Characterization of Biofilm Formation by Borrelia burgdorferi In Vitro

Borrelia burgdorferi, the causative agent of Lyme disease, has long been known to be capable of forming aggregates and colonies. It was recently demonstrated that Borrelia burgdorferi aggregate formation dramatically changes the in vitro response to hostile environments by this pathogen. In this study, we investigated the hypothesis that these aggregates are indeed biofilms, structures whose resistance to unfavorable conditions are well documented. We studied Borrelia burgdorferi for several known hallmark features of biofilm, including structural rearrangements in the aggregates, variations in development on various substrate matrices and secretion of a protective extracellular polymeric substance (EPS) matrix using several modes of microscopic, cell and molecular biology techniques. The atomic force microscopic results provided evidence that multilevel rearrangements take place at different stages of aggregate development, producing a complex, continuously rearranging structure. Our results also demonstrated that Borrelia burgdorferi is capable of developing aggregates on different abiotic and biotic substrates, and is also capable of forming floating aggregates. Analyzing the extracellular substance of the aggregates for potential exopolysaccharides revealed the existence of both sulfated and non-sulfated/carboxylated substrates, predominately composed of an alginate with calcium and extracellular DNA present. In summary, we have found substantial evidence that Borrelia burgdorferi is capable of forming biofilm in vitro. Biofilm formation by Borrelia species might play an important role in their survival in diverse environmental conditions by providing refuge to individual cells.     

Antibiosis of Commensal Bacteria Harboring the Gut of Estuarine Water Fish ‘Chelon parsia’

Microbiology - Screening of gut flora of the estuarine water fish ‘Chelon parsia’ for the presence of potential antibiotic producers resulted in finding a new strain Bacillus subtilis...     

Enzymatic esterification of starch using recovered coconut oil

Modification of maize and cassava starches was done using recovered coconut oil and microbial lipase. Microwave esterification was advantageous as it gave a DS 1.55 and 1.1 for maize starch and cassava starch, respectively. Solution state esterification of cassava starch for 36 h at 60 °C gave a DS of 0.08 and semi-solid state esterification gave a DS of 0.43. TGA and DSC studies showed that the higher DS attributed to the thermostability, since onset of decomposition is at a higher temperature (492 °C) than the unmodified (330 °C) and was stable above 600 °C. -Amylase digestibility and viscosity reduced for modified starch.     

1,2-Diaryl-1-ethanone and pyrazolo [4,3-c] quinoline-4-one as novel selective cyclooxygenase-2 inhibitors

Novel 1,2-diaryl-1-ethanone 1 and pyrazolo [4,3-c] quinoline-4-one 2, with pharmacophores different from the known COX inhibitors were identified as selective COX-2 inhibitors. The communication briefly describes SAR of both the series.     

Synthesis and biological evaluation of 2,3-diarylpyrazines and quinoxalines as selective COX-2 inhibitors

Several 2,3-diaryl pyrazines and quinoxalines with 4-sulfamoyl (SO(2)NH(2))/methylsulfonyl (SO(2)Me)-phenyl pharmacophores have been synthesized and evaluated for the cyclooxygenase (COX-1/COX-2) inhibitory activity. Smaller groups such as methoxy, methyl and fluoro when substituted at/around position-4 of the adjacent phenyl ring, have great impact on the selective COX-2 inhibitory activity of the series. Many potential compounds were obtained from a brief structure-activity relationship (SAR) study. Two of these, compounds 11 and 25 exhibited excellent in vivo activity in the established animal model of inflammation. Since compound 25 possessed an amenable sulfonamide group, two of its prodrugs 48 and 49 were also synthesized. Both of them have excellent in vivo potential, and represent a new class of COX-2 inhibitor.     

Novel highly selective inhibitors of ubiquitin specific protease 30 (USP30) accelerate mitophagy

Mitophagy is one of the processes that cells use to maintain overall health. An E3 ligase, parkin, ubiquitinates mitochondrial proteins prior to their degradation by autophagasomes. USP30 is an enzyme that de-ubiquitinates mitochondrial proteins; therefore, inhibiting this enzyme could foster mitophagy. Herein, we disclose the structure–activity relationships (SAR) within a novel series of highly selective USP30 inhibitors. Two structurally similar compounds, MF-094 (a potent and selective USP30 inhibitor) and MF-095 (a significantly less potent USP30 inhibitor), serve as useful controls for biological evaluation. We show that MF-094 increases protein ubiquitination and accelerates mitophagy.     

Morphological and seed protein characterization of the cultivated and the wild taxa of Sesamum L. (Pedaliaceae)

Seed protein analysis and morphological characterization were carried out in one cultivated and one wild species of Sesamum, Sesamum indicum L. and S. occidentale Regel and Heer. Data on 13 quantitative and 33 qualitative characters of the cultivated species and seven accessions of the wild taxa were analyzed. The genetic diversity of the taxa was assessed using UPGMA dendrogram and one-way ANOVA (p?<?0.05). Principal component analysis (PCA) was executed to identify the significant characters to delimit the taxa. Seed protein analysis showed diverse bands, ranging from 16 to 88?kDa. A dendrogram based on UPGMA analysis of seed protein suggested intraspecific relationships of the wild taxa as evidenced from the morphological characterization.