This paper reports results from training-related questions. The training area section had

one closed question (yes/no) and three sub-sections (two pertaining to therapeutic topics, which were the primary aim of analysis in this paper, and another section addressing issues such as supervision by doctors, continuing education, specialising in clinical areas and specialist registration) measuring attitudes see more on a five-point Likert scale. The questionnaire also had a section pertaining to participants’ demographic characteristics. In this section, information regarding respondents’ gender, years registered to practice, pharmacy ownership, location, professional area of practice, postcode and pharmacy size were obtained. As per existing models of prescribing in place in the UK, the question related to an independent prescribing model was proffered to respondents as ‘Pharmacists should be able to prescribe independent of medical practitioners, this includes assuming the responsibility of clinical assessment of the patient, establishing Raf inhibitor diagnosis and clinical management for a range of conditions within professional and clinical competence’ whereas the question related to supplementary

model of prescribing was proffered as ‘Pharmacists should be able to prescribe in a supplementary fashion through a partnership with an independent prescriber (a doctor or dentist) implementing an agreed patient-specific management plan. In this model the doctor diagnoses and initiates therapy while the pharmacist continues prescribing as long as the patient’s condition is within agreed management plan parameters’.[2, 11] The final questionnaire was sent to 2592 randomly selected pharmacists Cytoskeletal Signaling inhibitor around Australia. Random selection was done using an electronic randomiser. A follow-up questionnaire was sent after 1 month in January 2008. The questionnaire was anonymous and a follow-up reminder was sent to the entire original cohort, but pharmacists were asked to fill in and return the follow-up

questionnaire only if they have not done so previously. A more detailed description of the data collection process for this study has been published elsewhere.[11] Data were analysed using SPSS software (version 18) where frequency distributions were initially obtained to summarise the responses. Internal consistency of the statements used to measure pharmacists’ attitudes within each section of the questionnaire was evaluated using Cronbach’s alpha coefficient. In order to facilitate statistical analyses, a new variable with three categories was created from respondents who answered agreed/strongly agreed (n = 893/1049) to statements measuring attitudes regarding support for independent, supplementary or both of these prescribing models. The aim was to clearly distinguish between respondents who preferred both models as opposed to those who supported only one particular prescribing model for adoption by pharmacists in general.

Both clinics (n = 2, 100%) from Mexico, Central America, and the Caribbean and 80% (n = 4) of clinics from South America reported seldom or never having RIG accessible, respectively. Overall, the majority (76%; n = 114) of clinics reported using HRIG at their clinics (Table 1); 65 and 4% of these reported that an international pharmaceutical company or a local producer manufactured the HRIG, respectively (data not shown). However, 24% of

those reporting the use of HRIG did not know the manufacturer. Of the clinics reporting the use of ERIG (n = 15), six also reported the use of HRIG. Clinics reporting only ERIG use were from South Asia (n = 3); Eastern Europe and Northern Asia (n = 1); Metformin cost Middle East

and North Africa (n = 2); West, Central, and East Africa (n = 1); East and Southeast Asia (n = 1); and Tropical South America (n = 1). Of those using ERIG (n = 15), 80% reported using purified ERIG, 13% reported heat-treated digested ERIG FAB fragment, 7% reported heat-treated purified ERIG, and 7% reported not knowing the type of ERIG that was used. When asked where the travelers would be referred if RIG was not available, 63% (n = 119) of respondents reported that they would refer travelers to a clinic within the same city or elsewhere in their country, and 5% (n = 9) stated that they would refer only to clinics outside their country or send travelers back to their www.selleck.co.jp/products/cobimetinib-gdc-0973-rg7420.html home country. Ninety-one percent (n = 158) of all respondents reported that RV was often or always accessible (Table 2; Figure 3b). The use of human diploid cell and purified chick embryo cell vaccines

was most selleck inhibitor common in North America (60 and 31% of respondents, respectively) and Western Europe (56 and 34%, respectively). Vero cell vaccine was the predominant vaccine reported in Asia and Africa. Four clinics, in Tropical South America (n = 1), Eastern Europe and Northern Asia (n = 1), and the Middle East and North Africa (n = 2), reported the continued use of NTV. Most clinics (57%) responding to our survey indicated that they used the five-dose intramuscular administration schedule (Table 2). Thirty-two percent reported using the four-dose intramuscular administration schedule; 65% of these respondents were from North America. The Updated Thai Red Cross intradermal regimen was used by 56% of clinics in South Asia. When asked where the travelers would be referred if RV was not available at their clinics, 69% (n = 132) reported that they would refer travelers to clinics in the same city or elsewhere in their country, and 1% (n = 1) stated that they would refer only to clinics outside their country or send travelers back to their home country. Approximately one third of 187 respondents stated that patients presenting with wounds from an animal exposure seldom or never adequately cleansed those wounds (Table 3).

