Redefining the Service Experience: Forging Collaboration Between Librarians and Students

In response to changing pedagogical theory and practice in higher education, library designers have created innovative learning spaces that support informal learning outside the classroom. Informed by social constructivist theory, libraries can be justly proud of their new collaborative learning spaces that support interaction and discussion; social spaces that foster engagement and learning; as well as quiet places for independent study. The University of Melbourne Library is no exception, carrying out a program of works since 2007 to create dynamic and innovative spaces to support contemporary student learning in four successive library refurbishment projects. Although much attention has been paid to redeveloping student spaces in libraries, less attention has been paid to the interrelationship between library spaces and services and how this interrelationship and the pedagogical framework should jointly inform these redevelopments. It seems incongruous to redevelop student spaces to meet new pedagogical imperatives without rethinking the service experience, in particular the relationship between library staff and students, the model of service provision and the physical design of the service area. This paper focuses on the development of a new service model that is specifically designed to meet the needs of contemporary users at the University of Melbourne Library. In particular, the paper reflects upon the way in which the service desk has been transformed from a forbidding counter-style barrier that formalised the traditional expert/student relationship to a service area where librarians stand side by side with patrons, where the emphasis is on partnering and collaborating with students and researchers. The development of this model represents an attempt to re-define the relationship between librarians and students in line with current pedagogical practice. Underpinning this service model is a complex program of workforce change, professional development and service refinement to ensure that staff at service points are able to deliver quality services that meet students’ changing information needs

Tagore Pedagogy and Visual Cultures

The Tagore, Pedagogy and Contemporary Visual Cultures network brings together a group of leading international academics and visual arts practitioners to discuss and explore the legacy and continuing relevance of Indian poet and polymath Rabindranath Tagore (1861-1941) for contemporary art practice and visual culture. The group, made up of artists, curators and cultural theorists from Europe and India, has come together because they share an interest in exploring Tagore’s legacy and influence from different disciplinary backgrounds, often taking unorthodox approaches in order to think outside of the established conventions of Tagore scholarship. Tagore Pedagogy and Contemporary Visual Cultures is Directed by Andrea Phillips in collaboration with Grant Watson, Curator at Iniva. The project is funded by an AHRC International Network Grant

Giardia Cyst Wall Protein 1 Is a Lectin That Binds to Curled Fibrils of the GalNAc Homopolymer

The infectious and diagnostic stage of Giardia lamblia (also known as G. intestinalis or G. duodenalis) is the cyst. The Giardia cyst wall contains fibrils of a unique β-1,3-linked N-acetylgalactosamine (GalNAc) homopolymer and at least three cyst wall proteins (CWPs) composed of Leu-rich repeats (CWPLRR) and a C-terminal conserved Cys-rich region (CWPCRR). Our goals were to dissect the structure of the cyst wall and determine how it is disrupted during excystation. The intact Giardia cyst wall is thin (~400 nm), easily fractured by sonication, and impermeable to small molecules. Curled fibrils of the GalNAc homopolymer are restricted to a narrow plane and are coated with linear arrays of oval-shaped protein complex. In contrast, cyst walls of Giardia treated with hot alkali to deproteinate fibrils of the GalNAc homopolymer are thick (~1.2 µm), resistant to sonication, and permeable. The deproteinated GalNAc homopolymer, which forms a loose lattice of curled fibrils, is bound by native CWP1 and CWP2, as well as by maltose-binding protein (MBP)-fusions containing the full-length CWP1 or CWP1LRR. In contrast, neither MBP alone nor MBP fused to CWP1CRR bind to the GalNAc homopolymer. Recombinant CWP1 binds to the GalNAc homopolymer within secretory vesicles of Giardia encysting in vitro. Fibrils of the GalNAc homopolymer are exposed during excystation or by treatment of heat-killed cysts with chymotrypsin, while deproteinated fibrils of the GalNAc homopolymer are degraded by extracts of Giardia cysts but not trophozoites. These results show the Leu-rich repeat domain of CWP1 is a lectin that binds to curled fibrils of the GalNAc homopolymer. During excystation, host and Giardia proteases appear to degrade bound CWPs, exposing fibrils of the GalNAc homopolymer that are digested by a stage-specific glycohydrolase. Author SummaryWhile the walls of plants and fungi contain numerous sugar homopolymers (cellulose, chitin, and β-1,3-glucans) and dozens of proteins, the cyst wall of Giardia is relatively simple. The Giardia wall contains a unique homopolymer of β-1,3-linked N-acetylgalactosamine (GalNAc) and at least three cyst wall proteins (CWPs), each of which is composed of Leu-rich repeats and a C-terminal Cys-rich region. The three major discoveries here are: 1) Fibrils of the GalNAc homopolymer are curled and form a lattice that is compressed into a narrow plane by bound protein in intact cyst walls. 2) Leu-rich repeats of CWP1 form a novel lectin domain that is specific for fibrils of the GalNAc homopolymer, which can be isolated by methods used to deproteinate fungal walls. 3) A cyst-specific glycohydrolase is able to degrade deproteinated fibrils of the GalNAc homopolymer. We incorporate these findings into a new curled fiber and lectin model of the intact Giardia cyst wall and a protease and glycohydrolase model of excystation.National Institutes of Health (AI048082, AI44070, GM31318, RR1088

MutY-Homolog (MYH) inhibition reduces pancreatic cancer cell growth and increases chemosensitivity

Patients with pancreatic ductal adenocarcinoma (PC) have a poor prognosis due to metastases and chemoresistance. PC is characterized by extensive fibrosis, which creates a hypoxic microenvironment, and leads to increased chemoresistance and intracellular oxidative stress. Thus, proteins that protect against oxidative stress are potential therapeutic targets for PC. A key protein that maintains genomic integrity against oxidative damage is MutY-Homolog (MYH). No prior studies have investigated the function of MYH in PC cells. Using siRNA, we showed that knockdown of MYH in PC cells 1) reduced PC cell proliferation and increased apoptosis; 2) further decreased PC cell growth in the presence of oxidative stress and chemotherapy agents (gemcitabine, paclitaxel and vincristine); 3) reduced PC cell metastatic potential; and 4) decreased PC tumor growth in a subcutaneous mouse model in vivo. The results from this study suggest MYH may be a novel therapeutic target for PC that could potentially improve patient outcome by reducing PC cell survival, increasing the efficacy of existing drugs and reducing metastatic spread