Responding to the Challenges of Gifted Education in Rural Communities

There are both achievement and opportunity gaps for low-income students when compared to their economically advantaged peers; and, for rural students, these gaps may be even more pronounced. In this manuscript we draw from our ongoing work in a five-year federally-funded, Jacob K. Javits grant focusing on promoting gifted education in rural schools. To address issues of under-identification of gifted students in these settings, and to investigate ways to maximize achievement, we established an alternative process for identifying gifted students in rural schools; and we created units integrating place-based pedagogy within an evidence-based curriculum model as an intervention. Finally, we discuss preliminary findings from the pilot year and first half of the second year of the study documenting success in augmenting the pool of identified students and engaging teachers in implementing the curriculum. Perhaps more importantly, we document lessons learned and more global takeaways for the field. Specifically, we discuss the influence of deficit thinking with regard to rural schooling (and subsequent recognition of gifts and talents), the risk of generalizing rural to all rural places, and the nuances of rural poverty not captured in commonly used metrics, such as Free and Reduced Lunch

Biochemical Properties of Highly Neuroinvasive Prion Strains

Infectious prions propagate from peripheral entry sites into the central nervous system (CNS), where they cause progressive neurodegeneration that ultimately leads to death. Yet the pathogenesis of prion disease can vary dramatically depending on the strain, or conformational variant of the aberrantly folded and aggregated protein, PrPSc. Although most prion strains invade the CNS, some prion strains cannot gain entry and do not cause clinical signs of disease. The conformational basis for this remarkable variation in the pathogenesis among strains is unclear. Using mouse-adapted prion strains, here we show that highly neuroinvasive prion strains primarily form diffuse aggregates in brain and are noncongophilic, conformationally unstable in denaturing conditions, and lead to rapidly lethal disease. These neuroinvasive strains efficiently generate PrPSc over short incubation periods. In contrast, the weakly neuroinvasive prion strains form large fibrillary plaques and are stable, congophilic, and inefficiently generate PrPSc over long incubation periods. Overall, these results indicate that the most neuroinvasive prion strains are also the least stable, and support the concept that the efficient replication and unstable nature of the most rapidly converting prions may be a feature linked to their efficient spread into the CNS

Strain conformation, primary structure and the propagation of the yeast prion [PSI+]

Prion proteins can adopt multiple different infectious strain conformations. Here we examine how the sequence of a prion protein affects its capacity to propagate specific conformations by exploiting our ability to create two distinct infectious conformations of the yeast [PSI(+)] prion protein Sup35p, termed Sc4 and Sc37. PNM2, a Sup35p (G58D) point mutant originally identified for its dominant interference with prion propagation, leads to rapid, recessive loss of Sc4 but does not interfere with Sc37 propagation. PNM2 destabilizes the amyloid core of Sc37 causing compensatory effects that slow prion growth but aid prion division and result in robust Sc37 propagation. In contrast, PNM2 does not affect the structure or chaperone-mediated division of Sc4, but interferes with its delivery to daughter cells. Thus, effective delivery of infectious particles during cell division is a critical and conformation-dependent step in prion inheritance