Then, protoplasts were prepared and spread on a regeneration medium (R5) (Hopwood et al., 1985) without apramycin. From these protoplasts, two types of apramycin-sensitive mTOR inhibitor colonies were obtained: a ΔbldKB-g mutant in which the WT bldKB-g gene is deleted and a regenerated WT strain. Correct disruption was confirmed through Southern hybridization using an appropriate probe (data not shown). pTYMbldK-g containing the entire bldK-g cluster and flanking sequences comprising 885 bp upstream of SGR2418 and 158 bp downstream of SGR2414 was constructed as follows: the 6.9-kb fragment was amplified by PCR using the primers bldKCF (which contains an EcoRI site) and bldKCR (which contains a HindIII site), digested

with EcoRI and HindIII, and cloned into the EcoRI and HindIII sites of pTYM19 (Onaka et al., 2003). pTYMbldK-c containing the promoter region of bldK-g and the entire bldK-c cluster was constructed as follows: the 0.9-kb Osimertinib fragment of the promoter region of bldK-g and the 6.7-kb fragment of the bldK-c cluster were amplified by PCR using the primers bldKgPF (which contains a HindIII site) and bldKgPR (which contains an XbaI site), bldKcF (which contains an XbaI site), and bldKcR (which contains an EcoRI site), respectively. These fragments were digested with HindIII and XbaI, XbaI and EcoRI, respectively, and cloned together into the HindIII and EcoRI sites of pTYM19. The resulting plasmids were used to transform the ΔbldKB-g mutant. Several thiostrepton-resistance transformants were selected and the correct chromosomal integration of the plasmid into the att site (in the SGR3787 coding sequence) was confirmed

by PCR using the appropriate primers (data not shown). A mutation (5′-ATCACTAGTG-3′) was introduced into the AdpA-binding site (5′-TGTCCGGATT-3′) of bldK-g as follows: a 0.7-kb fragment upstream of the AdpA-binding site was amplified by PCR using the oligonucleotide primers bldKCF and bldKMUR, which contain the mutated sequence. Separately, a 2.5-kb fragment downstream of the AdpA-binding SPTLC1 site was amplified by PCR using the primers bldKMDF and bldKMDR. The two resulting fragments were then joined and amplified by PCR using the primers bldKCF and bldKMDR. A 3.2-kb fragment was cleaved from the resulting product using EcoRI and ScaI and used to replace the 3.2-kb EcoRI–ScaI fragment of pTYMbldK-g, thereby generating pTYMbldKmut. (The EcoRI site was introduced via the bldKCF primer, while the ScaI site was originally present in the bldKC-coding sequence.) pTYMbldKmut was used to transform the ΔbldKB-g mutant using a method similar to that used for pTYMbldK-g. Total RNA prepared from the WT strain grown on YMPD or in SMM was isolated using an RNAqueous-Midi kit (Ambion). S1 nuclease mapping was performed using the method described by Bibb et al. (1986) and Kelemen et al. (1998).

In multiple labeling experiments, however, this value changed by < 2% points between labeling reactions, suggesting that the unlabeled populations are stable. The results do not rule out the possibility of the other hypotheses. Resolving AZD2014 which mechanism is predominant remains an unresolved question. However, dockerin replacement may explain the surprising result that cells with and without the cipA gene showed similar levels of fluorescence after labeling with the SNAP-XDocII fusion protein, because the necessity of displacing

