Cleaning effects of decontamination methods on clinically failed TiUnite implants and their impacts on surface roughness and chemistry: An in vitro pilot study.

PURPOSE: To evaluate the in vitro cleaning effects of different decontamination methods and their impacts on surface characteristics using clinically failed TiUnite implants (Nobel Biocare, Kloten, Switzerland). MATERIALS AND METHODS: Thirty clinically failed TiUnite implants were treated using different decontamination methods. Group 1 (control group) received physiological saline irrigation; Group 2 underwent erythritol powder air polishing (AIRFLOW Master Piezon, EMS Dental, Nyon, Switzerland); Group 3 was treated with erythritol powder air polishing with ethylenediaminetetraacetic acid brushing (FileRite PRC, Pulpdent, Watertown, MA, USA); Group 4 received ultrasonic scaling with polyetheretherketone tips (EMS Dental); Group 5 underwent ultrasonic scaling with polyetheretherketone tips with ethylenediaminetetraacetic acid; and Group 6 was treated with a combination of ultrasonic scaling with polyetheretherketone tips, erythritol powder air polishing and ethylenediaminetetraacetic acid. Surface cleaning effects, quantified by relative contaminated area reduction and visual analogue scale score, as well as surface roughness and chemistry, were assessed after decontamination. The cleaning effects of each decontamination method were also compared between TiUnite and SLA (sandblasted, large-grit acid-etched; Straumann, Basel, Switzerland) implants. RESULTS: Group 6 showed the highest relative contaminated area reduction (stereoscopic microscopy 83.92%, scanning electron microscopy 96.40%), visual analogue scale score (2.83) and reduction in surface roughness (thread bottom -0.78 µm, tip -1.35 µm), as well as an almost maximal decrease in the proportion of carbon (thread bottom -12.33%, tip -8.77%) and increase in that of titanium (thread bottom 13.71%, tip 10.73%). Polyetheretherketone remnants were observed in Groups 4 and 5 but appeared to be reduced in Group 6. When comparing the outcomes with those for SLA implants, no significant differences were found. CONCLUSION: Within the limitations of the present study, the combination of ultrasonic scaling with polyetheretherketone tips, erythritol powder air polishing and ethylenediaminetetraacetic brushing achieved reasonable cleaning effects. The original surface modification did not seem to have any impact on the decontamination results for any of the methods examined.

Targeting the IspD Enzyme in the MEP Pathway: Identification of a Novel Fragment Class.

The enzymes of the 2-C-methylerythritol-d-erythritol 4-phosphate (MEP) pathway (MEP pathway or non-mevalonate pathway) are responsible for the synthesis of universal precursors of the large and structurally diverse family of isoprenoids. This pathway is absent in humans, but present in many pathogenic organisms and plants, making it an attractive source of drug targets. Here, we present a high-throughput screening approach that led to the discovery of a novel fragment hit active against the third enzyme of the MEP pathway, PfIspD. A systematic SAR investigation afforded a novel chemical structure with a balanced activity-stability profile (16). Using a homology model of PfIspD, we proposed a putative binding mode for our newly identified inhibitors that sets the stage for structure-guided optimization.

Construction of wood-based cellulose micro-framework composite form-stable multifunctional materials with thermal and electrical response via incorporating erythritol-urea (thiourea)-carbon nanotubes.

