- Volume 81, Issue 6, 2000
Volume 81, Issue 6, 2000
- Plant
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The GCD10 subunit of yeast eIF-3 binds the methyltransferase-like domain of the 126 and 183 kDa replicase proteins of tobacco mosaic virus in the yeast two-hybrid system
More LessThe tobacco mosaic virus (TMV) replicase complex contains virus- and host-encoded proteins. In tomato, one of these host proteins was reported previously to be related serologically to the GCD10 subunit of yeast eIF-3. The yeast two-hybrid system has now been used to show that yeast GCD10 interacts selectively with the methyltransferase domain shared by the 126 and 183 kDa TMV replicase proteins. These findings are consistent with a role for a GCD10-like protein in the TMV replicase complex and suggest that, in TMV-infected cells, the machinery of virus replication and protein synthesis may be closely connected.
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- Other Agents
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Characterization of the murine BSE infectious agent
Bovine spongiform encephalopathy (BSE) is a prion-associated disease where the infectious agent is thought to be a host-encoded protein with a protease-resistant conformation (PrPSc). Here, data are presented on the solubilization of purified murine BSE material, using guanidine–HCl as a denaturing agent. This treatment led to loss of infectivity, which was partially recovered on renaturation after dialysis to remove the chaotropic agent. The renatured product was then fractionated on an isopycnic sucrose-density gradient and the fractions were analysed for the presence of PrPSc, nucleic acids and infectivity. It was found that the major part of PrPSc (>90%) and the endogenous nucleic acids did not contribute towards the formation of infectious particles on renaturation. Infectivity was distributed in the top three, low-density fractions. Among these, the presence of considerable infectivity in the fraction of lowest density, with barely detectable PrPSc, is of particular interest.
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Molecular analysis of Irish sheep scrapie cases
More LessDifferent strains of transmissible spongiform encephalopathies in humans and rodent models are associated with the accumulation of PrPSc of distinct molecular characteristics. These characteristics include glycosylation profiles, fragment sizes and long-term resistance of PrPSc to proteinase K. The first objective of this study was to determine the applicability of these criteria to characterize and differentiate sheep scrapie PrPSc and bovine spongiform encephalopathy (BSE) PrPSc. PrPSc in sheep scrapie samples from Ireland had clearly distinct molecular characteristics to PrPSc in cattle BSE samples using a monoclonal antibody (MAb P4) directed to position 89–104 of ovine PrP using either brain homogenates or semi-purified scrapie-associated fibrils. Similar glycoprofiles were found when analysing scrapie PrPSc in six different CNS regions (thoracic spinal cord, thalamus, basal ganglia, mediobasal hypothalamus, medulla oblongata and cortex). While the long-term resistance results using a different monoclonal antibody (raised to ruminant PrP positions 145–163; MAb L42) were similar to the results obtained with MAb P4, different glycotyping results were obtained. Given the variation in glycosylation patterns using different antibodies, we conclude that standardization of methodology and antibodies is crucial to the applicability of molecular analysis of ruminant BSE and scrapie samples.
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- Corrigendum
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Volumes and issues
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