CipA protein in the wild type and cipA* strains did not reduce fluorescence intensity. We have shown that the SNAP-tag system can be used to fluorescently label C. thermocellum via the cohesin–dockerin interaction. Previous studies have visualized cellulosomes by transmission electron microscopy (Bayer et al., 1985); however, the ability to specifically label the cellulosome in aqueous solution could lead to the ability to observe cellulosome operation in-vivo. Although much is known about the interaction between free dockerins and free cohesins, the interaction between free dockerins and bound cohesin–dockerin pairs has been less well studied. Dockerin exchange suggests a mechanism for compositional change of the cellulosome. Clostridium thermocellum is known to

release cellulosomes in the late-stationary Neratinib research buy phase of growth, as well as optimize the composition of cellulosomes attached to its surface in response to substrate changes (Bayer & Lamed, 1986; Raman et al., 2009). It has been suggested that detachment of intact cellulosomes in these processes is achieved

by proteolytic cleavage of the cohesin-II containing anchor proteins (Raman et al., 2009). The results of this study suggest an alternate or complementary mechanism, wherein the mere production of CipA molecules can effect turnover by dockerin exchange. Similar experiments could be used to probe interactions between type I cohesins and dockerins. In this study, we have demonstrated displacement of bound dockerin-containing proteins with free dockerin-containing proteins. This result sheds light on a possible mechanism for the natural Niclosamide turnover and reordering of cellulosome subunits within the polycellulosome. Furthermore, the methods of this article have established the SNAP-tag system as a valuable tool for labeling components and sub-components of the cellulosome. The authors would like to thank G.W. for assistance with flow cytometry studies and K.O. for microscopy research. This research was supported by the BioEnergy Science Center, Oak Ridge National Laboratory, a Department of Energy Bioenergy Research Center supported by the Office of Biological and Environmental Research in the Department of Energy Office of Science, and a Dartmouth College Dean of Faculty Undergraduate Research Grant. We would like to declare one competing interest. L.R.L.

, 2001; García-González et al., 2005). The atzR-atzDEF cluster is physically separated from the unstable region containing

atzA, atzB and atzC by two large gene clusters, which include the functions for the replication, segregation and conjugational transfer of pADP-1 (Martinez et al., 2001). Cya− (unable to degrade cyanuric acid) mutants arise due to the spontaneous loss of the complete pADP-1 plasmid, but independent loss of atzD, atzE or atzF is not detected, suggesting that these genes do not share the genetic instability of atzA, atzB and atzC (V. García-González & F. Govantes, unpublished data). Because atrazine is used primarily as a nitrogen source by degrading strains, the effect of nitrogen availability on atrazine degradation rates has been documented extensively. Generally, nitrogen amendments reduce the rates of atrazine degradation both in soil microbial populations (Entry et al., 1993; Alvey & Crowley, 1995; beta-catenin inhibitor Abdelhafid et al., 2000a, b; Guillén-Garcés et al., 2007) and in pure cultures of degrading bacteria (Bichat et al., 1999; Gebendinger & Radosevich, 1999; García-González et al., 2003), although exceptions to this rule

have been documented (Bichat et al., 1999). Pseudomonas sp. strain ADP is the best-characterized bacterial strain in nitrogen control of atrazine utilization (reviewed by Govantes et al., 2009). Atrazine Y-27632 price degradation by resting cell suspensions of Pseudomonas sp. strain ADP is inhibited when cells are grown on nitrogen sources that support fast growth, whereas cells grown on growth-limiting nitrogen sources or metabolites of the pathway (including atrazine) C-X-C chemokine receptor type 7 (CXCR-7) support efficient degradation. Atrazine does not induce the pathway in the presence of other nitrogen sources (Bichat et al.,

1999; García-González et al., 2003). Similarly, nitrate amendment significantly inhibited atrazine mineralization by Pseudomonas sp. strain ADP when tested in soil microcosms. The negative effect of added nitrogen sources on atrazine elimination limits the use of Pseudomonas sp. strain ADP bioremediation of atrazine-polluted agricultural soils (García-González et al., 2003). It should be noted that inhibition of atrazine metabolism by nitrate is only relevant when it is provided as a nitrogen source, as Pseudomonas sp. ADP appears to mineralize atrazine normally when nitrate is provided as an electron acceptor under anoxic conditions (Katz et al., 2000). This observation highlights the notion that inhibition is not the result of the mere presence of nitrate in the medium, but of its contribution to nitrogen availability. Attempts to study the expression of the atzA, atzB and atzC genes in Pseudomonas sp. strain ADP failed to demonstrate regulation in response to atrazine (Martinez et al., 2001; Devers et al., 2004) or nitrogen limitation (O. Porrúa & F. Govantes, unpublished data).

