13,215 research outputs found
A proteomic investigation of Fusobacterium nucleatum alkaline-induced biofilms
No full textBackground: The Gram negative anaerobe Fusobacterium nucleatum has been implicated in the aetiology of periodontal diseases. Although frequently isolated from healthy dental plaque, its numbers and proportion increase in plaque associated with disease. One of the significant physico-chemical changes in the diseased gingival sulcus is increased environmental pH. When grown under controlled conditions in our laboratory, F. nucleatum subspecies polymorphum formed mono-culture biofilms when cultured at pH 8.2. Biofilm formation is a survival strategy for bacteria, often associated with altered physiology and increased virulence. A proteomic approach was used to understand the phenotypic changes in F. nucleatum cells associated with alkaline induced biofilms. The proteomic based identification of significantly altered proteins was verified where possible using additional methods including quantitative real-time PCR (qRT-PCR), enzyme assay, acidic end-product analysis, intracellular polyglucose assay and Western blotting. Results: Of 421 proteins detected on two-dimensional electrophoresis gels, spot densities of 54 proteins varied significantly (p < 0.05) in F. nucleatum cultured at pH 8.2 compared to growth at pH 7.4. Proteins that were differentially produced in biofilm cells were associated with the functional classes; metabolic enzymes, transport, stress response and hypothetical proteins. Our results suggest that biofilm cells were more metabolically efficient than planktonic cells as changes to amino acid and glucose metabolism generated additional energy needed for survival in a sub-optimal environment. The intracellular concentration of stress response proteins including heat shock protein GroEL and recombinational protein RecA increased markedly in the alkaline environment. A significant finding was the increased abundance of an adhesin, Fusobacterial outer membrane protein A (FomA). This surface protein is known for its capacity to bind to a vast number of bacterial species and human epithelial cells and its increased abundance was associated with biofilm formation. Conclusion: This investigation identified a number of proteins that were significantly altered by F. nucleatum in response to alkaline conditions similar to those reported in diseased periodontal pockets. The results provide insight into the adaptive mechanisms used by F. nucleatum biofilms in response to pH increase in the host environment.Jactty Chew, Peter S Zilm, Janet M Fuss and Neville J Gull
Ms. Courtney Chartier, RWWL AUC, August 2011
No full textThis video is a conversation with Ms. Courtney Chartier. Ms. Chartier talks about her work on the "New Georgia Encyclopedia" and "Online Voter Education Project." Andrea Jackson, AUC Woodruff Library, is the interviewer
Ms. Neely Terrell, RWWL AUC, March 2012
No full textThis video is a conversation with Ms. Neely Terrell. Ms. Terrell talks about her book, "Super Singles Activate". Anthony Kinsey and Jahnesta Horney, AUC Woodruff Library, are the interviewers
Ms. Felesha Love, Spelman College, January 2016
No full textThis video is a conversation with Felesha Love. Ms. Love talks about her book, "Brave Leap to Freedom: Integrating Mind, Body, and Spirit to Cultivate Healthy Relationships". Jordan Moore, AUC Woodruff Library, is the interviewer
Green state fluorescence comparison between pcFP-CheW fusions.
