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Fourteen polymorphic microsatellite DNA markers derived from the draft genome sequence of Rhizoctonia solani anastomosis group 3 (AG-3), strain Rhs 1AP, were designed and characterized from the potato-infecting soil fungus R. solani AG-3. All loci were polymorphic in two field populations collected from Solanum tuberosum and S. phureja in the Colombian Andes. The total number of alleles per locus ranged from two to seven, while gene diversity (expected heterozygosity) varied from 0.11 to 0.81. Considering the variable levels of genetic diversity observed, these markers should be useful for population genetic analyses of this important dikaryotic fungal pathogen on a global scale. [ABSTRACT FROM AUTHOR]

The in vitro effect of Praziquantel (PZQ) on Taenia solium cysticerci was analyzed. The oxygen consumption rate of the parasites was inhibited and the release of proteins was enhanced, but no statistically significant differences were found between the control group and the experimental groups. The drug had a significant, dose-dependent negative effect on the evagination ability of the larvae; 50% effect was seen at concentrations of between 10 and 10 M PZQ. The drug also induced morphological disturbances in the tegument of the worm and of the bladder wall. Finally, a very drastic effect was the induction of spastic paralysis in evaginated cysticerci at high drug doses and of flaccid paralysis at lower PZQ concentrations. The dose inducing these effects was various orders of magnitude lower than that inhibiting the evagination ability of intact cysts. Moreover, the latter effect was reversible after had been washed out the drug and the parasites had been cultured. We suggest that PZQ alters the Ca flux in T. solium as it does in other helminths. Furthermore, we corroborated the protective role of the bladder for the invaginated worm. Finally, we think that in vivo the drug must act synergistically with the immune system components so as to eliminate the parasite. [ABSTRACT FROM AUTHOR]

Ubiquitylation of receptor tyrosine kinases plays a critical role in regulating the trafficking and lysosomal degradation of these important signaling molecules. We identified the multidomain scaffolding protein intersectin 1 (ITSN1) as an important regulator of this process (N. P. Martin et al., Mol. Pharmacol. 70:1463-1653, 2006) ITSN1 stimulates ubiquitylation of the epidermal growth factor receptor (EGFR) through enhancing the activity of the Cbl E3 ubiquitin ligase. However, the precise mechanism through which ITSN1 enhances Cbl activity was unclear. In this study, we found that ITSN1 enhances Cbl activity through disrupting the interaction of Cbl with the Sprouty2 (Spry2) inhibitory protein. We demonstrate that ITSN1 binds Pro-rich regions in both Cbl and Spry2 and that interaction of ITSN1 with Spry2 disrupts Spry2-Cbl interaction, resulting in enhanced ubiquitylation of the EGFR. Disruption of ITSN1 binding to Spry2 through point mutation of the Pro-rich ITSN1 binding site in Spry2 results in enhanced Cbl-Spry2 interaction and inhibition of receptor ubiquitylation. This study demonstrates that ITSN1 enhances Cbl activity by modulating the interaction of Cbl with Spry2. In addition, our results reveal a new level of complexity in the regulation of Cbl through the interaction with ITSN1 and Spry2.