82 research outputs found

    Correction: The Genomes of the Fungal Plant Pathogens <i>Cladosporium fulvum</i> and <i>Dothistroma septosporum</i> Reveal Adaptation to Different Hosts and Lifestyles But Also Signatures of Common Ancestry

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    <p>Correction: The Genomes of the Fungal Plant Pathogens <i>Cladosporium fulvum</i> and <i>Dothistroma septosporum</i> Reveal Adaptation to Different Hosts and Lifestyles But Also Signatures of Common Ancestry</p

    Modulation of <i>Anopheles stephensi</i> Gene Expression by Nitroquine, an Antimalarial Drug against <i>Plasmodium yoelii</i> Infection in the Mosquito

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    <div><p>Background</p><p>Antimalarial drugs may impact mosquito’s defense against <i>Plasmodium</i> parasites. Our previous study showed nitroquine significantly reduced infection of <i>Anopheles stephensi</i> by <i>Plasmodium yoelii</i>, but the underlying mechanism remains unclear. In order to understand how transmission capacity of <i>An. stephensi</i> was affected by nitroquine, we explored the transcriptome of adult females after different treatments, examined changes in gene expression profiles, and identified transcripts affected by the drug and parasite.</p><p>Methodology/Principal Findings</p><p>We extended massively parallel sequencing and data analysis (including gene discovery, expression profiling, and function prediction) to <i>An. stephensi</i> before and after Plasmodium infection with or without nitroquine treatment. Using numbers of reads assembled into specific contigs to calculate relative abundances (RAs), we categorized the assembled contigs into four groups according to the differences in RA values infection induced, infection suppressed, drug induced, and drug suppressed. We found both nitroquine in the blood meal and <i>Plasmodium</i> infection altered transcription of mosquito genes implicated in diverse processes, including pathogen recognition, signal transduction, prophenoloxidase activation, cytoskeleton assembling, cell adhesion, and oxidative stress. The differential gene expression may have promoted certain defense responses of <i>An. stephensi</i> against the parasite and decreased its infectivity.</p><p>Conclusions/Significance</p><p>Our study indicated that nitroquine may regulate several immune mechanisms at the level of gene transcription in the mosquito against <i>Plasmodium</i> infection. This highlights the need for better understanding of antimalarial drug’s impact on parasite survival and transmission. In addition, our data largely enriched the existing sequence information of <i>An. stephensi</i>, an epidemiologically important vector species.</p></div

    Figure 6

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    <p>Cell numbers on the different scaffolds of different mix ratio of designer PRG and pure RADA16 scaffolds after 1-week culture. There is an increase in proliferation following the increase PRG % scaffold when increased from 0 to 40%. There was a decrease in cell proliferation at PRG 100% suggesting that there is an optimal ratio of PRG and RADA16 scaffolds.</p

    Temperatures induced d-EAK16 and l-EAK16 structural transition.

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    <p>d-EAK16 and l-EAK16 were incubated at 110°C and cooled to 25°C and the cycles were repeated 3 times. A) The d-EAK16 formed stable beta-sheets when measured at 25°C. The d-EAK16 underwent two-phase transitions when elevated at 110°C, from beta-sheet to alpha-helix. The figure insert is the time-dependence of d-EAK16 structural transition. The structural transition occurred in 3 stages. After first incubation, the beta-sheet became less stable and showed signs of structural change. After second incubation, it abruptly converted from a beta-sheet to an alpha-helix. After third and prolonged incubation, no significant change for alpha-helix was observed. B) The l-EAK16 stayed as a stable beta-sheet. No abrupt structural transition was observed for l-EAK16 even when temperature was elevated to 110°C. The insert is the time-dependence of l-EAK16 structural transition.</p

    Comparison of structural behaviors of d-EAK16 and l-EAK16.

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    <p>Although both peptides have identical sequences, their chiral amino acids are mirror images. In l-EAK, there was no obvious structural change at 110°C and return to 25°C (red and blue). On the other hand, d-EAK16 exhibited drastic structural change at 110°C and back to 25°C. Initially at 25°C, it had a beta-sheet structure (green spectrum); however, after heating, it converted to typical alpha-helix structure and remained stable even after cooling to 25°C (black spectrum).</p

    Designer self-assembling peptides used in this study.

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    <p>The sequences are from N→C. Ac  =  acetylated N-termini, -CONH<sub>2</sub>  =  amidated C-termini. The peptide motif souces from various protein origins.</p

    Location of gene models of <i>C. fulvum</i> in regions syntenic or non-syntenic with the <i>D. septosporum</i> genome.

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    a<p>Values are numbers of gene models located in regions of the <i>C. fulvum</i> genome syntenic or non-syntenic with the <i>D. septosporum</i> genome as described in Materials and Methods.</p>b<p>For all proteins the percentage of gene models represents the fraction of all gene models present in the <i>C. fulvum</i> genome; for other categories (BDBH, secreted proteins, secreted Cys-rich proteins) the percentage of gene models represents the fraction of gene models present in syntenic and non-syntenic regions.</p>c<p>All proteins encoded by predicted gene models in the <i>C. fulvum</i> genome.</p>d<p>Bi-directional best BLAST hit between <i>C. fulvum</i> and <i>D. septosporum</i> proteins with at least 50% (global) pairwise amino acid similarity and at least 60% coverage by overlap-corrected blastp HSPs.</p>e<p>Gene models predicted to encode secreted proteins.</p>f<p>Secreted small cysteine-rich proteins contain less than 300 amino acids of which at least four are cysteines.</p>g<p>The mean amino acid similarities of all protein gene models in syntenic regions and non-syntenic regions are 85.2% and 65.1%, respectively.</p>h<p>The mean amino acid similarities of secreted protein gene models in syntenic regions and non-syntenic regions are 81.1% and 60.7%, respectively.</p

    Phase diagrams of MO-based systems with differing A<sub>6</sub>D (A) and KA<sub>6</sub> content (B), respectively.

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    <p>The structural investigations were carried out for <i>R</i> values in the range of 0–0.2. The Pn3m phase regions in these diagrams have been highlighted in light grey and approximate phase boundaries are depicted. The lattice parameter values, <i>a</i>, for some of the Pn3m (•) and H<sub>2</sub> (O) phases are given in Ångstrøms.</p

    Organization of repeats and pathogenicity-related genes in the <i>Dothistroma septosporum</i> genome.

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    <p>The fourteen chromosomes from the <i>D. septosporum</i> genome assembly are shown as GC (dark grey line) and AT (pale grey line) content (%) plots made from a 500-bp sliding window using Geneious (<a href="http://www.geneious.com" target="_blank">www.geneious.com</a>). All chromosomes have telomere sequence at both ends except chromosomes 2, 11 and 14 which have telomere sequences only at the left end as shown in the figure. Chromosome 1 has been split into two parts in the figure (L, R) because of its length, and the GC/AT content scale is shown beside the right arm of this chromosome. The positions of putative <i>Avr</i> and <i>Ecp</i> effector, secondary metabolite, dothistromin biosynthesis, and mating type genes are shown above the GC/AT content plot, while the positions of repeats (>200-bp) are shown below the plot. Color-coding of the gene and repeat types is indicated in the legend. Most chromosomes have repeat clusters at one or two sites that coincide with regions of high AT content. The chromosome sizes are to scale, as indicated by the vertical pale grey lines, with the values (in kb) shown at the bottom; neither the genes nor the repeats are drawn to scale.</p
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