In this study, two kinds of form-stable multifunctional materials with thermal and electrical response (FPCMs: DP-E7U3-CNT, DP-E7T3-CNT) are composed of wood-based honeycomb-like celluloses micro-framework (DP), carbon nanotubes (CNT), erythritol-urea (E7U3) or erythritol-thiourea (E7T3). In FPCMs, DP acts as a skeleton structure to seal E7U3 and E7T3 and provide more pathways for heat conduction. The CNT acts as an extended surface to further improve thermal conductivity. FE-SEM showed that the honeycomb-like pore structure of DP was completely filled with E7U3, E7T3 and CNT. FTIR and XRD analysis show that there is only a combination of physical interactions between the components of FPCMs. DSC curves and thermal conductivity analysis results show that DP-E7U3-1.5CNT and DP-E7T3-1.5CNT with the mass fraction of carbon nanotubes (1.5 wt%) have the highest latent heat values (230.3 J/g, 272.2 J/g) and thermal conductivity (0.9832 W/(m·K), 0.9363 W/(m·K)). Both DP-E7U3-1.5CNT and DP-E7T3-1.5CNT exhibit high latent heat retention and thermal stability after 100 heating-cooling cycles. In addition, DP-E7U3-1.5CNT and DP-E7T3-1.5CNT show excellent performance in light-heat energy conversion-storage, actual latent heat storage and release, thermal and electrical response performance, which make it has great potential to be multifunctional materials with thermal storage sand electrical response.

Apicoplast Metabolism: Parasite's Achilles' Heel.

Malaria continues to impinge heavily on mankind, with five continents still under its clasp. Widespread and rapid emergence of drug resistance in the Plasmodium parasite to current therapies accentuate the quest for novel drug targets and antimalarial compounds. Plasmodium parasites, maintain a non-photosynthetic relict organelle known as Apicoplast. Among the four major pathways of Apicoplast, biosynthesis of isoprenoids via Methylerythritol phosphate (MEP) pathway is the only indispensable function of Apicoplast that occurs during different stages of the malaria parasite. Moreover, the human host lacks MEP pathway. MEP pathway is a validated repertoire of novel antimalarial and antibacterial drug targets. Fosmidomycin, an efficacious antimalarial compound against IspC enzyme of MEP pathway is already in clinical trials as a combination drugs. Exploitation of other enzymes of MEP pathway would provide a much-needed impetus to the antimalarial drug discovery programs for the elimination of malaria. We outline the cardinal features of the MEP pathway enzymes and progress made towards the characterization of new inhibitors.

Sodorifen Biosynthesis in the Rhizobacterium Serratia plymuthica Involves Methylation and Cyclization of MEP-Derived Farnesyl Pyrophosphate by a SAM-Dependent C-Methyltransferase.

The rhizobacterium Serratia plymuthica 4Rx13 releases a unique polymethylated hydrocarbon (C16H26) with a bicyclo[3.2.1]octadiene skeleton called sodorifen. Sodorifen production depends on a gene cluster carrying a C-methyltransferase and a terpene cyclase along with two enzymes of the 2- C-methyl-d-erythritol 4-phosphate (MEP) pathway of isoprenoid biosynthesis. Comparative analysis of wild-type and mutant volatile organic compound profiles revealed a C-methyltransferase-dependent C16 alcohol called pre-sodorifen, the production of which is upregulated in the terpene cyclase mutant. The monocyclic structure of this putative intermediate in sodorifen biosynthesis was identified by NMR spectroscopy. In vitro assays with the heterologously expressed S. plymuthica C-methyltransferase and terpene cyclase demonstrated that these enzymes act sequentially to convert farnesyl pyrophosphate (FPP) into sodorifen via a pre-sodorifen pyrophosphate intermediate, indicating that the S-adenosyl methionine (SAM)-dependent C-methyltransferase from S. plymuthica exhibits unprecedented cyclase activity. In vivo incorporation experiments with 13C-labeled succinate, l-alanine, and l-methionine confirmed a MEP pathway to FPP via the canonical glyceraldehyde-3-phosphate and pyruvate, as well as its SAM-dependent methylation in pre-sodorifen and sodorifen biosynthesis. 13C{1H} NMR spectroscopy facilitated the localization of 13C labels and provided detailed insights into the biosynthetic pathway from FPP via pre-sodorifen pyrophosphate to sodorifen.

Deciphering the role of IspD (2­C­methyl­D­erythritol 4­phosphate cytidyltransferase) enzyme as a potential therapeutic drug target against Plasmodium vivax.