Conversely, a randomized placebo-controlled trial of

pneumococcal polysaccharide and conjugate vaccines showed no virological differences between adult groups on or off HAART [16], and an observational study of diphtheria/tetanus/acellular pertussis (DTaP) immunization of 2–9-year-olds receiving HAART also reported no effect on HIV viral load [17]. Whether there are long-term consequences of repeated bursts of HIV viraemia post-vaccination is unknown [18] and there is currently no evidence that vaccination adversely affects the pace of HIV disease progression [19]. HIV-positive children are at greater risk of vaccine-preventable infections than other children, yet vaccination coverage in this INCB024360 mw group is suboptimal selleck chemicals in populations across Europe [20-22]. Reasons for this may include physician uncertainty regarding the safety or appropriateness of vaccinating such children, deferral at times of intercurrent illness, or concerns that ‘intervention fatigue’ in patients may have adverse effects on HAART adherence. National and international societies recommend vaccination of HIV-positive children with some modification of routine schedules; for example, recommendations are available from the World

Health Organization (WHO)/United Nations Children’s Fund (UNICEF), the American Academy of Pediatrics and the British HIV Association (BHIVA) [5, 23-25]. Variation among these guidelines, compounded by differences among national schedules, may serve to reduce vaccine coverage in this vulnerable patient group. The development of uniform schedules for all HIV-positive children

Thiamet G living in European countries would be greatly beneficial, especially as new and more effective vaccines become available which potentially confer more benefits for HIV-infected children than for other children. However, achieving uniformity in guidelines is challenging given the inherent variation of the clinical, immunological and virological status of the cohort across Europe and within individual nations. Furthermore, increasing numbers of HIV-infected children living in Europe originate from developing countries and have incomplete or unknown vaccination status, unrelated to their immunological status or whether they are receiving HAART [26]. Recommendations need to accommodate the different requirements of (a) newly diagnosed children, whether immunocompetent or already immunocompromised; (b) those on HAART, whether complete or incomplete responders; (c) partially immunized or nonimmunized children within these groups; and (d) children during time periods when they fall below thresholds for effective or safe immunization. Yet European guidelines must also aim to minimize deviation from existing routine schedules, lest they generate confusion and further reduce vaccine uptake.

5 and incubated for a further 5 min. Cells were pelleted and washed with cold PBS and resuspended in 50 μL Towbin buffer. Samples were then boiled for 5 min and TraJ was separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and detected by immunoblot as described above. Because PD32 (hns) is Apr, pILJ14 (Cmr) was used instead of pBADTraJ. Mass spectroscopic

analysis of purified TraJ protein revealed a mass that was consistent with a polypeptide missing the first four amino acids (MYPM; data not shown). Because the initiating methionine is often clipped off in vivo, this suggested that TraJ translation initiated at M4 and not the previously reported M1 (numbered here according to Frost et al., 1994; see also Fig.

1 for the sequence with revised numbering). Mutagenic oligonucleotides were designed to mutate SRT1720 M1 and M4 codons, both separately and together, to threonine codons. These mutations (M1T, M4T and M1,4T) were constructed in pILJ11 to yield pJ-M1T, pJ-M4T and pJ-M1,4T (Table 1). These constructs were assayed for their ability to complement the traJ90 (traJQ26 amber) mutation in Flac traJ90, which is transfer-negative (Achtman et al., 1971; Table 1), and for protein production by immunoblot (Fig. 2). pJ-M1T produced Selleckchem Palbociclib TraJ at normal levels and complemented the traJ90 mutation, whereas pJ-M4T and pJ-M1,4T failed to produce the protein and had a low mating efficiency. Thus, M4 appears to be ID-8 the correct start codon for F traJ and the size of TraJ should be revised to 226 aa (26 670 kDa). Henceforth, all numbering is based on 226 residues (Fig. 1). The alignment of four orthologues of TraJ from plasmids F, R1, R100 and P307 revealed low sequence identity (20–30%; Frost et al., 1994). However, two clusters of

conserved amino acids were identified near the N-terminus (aa 28–50) and the C-terminus (aa 154–180) (Fig. 1). The function of the cluster of conserved amino acids at the N-terminus is currently unknown. Previously, TraJ has been suggested to contain an HTH DNA-binding motif (Frost et al., 1994), which usually contains 20–25 aa and a conserved glycine (Pabo & Sauer, 1992). The cluster at aa 154–180, centered around G166, matched these requirements and was considered to contain a putative HTH motif. blast analysis revealed that F TraJ resembled LuxR, a tetra-helical bundle DNA-binding protein (Aravind et al., 2005). Secondary structure prediction using the JPred3 algorithm (http://www.compbio.dundee.ac.uk) revealed a number of putative α-helical segments in the C-terminal half of the protein (Fig. 1) that is consistent with a similar prediction carried out for LuxR (data not shown). To test whether the HTH motif was functional, mutagenic oligonucleotides were designed for conserved amino acids in the region aa 154–180 (Fig. 1).

