited screening utility of these parameters. Microscopic bacteriuria (likelihood ratio [LR] 1.1, 95%CI 0.7–1.5) and urine dipstick leukocyte esterase (LR 1.4, 95%CI 1.1–1.8), nitrites (LR 2.3, 95%CI 0.3–17.2), protein (LR 1.0, 95%CI 0.7–1.6) and hemoglobin (LR 0.8, 95%CI 0.4–1.5) were not useful screening tests for UTI in HG. Elicited symptoms were also not predictive of UTI. Conclusion:  Urine microscopy, dipstick analysis and urinary symptoms were not useful in screening for UTI in HG. UTI should be established by urine culture in HG before starting antibiotic treatment. “
“Developments in immunohistochemistry, which are closely linked with the advances in the analyses of genetic abnormalities and their associated molecular disorders as early and late histogenetic events, have contributed greatly to the improvement of pathological diagnostic confirmation and validation. Immunohistochemistry has also generated great benefit to the innovation of therapeutic strategies for various kinds of cancers.

3, Fig S2). Similar strong effects of DNase treatment on biofilm integrity has been observed for P. aeruginosa, Streptococcus mutans, and Streptococcus intermedius (Whitchurch et al., 2002; Petersen et al., 2005). Hence, eDNA may be responsible for the development or stabilization of the air–liquid interface biofilm formed by KT2440 TOL. Its removal by DNase treatment reduces the cohesiveness of the pellicle and probably results in a higher turnover of the pellicle. eDNA release in biofilms (P. aeruginosa, E. faecalis) is often caused by cell lysis under control of density-dependent Epacadostat clinical trial mechanisms (Allesen-Holm et al., 2006; Qin et al., 2007; Thomas et al., 2009), while in other cases, the mechanisms

of its excretion are not clear (Bockelmann et al., 2006; Vilain et al., 2009). Hence, we examined differential culture viability in the static cultures. Using a live/dead staining procedure and flow cytometric quantification of cells, three core observations were made (Table 2). First, TOL carriage delayed initial increase in culture densities, but final densities of both cultures were similar. Second, the fraction of dead cells increased at the end of incubation, but was not affected by plasmid carriage. Third, cell sizes increased slightly Thiazovivin with culture age, and this effect was strongest for the TOL-carrying strain (Table 2). Exocellular β-glucosidase activity increased in both cultures with time, and sharply

after 7 days, but with little relation to TOL carriage. Therefore, we could not obtain proof for plasmid-carriage-dependent cell lysis as the reason for increased eDNA concentrations. Similar cell counts and live/dead fractions were observed in static cultures of both strains irrespective of plasmid carriage, and measures of released cellular

enzymatic activity were similar. The stimulatory role of plasmid carriage on biofilm formation was first documented and examined with E. coli K-12. The effect was restricted to derepressed plasmids, and pointed to the need for traA-like gene expression, suggesting a direct involvement of conjugal pili as adhesion factors (Ghigo, 2001; Reisner et al., 2003). Observations with a range of E. coli isolates confirmed that selleck chemical biofilm stimulation was contingent on active conjugal plasmid transfer (Reisner et al., 2006). Although some direct proof of IncF-mating pili involvement in initial biofilm establishment has been provided (May & Okabe, 2008), the exact mechanisms responsible for plasmid-mediated biofilm enhancement remain unresolved. Yang et al. (2008) have shown that enhanced biofilm formation caused by the presence of R1drd19 in E. coli is contingent on the envelope stress response system, speculating that pili synthesis imposes stress on membranes. The virulence plasmid pO157 enhances biofilm formation in E. coli 0157:H7 due to increased exopolysaccharide production (Lim et al.

