Discovering The Potential Of Service Learning In Perugia, Italy: An Evaluation Of The Umbra Institute’s La Famiglia Italiana Project

Today, American study abroad programs are increasingly shifting their focus to students’ community engagement efforts, one approach of which is service learning (Stone, 2008). Service learning principles and approach, however, are not always quickly and easily transported into other cultures. As an American pedagogical export, service learning in the study abroad context has the potential to overlook essential factors such as reciprocity, sustainability, and evaluation of student, faculty, and community partner experiences. This type of learning remains unexplored territory in many countries including Italy (Tosi, 2000). As the only American study abroad program of its kind in Perugia, Italy, The Umbra Institute provided an ideal case study to research the integration of service learning into a local Italian community. The following research explores how The Umbra Institute service learning program entitled La Famiglia Italiana Project (The Italian Family Project) can best meet the needs and expectations of American college students and Italian family community partners while preserving partner reciprocity and program sustainability. The findings are comprised of results from four research groups. Group 1 consists of past Italian family participant phone and in-person interviews; Group 2 includes data from past Umbra Institute student participant electronic evaluations; Group 3 contains current student and Italian family participant in-person interviews; Group 4 consists of in-person interviews with The Umbra Institute faculty and staff member responsible for the La Famiglia Italiana Project. The research reveals that initial program expectations were higher for students than Italian families; the language was less of a hindrance for families than for students; students preferred more guidance before and during the program, while families preferred more guidance before or during the first meeting; and nearly all participants would recommend the program and identified educational value regardless of perceived challenges or unmet expectations

STEM Principal Investigators Perceptions and Practice of Broader Impacts: Front-end report for the Center for the Advancement of Informal Science Education

The analysis contained in this report is a result of work conducted in October 2013 by Julie Risien and John Falk of the Center for Research on Lifelong STEM Learning located at Oregon State University. This undertaking should not be considered research, but an exercise intended to provide insights that may enhance the outcomes of the CAISE Broader Impacts and Informal Science Education Year 7 Convening

Redefining Undergraduate Success at Oregon State University: Report from Spring 2014 Invitational Workshop

On April 7, 2014 the Center for Research on Lifelong STEM Learning and the Office of the Associate Provost for Academic Success and Engagement1 launched the Undergraduate Success Initiative with an invitational workshop entitled Redefining Undergraduate Success. A small planning team convened a group of 32 faculty and administrators with a wide array of perspectives and experiences. The goal of the workshop was to define “success” or “derived benefits” of an undergraduate OSU experience, a definition that will form the foundation for a comprehensive framework that ties student outcomes with OSU facilitated experiences within and outside of classrooms and laboratories. Ultimately, this report will serve as the basis for a well-reasoned and supported research agenda that will directly contribute to understanding and measurably improving student success. The research agenda will be part of an overarching initiative to reform undergraduate education at OSU through design-based implementation of evidence-based educational and learning practices at OSU

West Nile virus methyltransferase domain interacts with protein kinase G

Background: The flaviviral nonstructural protein 5 (NS5) is a phosphoprotein, though the precise identities and roles of many specific phosphorylations remain unknown. Protein kinase G (PKG), a cGMP-dependent protein kinase, has previously been shown to phosphorylate dengue virus NS5. Methods: We used mass spectrometry to specifically identify NS5 phosphosites. Co-immunoprecipitation assays were used to study protein-protein interactions. Effects on viral replication were measured via replicon system and plaque assay titering. Results: We identified multiple sites in West Nile virus (WNV) NS5 that are phosphorylated during a WNV infection, and showed that the N-terminal methyltransferase domain of WNV NS5 can be specifically phosphorylated by PKG in vitro. Expressing PKG in cell culture led to an enhancement of WNV viral production. We hypothesized this effect on replication could be caused by factors beyond the specific phosphorylations of NS5. Here we show for the first time that PKG is also able to stably interact with a viral substrate, WNV NS5, in cell culture and in vitro. While the mosquito-borne WNV NS5 interacted with PKG, tick-borne Langat virus NS5 did not. The methyltransferase domain of NS5 is able to mediate the interaction between NS5 and PKG, and mutating positive residues in the αE region of the methyltransferase interrupts the interaction. These same mutations completely inhibited WNV replication. Conclusions: PKG is not required for WNV replication, but does make a stable interaction with NS5. While the consequence of the NS5:PKG interaction when it occurs is unclear, mutational data demonstrates that this interaction occurs in a region of NS5 that is otherwise necessary for replication. Overall, the results identify an interaction between virus and a cellular kinase and suggest a role for a host kinase in enhancing flaviviral replication

West Nile Virus Methyltransferase Domain Interacts with Protein Kinase

Background The flaviviral nonstructural protein 5 (NS5) is a phosphoprotein, though the precise identities and roles of many specific phosphorylations remain unknown. Protein kinase G (PKG), a cGMP-dependent protein kinase, has previously been shown to phosphorylate dengue virus NS5. Methods We used mass spectrometry to specifically identify NS5 phosphosites. Co-immunoprecipitation assays were used to study protein-protein interactions. Effects on viral replication were measured via replicon system and plaque assay titering. Results We identified multiple sites in West Nile virus (WNV) NS5 that are phosphorylated during a WNV infection, and showed that the N-terminal methyltransferase domain of WNV NS5 can be specifically phosphorylated by PKG in vitro. Expressing PKG in cell culture led to an enhancement of WNV viral production. We hypothesized this effect on replication could be caused by factors beyond the specific phosphorylations of NS5. Here we show for the first time that PKG is also able to stably interact with a viral substrate, WNV NS5, in cell culture and in vitro. While the mosquito-borne WNV NS5 interacted with PKG, tick-borne Langat virus NS5 did not. The methyltransferase domain of NS5 is able to mediate the interaction between NS5 and PKG, and mutating positive residues in the αE region of the methyltransferase interrupts the interaction. These same mutations completely inhibited WNV replication. Conclusions PKG is not required for WNV replication, but does make a stable interaction with NS5. While the consequence of the NS5:PKG interaction when it occurs is unclear, mutational data demonstrates that this interaction occurs in a region of NS5 that is otherwise necessary for replication. Overall, the results identify an interaction between virus and a cellular kinase and suggest a role for a host kinase in enhancing flaviviral replication