5 and incubated for a further 5 min. Cells were pelleted and washed with cold PBS and resuspended in 50 μL Towbin buffer. Samples were then boiled for 5 min and TraJ was separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and detected by immunoblot as described above. Because PD32 (hns) is Apr, pILJ14 (Cmr) was used instead of pBADTraJ. Mass spectroscopic

analysis of purified TraJ protein revealed a mass that was consistent with a polypeptide missing the first four amino acids (MYPM; data not shown). Because the initiating methionine is often clipped off in vivo, this suggested that TraJ translation initiated at M4 and not the previously reported M1 (numbered here according to Frost et al., 1994; see also Fig.

1 for the sequence with revised numbering). Mutagenic oligonucleotides were designed to mutate Selleckchem CH5424802 M1 and M4 codons, both separately and together, to threonine codons. These mutations (M1T, M4T and M1,4T) were constructed in pILJ11 to yield pJ-M1T, pJ-M4T and pJ-M1,4T (Table 1). These constructs were assayed for their ability to complement the traJ90 (traJQ26 amber) mutation in Flac traJ90, which is transfer-negative (Achtman et al., 1971; Table 1), and for protein production by immunoblot (Fig. 2). pJ-M1T produced buy SCH 900776 TraJ at normal levels and complemented the traJ90 mutation, whereas pJ-M4T and pJ-M1,4T failed to produce the protein and had a low mating efficiency. Thus, M4 appears to be P-type ATPase the correct start codon for F traJ and the size of TraJ should be revised to 226 aa (26 670 kDa). Henceforth, all numbering is based on 226 residues (Fig. 1). The alignment of four orthologues of TraJ from plasmids F, R1, R100 and P307 revealed low sequence identity (20–30%; Frost et al., 1994). However, two clusters of

conserved amino acids were identified near the N-terminus (aa 28–50) and the C-terminus (aa 154–180) (Fig. 1). The function of the cluster of conserved amino acids at the N-terminus is currently unknown. Previously, TraJ has been suggested to contain an HTH DNA-binding motif (Frost et al., 1994), which usually contains 20–25 aa and a conserved glycine (Pabo & Sauer, 1992). The cluster at aa 154–180, centered around G166, matched these requirements and was considered to contain a putative HTH motif. blast analysis revealed that F TraJ resembled LuxR, a tetra-helical bundle DNA-binding protein (Aravind et al., 2005). Secondary structure prediction using the JPred3 algorithm (http://www.compbio.dundee.ac.uk) revealed a number of putative α-helical segments in the C-terminal half of the protein (Fig. 1) that is consistent with a similar prediction carried out for LuxR (data not shown). To test whether the HTH motif was functional, mutagenic oligonucleotides were designed for conserved amino acids in the region aa 154–180 (Fig. 1).

However, it has been recently reported that PTEN

mutations are more frequent in low-grade endometrial EMA (67%) compared with low grade ovarian EMA (17%); contrastingly, CTNNB1 mutations are significantly different in low-grade ovarian EMA (53%) compared with low-grade endometrial EMA (28%).[56] This type of endometrial carcinoma typically has papillary growth and is comprised of atypical cells showing a high nucleus/cytoplasm ratio and high mitotic EGFR inhibitor review count. These cells are tufting and budding, and may often form glands. The background endometrium is usually atrophic. SEA typically displays the significant overexpressions of p53 and p16. Overexpression of p16 is thought to be due to dysregulation of the p16INKA/cyclin D-CDK/pRb-E2F pathway.[57-59] ER is usually diminished or negative, the