3, Fig S2). Similar strong effects of DNase treatment on biofilm integrity has been observed for P. aeruginosa, Streptococcus mutans, and Streptococcus intermedius (Whitchurch et al., 2002; Petersen et al., 2005). Hence, eDNA may be responsible for the development or stabilization of the air–liquid interface biofilm formed by KT2440 TOL. Its removal by DNase treatment reduces the cohesiveness of the pellicle and probably results in a higher turnover of the pellicle. eDNA release in biofilms (P. aeruginosa, E. faecalis) is often caused by cell lysis under control of density-dependent Neratinib concentration mechanisms (Allesen-Holm et al., 2006; Qin et al., 2007; Thomas et al., 2009), while in other cases, the mechanisms

of its excretion are not clear (Bockelmann et al., 2006; Vilain et al., 2009). Hence, we examined differential culture viability in the static cultures. Using a live/dead staining procedure and flow cytometric quantification of cells, three core observations were made (Table 2). First, TOL carriage delayed initial increase in culture densities, but final densities of both cultures were similar. Second, the fraction of dead cells increased at the end of incubation, but was not affected by plasmid carriage. Third, cell sizes increased slightly VE-821 supplier with culture age, and this effect was strongest for the TOL-carrying strain (Table 2). Exocellular β-glucosidase activity increased in both cultures with time, and sharply

after 7 days, but with little relation to TOL carriage. Therefore, we could not obtain proof for plasmid-carriage-dependent cell lysis as the reason for increased eDNA concentrations. Similar cell counts and live/dead fractions were observed in static cultures of both strains irrespective of plasmid carriage, and measures of released cellular

enzymatic activity were similar. The stimulatory role of plasmid carriage on biofilm formation was first documented and examined with E. coli K-12. The effect was restricted to derepressed plasmids, and pointed to the need for traA-like gene expression, suggesting a direct involvement of conjugal pili as adhesion factors (Ghigo, 2001; Reisner et al., 2003). Observations with a range of E. coli isolates confirmed that Exoribonuclease biofilm stimulation was contingent on active conjugal plasmid transfer (Reisner et al., 2006). Although some direct proof of IncF-mating pili involvement in initial biofilm establishment has been provided (May & Okabe, 2008), the exact mechanisms responsible for plasmid-mediated biofilm enhancement remain unresolved. Yang et al. (2008) have shown that enhanced biofilm formation caused by the presence of R1drd19 in E. coli is contingent on the envelope stress response system, speculating that pili synthesis imposes stress on membranes. The virulence plasmid pO157 enhances biofilm formation in E. coli 0157:H7 due to increased exopolysaccharide production (Lim et al.

, 1995; Loeffler et al., 2003; Schmelcher et al., 2012). This may be an advantage of this endolysin, as these ionic conditions correspond to the salt concentration of many food products. LysBPS13 seems to need no metal ions for its lytic activity, because the addition of EDTA (300 mM) did not affect its lytic activity (Fig. 4d), nor did the presence of metal ions (1 mM MgCl2, CaCl2, ZnCl2, or MnCl2) (data not shown). This result was unexpected because the three Zn2+-binding residues in the PGRP domain were completely conserved

in LysBPS13. While T7 lysozyme that belongs to the PGRP family has Zn2+-dependent amidase activity (Gelius et al., 2003; Kim et al., 2003), another report found a Zn2+-independent amidase (ORF9) in GKT137831 in vivo the E. faecalis selleck inhibitor bacteriophage EF24C (Uchiyama et al., 2011). Like LysBPS13, E. faecalis ORF9 has a PGRP domain at its N-terminus, and blastp analysis

indicated Zn2+-binding sites, but Zn2+ did not seem to be essential for its activity. Yet, we cannot rule out the possibility that Zn2+ or other metal cofactors are bound to LysBPS13 too tightly to be removed by EDTA. Therefore, further study is necessary to elucidate the structure of the PGRP domain in endolysins, particularly the Zn2+-binding site. When LysBPS13 was tested in combination with various detergents (Fig. 4d), LysBPS13 showed full or higher activity in the presence of zwitterionic (CHAPS) PLEKHM2 and nonionic detergents (Triton X-100, Tween-20). However, both anionic (SDS) and cationic (CTAB) detergents inactivated LysBPS13. Thermostability of phage endolysins would be advantageous for applications as biocontrol agents