Biosynthesis of isoprenoids (MEP Pathway) in apicoplast has an important role during the erythrocytic stages of Plasmodium, as it is the sole pathway to provide the major isoprene units required as metabolic precursor for various housekeeping activities. With the intensifying need to identify a novel therapeutic drug target against Plasmodium, the MEP pathway and its components are considered as potential therapeutic targets, due to the difference in the isoprenoid synthesis route (MVA) functional in the host cells. While few major components have already been studied from this pathway for their potential as a drug target, IspD (2-C-methyl-D-erythritol-4-phosphate cytidyltransferase) enzyme, the enzyme catalyzing the third step of the pathway has only been tested against a synthetic compound from Malaria box called MMV008138, which also has not shown adequate inhibitory activity against P. vivax IspD. In the present study, to validate the potential of PvIspD as a drug target, various antimicrobial agents were screened for their inhibition possibilities, using in-vitro High Throughput Screening (HTS) technique. Shortlisted antimicrobial drug molecules like Cefepime, Tunicamycin and Rifampicin were further validated by in-vitro biochemical enzyme inhibition assays where they showed activity at nanomolar concentrations suggesting them or their derivatives as prospective future antimalarials. This study also confirmed the in-vivo expression of PvIspD protein during asexual stages by sub-cellular localization in apicoplast and explores the importance of the IspD enzyme in the development of new therapeutics.

Synthesis and Evaluation of Fluoroalkyl Phosphonyl Analogues of 2- C-Methylerythritol Phosphate as Substrates and Inhibitors of IspD from Human Pathogens.

Targeting essential bacterial processes beyond cell wall, protein, nucleotide, and folate syntheses holds promise to reveal new antimicrobial agents and expand the potential drugs available for combination therapies. The synthesis of isoprenoid precursors, isopentenyl diphosphate (IDP) and dimethylallyl diphosphate (DMADP), is vital for all organisms; however, humans use the mevalonate pathway for production of IDP/DMADP while many pathogens, including Plasmodium falciparum and Mycobacterium tuberculosis, use the orthogonal methylerythritol phosphate (MEP) pathway. Toward developing novel antimicrobial agents, we have designed and synthesized a series of phosphonyl analogues of MEP and evaluated their abilities to interact with IspD, both as inhibitors of the natural reaction and as antimetabolite alternative substrates that could be processed enzymatically to form stable phosphonyl analogues as potential inhibitors of downstream MEP pathway intermediates. In this compound series, the S-monofluoro MEP analogue displays the most potent inhibitory activity against Escherichia coli IspD and is the best substrate for both the E. coli and P. falciparum IspD orthologues with a Km approaching that of the natural substrate for the E. coli enzyme. This work represents a first step toward the development of phosphonyl MEP antimetabolites to modulate early isoprenoid biosynthesis in human pathogens.

Structural modeling identifies Plasmodium vivax 4-diphosphocytidyl-2C-methyl-d-erythritol kinase (IspE) as a plausible new antimalarial drug target.

Malaria parasites utilize Methylerythritol phosphate (MEP) pathway for synthesis of isoprenoid precursors which are essential for maturation and survival of parasites during erythrocytic and gametocytic stages. The absence of MEP pathway in the human host establishes MEP pathway enzymes as a repertoire of essential drug targets. The fourth enzyme, 4-diphosphocytidyl-2C-methyl-d-erythritol kinase (IspE) has been proved essential in pathogenic bacteria, however; it has not yet been studied in any Plasmodium species. This study was undertaken to investigate genetic polymorphism and concomitant structural implications of the Plasmodium vivax IspE (PvIspE) by employing sequencing, modeling and bioinformatics approach. We report that PvIspE gene displayed six non-synonymous mutations which were restricted to non-conserved regions within the gene from seven topographically distinct malaria-endemic regions of India. Phylogenetic studies reflected that PvIspE occupies unique status within Plasmodia genus and reflects that Plasmodium vivax IspE gene has a distant and non-conserved relation with human ortholog Mevalonate Kinase (MAVK). Structural modeling analysis revealed that all PvIspE Indian isolates have critically conserved canonical galacto-homoserine-mevalonate-phosphomevalonate kinase (GHMP) domain within the active site lying in a deep cleft sandwiched between ATP and CDPME-binding domains. The active core region was highly conserved among all clinical isolates, may be due to >60% ß-pleated rigid architecture. The mapped structural analysis revealed the critically conserved active site of PvIspE, both sequence, and spacially among all Indian isolates; showing no significant changes in the active site. Our study strengthens the candidature of Plasmodium vivax IspE enzyme as a future target for novel antimalarials.