No full text<p>(<b>A</b>) <i>E. coli</i> was transformed with plasmids encoding CheW fusion proteins and cultures were induced with 0.01% L-arabinose (top row) and 0.2% L-arabinose (bottom row) for 3 h at 30°C and then imaged using 488 nm excitation. Note the brightness of the cells expressing mMaple fusions and the large percentage of cells with the correct polar localization pattern. (<b>B</b>) Fluorescence image of the bands corresponding to pcFP-CheW fusions extracted from <i>E. coli</i> and analyzed by SDS-PAGE gel. Proteins were either purified from the soluble fraction by Ni<sup>2+</sup>-NTA, solubilized from inclusion bodies with urea (IB), or loaded onto the gel as a whole cell lysate (WCL). Exposure times were increased from 60 ms to 2 sec in order to visualize the fluorescence of GFP-CheW and mEos2-CheW (right). Relative fluorescence intensities after correction for exposure times are: 1.00, 2.56, 0 (mMaple-CheW), 4.79, 0.43 (mClavGR2-CheW), 0, 0.08, 0.14 (EGFP-CheW), 0, 0.03 and 0 (mEos2-CheW). The Coomassie stained version of this gel is shown in <b><a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0051314#pone.0051314.s002" target="_blank">Fig. S2C</a></b>. (<b>C</b>) Cells expressing only cytoplasmic versions of each pcFP were grown in LB and induced with 0.002% L-arabinose for 3 hours. The mean fluorescence intensity for cells expressing mMaple was more than three times that of mEos2 (1489±636 for mMaple in comparison to 463±281 for mEos2) (<i>N</i> = 58 cells for mMaple, <i>N</i> = 57 cells for mClavGR2 and mEos2. (<b>D</b>) Mean fluorescence intensity for cells expressing each pcFP-CheW fusion. Consistent with the images in (A) and (B), at both induction levels, the mean fluorescence intensity level of mMaple-CheW is higher than all other CheW fusions (for 0.01% arabinose conditions, the number of cells analyzed was 69 for mMaple-CheW and 46 for mClavGR2-CheW respectively; for 0.2% conditions, <i>N</i> = 91, 62, 40, 71 cells for mMaple, mClavGR2, mEos2 and GFP fusions respectively).</p
Coon Mountain and Its Crater, and Coon Butte, Arizona
No full textTwo articles from the Proceedings of the Academy of Natural Sciences of Philadelphia, December 1905, by Daniel Moreau Barringer [Jr.] and Benjamin Chew Tilghman respectively, relating to Canyon Diablo
Effects of the mutation R62A on the global and local backbone dynamics of CheW.
No full text<p>Backbone amide <sup>15</sup>N relaxation parameters for CheW vs. residue number are shown. The black squares represent wild-type CheW, the red circles represent R62A mutant, and the green triangles represent the difference between these two constructs. Approximate location of secondary structural elements is shown at the top: (a) the longitudinal relaxation rate R<sub>1</sub>; (b) the transverse relaxation rate R<sub>2</sub>; (c) <sup>1</sup>H-<sup>15</sup>N NOE; (d) the extracted order parameter S<sup>2</sup> (e) the differences phenomenological transverse relaxation rate constant ΔR<sub>ex</sub> = R<sub>ex</sub>(20 ms)−R<sub>ex</sub>(1 ms); (f) the differences between the ΔR<sub>ex</sub> in (e) ΔR<sub>ex</sub>(R62A)−ΔR<sub>ex</sub>(WT).</p
Étude sur le patois de Valbonnais
No full textA lexical and morphologic description of Valbonnais dialect. A 319-page PhD dissertation under the direction of Prof. Antonin DURAFFOUR (Univ. Stendhal, Grenoble, France, 1943)Description lexicale et morphologique du patois de Valbonnais sous la forme d'un manuscrit de 319 pages.Thèse sous la direction du Prof. Antonin DURAFFOUR (Univ. Stendhal, Grenoble, 1943
Radar Chart of Citation topic Meso, source: Formulated by author using MS Excel (2016).
No full textRadar Chart of Citation topic Meso, source: Formulated by author using MS Excel (2016).</p
Improving MHC-I ligand identifications from LC-MS/MS data by incorporating allelic peptide motifs
No full textMHC class I (MHC-I)-bound ligands play a pivotal role in CD8 T cell immunity and are hence of major interest in understanding and designing immunotherapies. One of the most commonly utilized approaches for detecting MHC ligands is LC-MS/MS. Unfortunately, the effectiveness of current algorithms to identify MHC ligands from LC-MS/MS data is limited because the search algorithms used were originally developed for proteomics approaches detecting tryptic peptides. Consequently, the analysis often results in inflated false discovery rate (FDR) statistics and an overall decrease in the number of peptides that pass FDR filters. Andreatta et al. describe a new scoring tool (MS-rescue) for peptides from MHC-I immunopeptidome datasets. MS-rescue incorporates the existence of MHC-I peptide motifs to rescore peptides from ligandome data. The tool is demonstrated here using peptides assigned from LC-MS/MS data with PEAKs software but can be deployed on data from any search algorithm. This new approach increased the number of peptides identified by up to 20-30% and promises to aid the discovery of novel MHC-I ligands with immunotherapeutic potential
- …