that undergo heat treatment. B. cereus food poisoning is often associated with cooked rice products, because B. cereus spores are able to endure high temperatures and germinate when cooling down (Stenfors Arnesen et al., 2008). Most endolysins are labile to heat (Lavigne et al., 2004). However, to date, only a few lysins have been reported to be thermostable, including Gp36 from the Pseudomonas aeruginosa bacteriophage φKMV (Lavigne et al., 2004); the lysins HPL118, HPL511, and HPLP35 from Listeria bacteriophages (Schmelcher et al., 2012); and the GVE2 lysin (EF079891) from Geobacilllus phage GVE2 (Ye & Zhang, 2008). Gp36 has extremely high thermostability, retaining 21% of its activity after autoclaving at 121 °C for 20 min; other lysins have milder thermostability (Lavigne et al., 2004; Ye & Zhang, 2008). LysBPS13 appeared to be highly stable, as the protein retained full lytic activity after a week-long incubation in storage buffer at room temperature. The thermostability of LysBPS13 was further assessed after pre-incubation of the enzyme at temperatures between 4 and 100 °C (Fig. 5). LysBPS13 demonstrated lytic activity after incubation for 30 min at all tested temperatures.

, 2010) and VctA and IrgA in Vibrio cholerae (Mey

et al., 2002). However, little is known about multiple receptors for a cognate siderophore with the exception of the type I ferric pyoverdine receptors FpvA and FpvB in Pseudomonas aeruginosa (Ghysels et al., 2004). Because fpvA and fpvB are located on separate replicons and both proteins exhibit 54% amino acid sequence similarity, our study presents the first examples of two IROMPs encoded by different tandem genes in the same operon functioning as the receptors for the same Tacrolimus datasheet cognate siderophore. This strategy may provide an alternative backup system – that is, protection against mutational loss – for VF-mediated iron acquisition in V. parahaemolyticus. However, the coexistence of pvuA1 and pvuA2 in the VF-utilization cluster raise the possibility that either pvuA1 or pvuA2 actually preferentially binds and transports an unknown siderophore ligand that is structurally related to VF. We also determined the specificities of the ferric VF receptors on three sets of TonB systems for ferric VF. It is noteworthy high throughput screening assay that TonB2 is exclusively required for the PvuA1-mediated transport of ferric VF; meanwhile, the PvuA2-mediated transport of ferric VF is supported by both TonB1 and TonB2. Further studies are needed to understand the specificities of TonB for other V. parahaemolyticus receptors for the uptake of heme/hemoglobin as well as exogenous siderophores such

as aerobactin (Funahashi et al., 2003) and ferrichrome (Funahashi

Aldol condensation et al., 2009). We thank T. Kuroda for providing E. coli β2155 and a suicide vector pXAC623 and for his helpful comments. This work was supported in part by a grant from the Cooperative and Collaboration Agreement between Ehime University and Matsuyama University. “
“Members of the genus Rhodococcus were investigated for their ability to produce glycogen during cultivation on gluconate or glucose. Strains belonging to Rhodococcus ruber, Rhodococcus opacus, Rhodococcus fascians, Rhodococcus erythropolis and Rhodococcus equi were able to produce glycogen up to 0.2–5.6% of cellular dry weight (CDW). The glycogen content varied from 0.8% to 3.2% of CDW in cells of R. opacus PD630, which is a well-known oleaginous bacterium, during the exponential growth phase, when cultivated on diverse carbon sources. Maltose and pyruvate promoted glycogen accumulation by cells of strain PD630 to a greater extent than glucose, gluconate, lactose, sucrose or acetate. This strain was able to produce triacylglycerols, polyhydroxyalkanoates and glycogen as storage compounds during growth on gluconate, although triacylglycerols were always the main product under the conditions of this study. Cerulenin, an inhibitor of de novo fatty acid synthesis, inhibited the accumulation of triacylglycerols from gluconate and increased the content of polyhydroxyalkanoates (from 2.0% to 4.2%, CDW) and glycogen (from 0.1% to 3.0%, CDW).