Selective production of deacetylated mannosylerythritol lipid, MEL-D, by acetyltransferase disruption mutant of Pseudozyma hubeiensis.

Mannosylerythritol lipids (MELs) are produced by several smut fungi of the Ustilaginaceae family; they are promising microbial biosurfactants and have excellent surface-active and self-assembling properties. Pseudozyma hubeiensis is a candidate for abundant MEL production and produces large amounts of 4-O-[(4'-mono-O-acetyl-2',3'-di-O-alkanoyl)-ß-d-mannopyranosyl]-meso-erythritol (MEL-C). An acetyltransferase disruption mutant of P. hubeiensis, SY62-MM36, was obtained to selectively produce deacetylated 4-O-[(2',3'-di-O-alkanoyl)-ß-d-mannopyranosyl]-meso-erythritol (MEL-D), and the structures of the products were determined. Lower mobility of major spots of the mutant on silica gel thin-layer chromatography verified its more hydrophilic nature than that of wild-type MEL-A, B, and C. Structural analyses confirmed the product to be MEL-D, which comprises acyl chains of caproic acid (C6:0), capric acid (C10:0), and lauric acid (C12:0). The critical micelle concentration (CMC) and the surface tension (γCMC) of the MEL-D were 2.0 × 10-5 M and 29.7 mN/m, respectively. SY62-MM36 also produced a minor product that was estimated as triacylated MEL-D. The triacylated MEL-D had a CMC of 3.5 × 10-5 M and a γCMC of 29.6 mN/m. In water, MEL-D formed a lamella liquid crystal phase over a broad range of concentrations. By fed-batch cultivation, the mutant produced 91.6 ± 6.3 g/L of MEL-D for 7 days.

Roccellatol, a new ß-orcinol based metabolite from the lichen Roccella montagnei.

Roccellatol, a new (2'R,3'S)-erythrityl-2,6-dihydroxy-4-methylbenzoate was isolated along with nine known compounds from the fruticose lichen, Roccella montagnei Bel. em. D.D. Awasthi. The structure of the new compound was elucidated by detailed spectroscopic analysis (1H, 13C, DEPT and HRMS). The present isolation of roccellatol (10) assumes significance as the esters of p-orcellinic acid are rare in lichens. Interestingly, among the known compounds, (+)-montagnetol (9) was now isolated in very large quantity (4.66%).

Genetic diversity and structural analysis of 4-diphosphocytidyl-2C-methyl-D-erythritol kinase (IspE) from Plasmodium falciparum.

