74 research outputs found

    Progress toward the production of transgenic grapevines by Agrobacterium-mediated transformation

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    Grape possesses the basic prerequisites for Agrobacterium-mediated transformation it is a host for Agrobacterium and plant regeneration can be induced from cultured grape explants. Leaf explants were cocultivated with disarmed Agrobacterium vectors carrying kanamycin resistance and GUS genes and cultured on shoot-inducing medium containing kanamycin. After 21 d, intense and sharply-defined blue regions were observed, including some blue organized meristematic structures, consistent with plant-driven GUS gene expression. No GUS activity was detected in control explants. Among single leaf tips excised from over 200 regenerated shoots, one was GUS positive. The recovery of transgenic shoots might be improved by increasing the frequency or modifying the site of transformation and/or regeneration

    The Interferon Response Inhibits HIV Particle Production by Induction of TRIM22

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    Treatment of human cells with Type 1 interferons restricts HIV replication. Here we report that the tripartite motif protein TRIM22 is a key mediator. We used transcriptional profiling to identify cellular genes that were induced by interferon treatment and identified TRIM22 as one of the most strongly up-regulated genes. We confirmed, as in previous studies, that TRIM22 over-expression inhibited HIV replication. To assess the role of TRIM22 expressed under natural inducing conditions, we compared the effects of interferon in cells depleted for TRIM22 using RNAi and found that HIV particle release was significantly increased in the knockdown, implying that TRIM22 acts as a natural antiviral effector. Further studies showed that TRIM22 inhibited budding of virus-like particles containing Gag only, indicating that Gag was the target of TRIM22. TRIM22 did not block the release of MLV or EIAV Gag particles. Inhibition was associated with diffuse cytoplasmic staining of HIV Gag rather than accumulation at the plasma membrane, suggesting TRIM22 disrupts proper trafficking. Mutational analyses of TRIM22 showed that the catalytic amino acids Cys15 and Cys18 of the RING domain are required for TRIM22 antiviral activity. These data disclose a pathway by which Type 1 interferons obstruct HIV replication
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