One University Making a Difference in Graduate Education: Caring in the Online Learning Environment.

As online education gains momentum, strategies to promote student engagement, develop social presence, and create a virtual community are essential for students' successful learning. A university with a philosophy grounded in caring developed two strategies for the graduate online education setting. These two strategies intentionally promote caring for self and others as a means to foster engagement, social presence, and a vibrant online community. One strategy was online Caring Groups, that is, small groups of four to five nursing students created each semester in one of the students' required courses in the online setting. The second strategy was the creation of two Caring Connections online sites, one for master of science in nursing students and one for doctorate in education nursing students. The sites were developed external to required courses to provide support for the online students throughout the graduate programs. Each site provides an ongoing space for students and faculty to post and discuss inspirational quotes, self-care tips, music, and photographs. The online Caring Groups and Caring Connections sites will be described, including how they were created, how they are used by students, how faculty support students, lessons learned, and how Caring Groups are integrated into the curriculum.

A mentor-protégé program for new faculty, part I: stories of protégés.

With the projected shortage of nursing faculty, formalized programs are needed to provide mentorship programs that will encourage and support faculty as they move from the role of novice to expert educator. The purpose of this qualitative study is to explore the experience of protégés participating in a mentorship program for novice faculty. An interpretive phenomenological research study was conducted to illuminate the meaning of the experiences of the protégés participating in the program. The study of the experience of protégés participating in a mentor-protégé program led to the emergence of three main themes: Creating a Meaningful Mentor-Protégé Relationship, Transitioning as a New Nurse Educator, and the Mentor-Protégé Program-Lessons Learned. Data from the study will provide insight into the meaning of receiving mentorship in the role of novice nurse educator.

A mentor-protégé program for new faculty, Part II: Stories of mentors.

Mentorship has been identified as an influential factor in retaining new nursing faculty. A mentor-protégé program for novice faculty was implemented to promote development of the protégés in their role as nurse educators. A qualitative research study conducted to illuminate the meaning of experiences of mentors led to the emergence of four patterns: The Significance of the Mentor-Protégé Relationship, Communication as Important Between Mentor and Protégé, The Mentor-Protégé Program-Protégé's Perspectives, and The Mentoring Role as Expert Educator. The data from the study support the significance of providing mentorship to novice or new nurse educators. The data suggest that mentors benefit from participation in a mentor-protégé program as much as the protégés. Similar programs are needed in nursing if we are to mentor and encourage faculty to begin and remain in the role of educators to combat the future nurse educator shortage.

Interaction domains of the UL16 and UL21 tegument proteins of herpes simplex virus.

The UL16 protein of herpes simplex virus is capsid associated and was previously identified as a binding partner of the membrane-associated UL11 tegument protein (J. S. Loomis, R. J. Courtney, and J. W. Wills, J. Virol. 77:11417-11424, 2003). In those studies, a less-prominent, approximately 65-kDa binding partner of unknown identity was also observed. Mass spectrometry studies have now revealed this species to be UL21, a tegument protein that has been implicated in the transport of capsids in the cytoplasm. The validity of the mass spectrometry results was tested in a variety of coimmunoprecipitation and glutathione S-transferase pull-down experiments. The data revealed that UL21 and UL16 can form a complex in the absence of other viral proteins, even when the assays used proteins purified from Escherichia coli. Moreover, UL11 was able to pull down UL21 only when UL16 was present, suggesting that all three proteins can form a complex. Deletion analyses revealed that the second half of UL21 (residues 268 to 535) is sufficient for the UL16 interaction and packaging into virions; however, attempts to map a subdomain of UL16 were largely unsuccessful, with only the first 40 (of 373) residues being found to be dispensable. Nevertheless, it is clear that UL16 must have two distinct binding sites, because covalent modification of its free cysteines with N-ethylmaleimide blocked binding to UL11 but not UL21. These findings should prove useful for elucidating the molecular machinery used to transmit a signal into a virion when it attaches to cells, a recently discovered mechanism in which UL16 is a central player.

Genetic Studies of the beta-hairpin loop of Rous sarcoma virus capsid protein.

The first few residues of the Rous sarcoma virus (RSV) CA protein comprise a structurally dynamic region that forms part of a Gag-Gag interface in immature virus particles. Dissociation of this interaction during maturation allows refolding and formation of a beta-hairpin structure important for assembly of CA monomers into the mature capsid shell. A consensus binding site for the cellular Ubc9 protein was previously identified within this region, suggesting that binding of Ubc9 and subsequent small ubiquitin-like modifier protein 1 (SUMO-1) modification of CA may play a role either in regulating the assembly activity of CA in immature particles or mature cores or in controlling postentry function(s) during the establishment of infection. In the present study, mutations designed to eliminate the consensus binding site were used to dissect the potentially overlapping functions of these residues. The resulting replication defects could not be traced to a failure to form particles of normal composition but, rather, to a deficit in genome replication. Genetic suppressors of two detrimental beta-hairpin mutations improved infectivity without restoring the consensus site or creating a novel one elsewhere. Optimal restoration of infectivity to a Lys-to-Arg mutant required a combination of secondary changes, one on the surface of each domain of CA. Rather than arguing for a critical role of Ubc9 and SUMO in RSV replication, these findings provide strong support for a structural role of the N-terminal residues and a particularly striking example of long-range interactions between regions of CA in achieving a functional core competent for genome replication.

Lysines close to the Rous sarcoma virus late domain critical for budding.

The release of retroviruses from the plasma membrane requires host factors that are believed to be recruited to the site of budding by the late (L) domain of the virus-encoded Gag protein. The L domain of Rous sarcoma virus (RSV) has been shown to interact with a ubiquitin (Ub) ligase, and budding of this virus is dependent on Ub. RSV is similar to other retroviruses in that it contains approximately 100 molecules of Ub, but it is unique in that none of these molecules has been found to be conjugated to Gag. If transient ubiquitination of RSV Gag is required for budding, then replacement of the target lysine(s) with arginine should prevent the addition of Ub and reduce budding. Based on known sites of ubiquitination in other viruses, the important lysines would likely reside near the L domain. In RSV, there are five lysines located just upstream of the L domain in a region of the matrix (MA) protein that is dispensable for membrane binding, and replacement of these with arginine (mutant 1-5KR) reduced budding 80 to 90%. The block to budding was found to be on the plasma membrane; however, the few virions that were released had normal size, morphology, and infectivity. Budding was restored when any one of the residues was changed back to lysine or when lysines were inserted in novel positions, either within this region of MA or within the downstream p10 sequence. Moreover, the 1-5KR mutant could be rescued into particles by coexpression of budding-competent Gag molecules. These data argue that the phenotype of mutant 1-5KR is not due to a conformational defect. Consistent with the idea that efficient budding requires a specific role for lysines, human T-cell leukemia virus type 1, which does not bud well compared to RSV and lacks lysines close to its L domain, was found to be released at a higher level upon introduction of lysines near its L domain. This report strongly supports the hypothesis that ubiquitination of the RSV Gag protein (and perhaps those of other retroviruses) is needed for efficient budding.