same as PgR. PTEN and ARID1A expressions are retained. Insulin-like growth factor II mRNA-binding protein 3 (IMP3) is overexpressed typically in embryonic tissue.[60-62] These results suggest that IMP3 is associated with cell migration and tumor LY2157299 in vivo invasion.[60, 63] The significant expression of IMP3 in SEA is, therefore, considered to be related to its development and aggressive clinical behavior.[63-65] SEA of the corpus and ovary share a considerable number of similar characteristics. But, as with WT-1, SEA of the ovary diffusely shows the expression in a frequency of 70–80%, and SEA of the endometrium is less frequently positive, at no more than 20–30%.[66-68] Endometrial intraepithelial

carcinoma (EIC), which is considered as a putative precursor of SEA,[69-71] usually occurs in the setting of inactive or resting endometrium and frequently involves endometrial polyps.[72] Many of minimal SEAs, defined as limited to the endometrium and less than 1 cm, are also frequently found to have EIC and involve endometrial polyps.[73] However, the nomenclature of EIC remains controversial because there are morphological variations in the endometrial intraepithelial precancerous Resminostat lesions. Therefore, instead of EIC, a newly defined terminology of endometrial glandular dysplasia has been proposed.[74] EIC is known to be potentially complicated with extrauterine lesions. The 10–34% of endometrial carcinomas in postmenopausal women have been reported to be associated with endometrial polyps, and the majority of them are the most common type EMA, with the second most common type being SEA.[75] These EICs show frequent p53 mutation with the ratio ranging 63–72%.[76] The labeling index of Ki-67 is approximately 40%, and ER and PgR are exceptionally expressed but not significantly.[72] CCA of the uterine corpus is also categorized as type II, but is not as frequent as SEA.[10, 11] Histologically, the CCA cells show papillary, tubular, tubulocystic and solid architecture, and possess polygonal nuclei with typically clear cytoplasm.

diphtheriae KCTC3075 has been characterized (Kim et al., 2010), which is the orthologue of DIP0543 C. diphtheriae NCTC GSK-3 cancer 13129 (Fig. 4), confirming that this organism has both normal sialidase but also a reported trans-sialidase activity (Mattos-Guaraldi et al., 1998). Other data suggested that C. diphtheriae harbours sialic acid on its cell envelope (Mattos-Guaraldi

et al., 1999). This could originate from the trans-sialidase activity moving sialic acid directly from host sialoglycans onto the bacterium’s surface. Both the lack of association of the sialidase with production of the diphtheria toxin (Warren & Spearing, 1963; Moriyama & Barksdale, 1967) and the lack of a need for uptake for cell surface modification were perhaps the reason why no study has ever examined the capability of C. diphtheriae to use sialic acid as a nutrient in vivo, which this study would suggest it is capable of. While the identity of a sialidase Selleck Ridaforolimus in C. diphtheriae has been known for

nearly 50 years, the presence of a sialidase in C. glutamicum has not been suspected. This enzyme is not orthologous to the sialidases seen in C. diphtheriae, C. ulcerans and C. pseudotuberculosis, but rather is most similar to Arthrobacter sp. The essential nature of the ABC transporter in the same gene cluster as the sialidase (cg2935) suggests that Cg2935 is a sialidase; however, this will need experimental confirmation. This study presents the first evidence for an active transporter for Neu5Ac in an actinobacterium and increases the range of bacteria that appear to use an ABC transporter for this purpose. Other bacteria where sialic acid transporters have been characterized use tripartite ATP-independent periplasmic (TRAP) transporters (Severi et al.,

2005; Mulligan et al., 2009, 2012; Chowdhury et al., 2012), classical secondary transporters of the Amylase major facilitator superfamily (Martinez et al., 1995; Mulligan et al., 2012) or sodium solute symporter family (SSS) transporters (Severi et al., 2010), although perhaps significantly all these are Gram-negative bacteria. The only clear work on sialic acid transport in Gram-positives are from Streptococcus pneumoniae, which also uses an ABC transporter (Marion et al., 2011a, b). The reduced growth lag when cells are precultured in the presence of sialic acid suggests either the presence of a sialic acid-specific activator or the inactivation of a repressor. Given the presence of a GntR-family transcription factor in the cluster (cg2936), it is probable that the presence of Neu5Ac or one of its catabolic product acts as the ligand to cause depression of the cluster. The additional observation is that derepression by Neu5Ac is not seen in the presence of glucose, suggesting a catabolic repression-type mechanism is in operation. The mechanisms of catabolite repression are not well studied in C. glutamicum, and in many cases, different carbon sources are co-metabolized.