BACKGROUND & OBJECTIVES: Plasmodium parasite harbours unique methylerythritol phosphate (MEP) pathway which is obligatory for the biosynthesis of isoprenoids. In malaria parasites, the isoprenoids are indispensable during hepatic, erythrocytic and gametocytic stages. Owing to the criticality of MEP pathway and the potential of its enzymes to act as antimalarial drug target, this study comprehensively investigated the genetic diversity and structural composition of 4-diphosphocytidyl-2C-methyl-D-erythritol kinase (IspE), fourth enzyme of MEP pathway in Indian Plasmodium falciparum (PfIspE). METHODS: The study employed sequencing, modeling and bioinformatics approaches to examine the genetic diversity and associated structural polymorphism in the PfIspE gene amplified from the clinical blood samples collected from seven malaria endemic geographical regions of India. RESULTS: The sequence analysis showed that PfIspE gene is highly conserved with 100% sequence identity among all the P. falciparum Indian isolates as well as with the PfIspE gene of reference strain 3D7. Phylogenetic analysis suggested that PfIspE is highly evolved and differ sufficiently from human orthologue mevalonate kinase gene. Structural modeling studies revealed that PfIspE has conserved ATP and CDPME-binding domains. The active site was observed to be relatively rigid in architecture with >60% ß-pleated sheets. INTERPRETATION & CONCLUSION: The results of genetic, phylogeny and modeling studies strengthen the potential of PfIspE enzyme as a promising antimalarial drug target.

Highly Efficient Erythritol Recovery from Waste Erythritol Mother Liquor by a Yeast-Mediated Biorefinery Process.

Erythritol, a natural sugar alcohol, is produced industrially by fermentation and crystallization, but this process leaves a large amount of waste erythritol mother liquor (WEML) which contains more than 200 g/L erythritol as well as other polyol byproducts. These impurities make it very difficult to crystallize more erythritol. In our study, an efficient process for the recovery of erythritol from the WEML is described. The polyol impurities were first identified by high-performance liquid chromatography and gas chromatography-mass spectrometry, and a yeast strain Candida maltosa CGMCC 7323 was then isolated to metabolize those impurities to purify erythritol. Our results demonstrated that the process could remarkably improve the purity of erythritol and thus make the subsequent crystallization easier. This newly developed strategy is expected to have advantages in WEML treatment and provide helpful information with regard to green cell factories and zero-waste processing.

Supported Molybdenum Catalysts for the Deoxydehydration of 1,4-Anhydroerythritol into 2,5-Dihydrofuran.

Efficient deoxygenation strategies are crucial for the valorization of renewable feedstocks. Deoxydehydration (DODH) enables the direct transformation of two adjacent hydroxyl groups into a double bond. Supported molybdenum-based catalysts were utilized for the first time in DODH. MoOx /TiO2 showed superior catalytic activity compared to common molybdenum salts. The catalyst efficiently converted 1,4-anhydroerythritol into 2,5-dihydrofuran in the presence of 3-octanol as reducing agent, showing high reproducibility and stability.

New erythritol derivatives from the fertile form of Roccella montagnei.

Chemical investigation of the methanol extract of the fertile form of Roccella montagnei collected in Vietnam afforded twelve secondary metabolites, including five new montagnetol derivatives, orsellinylmontagnetols A-D and a furanyl derivative together with seven known compounds. Their chemical structures were elucidated by analysis of 1D and 2D NMR and high resolution mass spectroscopic data. The relative stereochemistry of two chiral centers (C-2 and C-3) of orsellinylmontagnetols A and B was elucidated by comparison of their coupling constants and the specific rotation with those reported in the literature while the absolute stereochemistry was determined by the application of a modified Mosher method for the hydroxy group at C-3. The absolute configuration (2R,3S) of the butanetetraol moiety of these compounds is in accordance with that of erythrin, a recognized chemotaxonomic marker of the genus Roccella. Five of these compounds were evaluated for their cytotoxic activities against four cancer cell lines. Only orsellinylmontagnetol A exerted a moderate activity against MCF-7 cell line with an IC50 value of 68.39 ± 3.46 µM.

Exposed Dentin: Influence of Cleaning Procedures and Simulated Pulpal Pressure on Bond Strength of a Universal Adhesive System.

PURPOSE: To compare various pre-treatments serving as cleaning procedures of dentin on the bond strength of resin composite promoted by a universal adhesive system applied either in the absence or presence of simulated pulpal pressure. MATERIALS AND METHODS: Prior to application of the adhesive system (Scotchbond Universal) and resin composite (Filtek Z250), ground dentin surfaces were given one of five pre-treatments either without or with simulated pulpal pressure: 1) no pre-treatment, adhesive system in "self-etch" mode, 2) phosphoric acid etching, adhesive system in "total-etch" mode, 3) polishing with pumice on prophylaxis cup, 4) air abrasion with AIR-FLOW PLUS powder, 5) air abrasion with AIR-FLOW PERIO powder; n = 20/group of pre-treatment. After storage (37°C, 100% humidity, 24 h), micro shear bond strength was measured and data analyzed with parametric ANOVA including Bonferroni-Holm correction for multiple testing followed by Student's t tests (significance level: α = 0.05). RESULTS: The ANOVA found type of pre-treatment and simulated pulpal pressure to have no significant effect on dentin bond strength. The explorative post-hoc tests showed a negative effect of simulated pulpal pressure for phosphoric acid etching (adhesive system in "total-etch" mode; p = 0.020), but not for the other four pre-treatments (all p = 1.000). CONCLUSION: Air abrasion with powders containing either erythritol and chlorhexidine (AIR-FLOW PLUS) or glycine (AIR-FLOW PERIO) yielded dentin bond strengths similar to no pre-treatment, phosphoric acid etching, or polishing with pumice. Simulated pulpal pressure reduced the bond strength only when the self-etch adhesive system was used in total-etch mode.

Molecular Mechanism of Action of Antimalarial Benzoisothiazolones: Species-Selective Inhibitors of the Plasmodium spp. MEP Pathway enzyme, IspD.

The methylerythritol phosphate (MEP) pathway is an essential metabolic pathway found in malaria parasites, but absent in mammals, making it a highly attractive target for the discovery of novel and selective antimalarial therapies. Using high-throughput screening, we have identified 2-phenyl benzo[d]isothiazol-3(2H)-ones as species-selective inhibitors of Plasmodium spp. 2-C-methyl-D-erythritol-4-phosphate cytidyltransferase (IspD), the third catalytic enzyme of the MEP pathway. 2-Phenyl benzo[d]isothiazol-3(2H)-ones display nanomolar inhibitory activity against P. falciparum and P. vivax IspD and prevent the growth of P. falciparum in culture, with EC50 values below 400 nM. In silico modeling, along with enzymatic, genetic and crystallographic studies, have established a mechanism-of-action involving initial non-covalent recognition of inhibitors at the IspD binding site, followed by disulfide bond formation through attack of an active site cysteine residue on the benzo[d]isothiazol-3(2H)-one core. The species-selective inhibitory activity of these small molecules against Plasmodium spp. IspD and cultured parasites suggests they have potential as lead compounds in the pursuit of novel drugs to treat malaria.

Phase State and Saturation Vapor Pressure of Submicron Particles of meso-Erythritol at Ambient Conditions.

meso-Erythritol is a sugar alcohol identified in atmospheric aerosol particles. In this work, evaporation of submicron-sized particles of meso-erythritol was studied in a TDMA system including a laminar flow tube under dry conditions at five temperatures (278-308 K) and ambient pressure. A complex behavior was observed and attributed to the formation of particles of three different phase states: (1) crystalline, (2) subcooled liquid or amorphous, and (3) mixed. With respect to saturation vapor pressure, the subcooled liquid and amorphous states are treated to be the same. The particle phase state was linked to initial particle size and flow tube temperature. Saturation vapor pressures of two phase states attributed to the crystalline and subcooled liquid state respectively are reported. Our results suggest a mass accommodation coefficient close to one for both states.

Comparison of the cohesion-adhesion balance approach to colloidal probe atomic force microscopy and the measurement of Hansen partial solubility parameters by inverse gas chromatography for the prediction of dry powder inhalation performance.

The abilities of the cohesive-adhesive balance approach to atomic force microscopy (AFM) and the measurement of Hansen partial solubility parameters by inverse gas chromatography (IGC) to predict the performance of carrier-based dry powder inhaler (DPI) formulations were compared. Five model drugs (beclometasone dipropionate, budesonide, salbutamol sulphate, terbutaline sulphate and triamcinolone acetonide) and three model carriers (erythritol, α-lactose monohydrate and d-mannitol) were chosen, giving fifteen drug-carrier combinations. Comparison of the AFM and IGC interparticulate adhesion data suggested that they did not produce equivalent results. Comparison of the AFM data with the in vitro fine particle delivery of appropriate DPI formulations normalised to account for particle size differences revealed a previously observed pattern for the AFM measurements, with a slightly cohesive AFM CAB ratio being associated with the highest fine particle fraction. However, no consistent relationship between formulation performance and the IGC data was observed. The results as a whole highlight the complexity of the many interacting variables that can affect the behaviour of DPIs and suggest that the prediction of their performance from a single measurement is unlikely to be successful in every case.

Synthesis of 2-Butanol by Selective Hydrogenolysis of 1,4-Anhydroerythritol over Molybdenum Oxide-Modified Rhodium-Supported Silica.

Rh-MoOx /SiO2 (Mo/Rh=0.13) is an effective catalyst for the hydrogenolysis of 1,4-anhydroerythritol (1,4-AHERY) and provides 2-BuOH in high yield of 51 %. This is the first report of the production of 2-BuOH from 1,4-AHERY by hydrogenolysis. 1,4-AHERY was more suitable as a starting material than erythritol because the 2-BuOH yield from erythritol was low (34 %). Based on the kinetics and comparison of reactivities of the related compounds using Rh-MoOx /SiO2 and Rh/SiO2 catalysts, the modification of Rh/SiO2 with MoOx leads to the high activity and high selectivity to 2-BuOH because of the generation of reactive hydride species and the strong adsorption of 1,4-AHERY on MoOx species. The reaction proceeds by main two routes, (I) the combination of single C-O hydrogenolysis with the desorption of intermediates, a usual route in hydrogenolysis, and (II) multiple C-O hydrogenolysis without the desorption of intermediates from the active site, and the reaction mechanism for Route (II) is proposed.

De Novo Transcriptome and Expression Profile Analysis to Reveal Genes and Pathways Potentially Involved in Cantharidin Biosynthesis in the Blister Beetle Mylabris cichorii.

The dried body of Mylabris cichorii is well-known Chinese traditional medicine. The sesquiterpenoid cantharidin, which is secreted mostly by adult male beetles, has recently been used as an anti-cancer drug. However, little is known about the mechanisms of cantharidin biosynthesis. Furthermore, there is currently no genomic or transcriptomic information for M. cichorii. In this study, we performed de novo assembly transcriptome of M. cichorii using the Illumina Hiseq2000. A single run produced 9.19 Gb of clean nucleotides comprising 29,247 sequences, including 23,739 annotated sequences (about 81%). We also constructed two expression profile libraries (20-25 day-old adult males and 20-25 day-old adult females) and discovered 2,465 significantly differentially-expressed genes. Putative genes and pathways involved in the biosynthesis of cantharidin were then characterized. We also found that cantharidin biosynthesis in M. cichorii might only occur via the mevalonate (MVA) pathway, not via the methylerythritol 4-phosphate/deoxyxylulose 5-phosphate (MEP/DOXP) pathway or a mixture of these. Besides, we considered that cantharidin biosynthesis might be related to the juvenile hormone (JH) biosynthesis or degradation. The results of transcriptome and expression profiling analysis provide a comprehensive sequence resource for M. cichorii that could facilitate the in-depth study of candidate genes and pathways involved in cantharidin biosynthesis, and may thus help to improve our understanding of the mechanisms of cantharidin biosynthesis in blister beetles.