Civil society organisations

There are few civil society organisations (CSOs) in Vanuatu that have a specific anti-corruption mandate, although many of them do address issues of governance more generally. CSOs face challenges due to the general issue of limited human resource capacity within Vanuatu. The geographical nature of Vanuatu also makes it difficult for NGOs to effectively and sustainably engage with communities throughout the country or to mobilise the public to demand that government is held accountable for its actions. Another issue which makes it difficult for CSOs to effectively fulfil their role within the national integrity system is that there is no forum within which CSOs and government can engage. Internal governance mechanisms are variable, and very much depend upon the individual CSO. This is another area which needs strengthening across the entire CSO sector

High resolution crystal structure of the Endo-N-acetyl-beta-D-glucosaminidase responsible for the deglycosylation of hypocrea jecorina cellulases

Endo-N-acetyl-beta-D-glucosaminidases (ENGases) hydrolyze the glycosidic linkage between the two N-acetylglucosamine units that make up the chitobiose core of N-glycans. The endo-N-acetyl-beta-D-glucosaminidases classified into glycoside hydrolase family 18 are small, bacterial proteins with different substrate specificities. Recently two eukaryotic family 18 deglycosylating enzymes have been identified. Here, the expression, purification and the 1.3 angstrom resolution structure of the ENGase ( Endo T) from the mesophilic fungus Hypocrea jecorina (anamorph Trichoderma reesei) are reported. Although the mature protein is C-terminally processed with removal of a 46 amino acid peptide, the protein has a complete (beta/alpha) 8 TIM-barrel topology. In the active site, the proton donor (E131) and the residue stabilizing the transition state (D129) in the substrate assisted catalysis mechanism are found in almost identical positions as in the bacterial GH18 ENGases: Endo H, Endo F1, Endo F3, and Endo BT. However, the loops defining the substrate-binding cleft vary greatly from the previously known ENGase structures, and the structures also differ in some of the alpha-helices forming the barrel. This could reflect the variation in substrate specificity between the five enzymes. This is the first three-dimensional structure of a eukaryotic endo-N-acetyl-beta-D-glucosaminidase from glycoside hydrolase family 18. A glycosylation analysis of the cellulases secreted by a Hypocrea jecorina Endo T knock-out strain shows the in vivo function of the protein. A homology search and phylogenetic analysis show that the two known enzymes and their homologues form a large but separate cluster in subgroup B of the fungal chitinases. Therefore the future use of a uniform nomenclature is proposed

How Do Communities Use a Participatory Public Health Approach to Build Resilience? The Los Angeles County Community Disaster Resilience Project.

Community resilience is a key concept in the National Health Security Strategy that emphasizes development of multi-sector partnerships and equity through community engagement. Here, we describe the advancement of CR principles through community participatory methods in the Los Angeles County Community Disaster Resilience (LACCDR) initiative. LACCDR, an initiative led by the Los Angeles County Department of Public Health with academic partners, randomized 16 community coalitions to implement either an Enhanced Standard Preparedness or Community Resilience approach over 24 months. Facilitated by a public health nurse or community educator, coalitions comprised government agencies, community-focused organizations and community members. We used thematic analysis of data from focus groups (n = 5) and interviews (n = 6 coalition members; n = 16 facilitators) to compare coalitions' strategies for operationalizing community resilience levers of change (engagement, partnership, self-sufficiency, education). We find that strategies that included bidirectional learning helped coalitions understand and adopt resilience principles. Strategies that operationalized community resilience levers in mutually reinforcing ways (e.g., disseminating information while strengthening partnerships) also secured commitment to resilience principles. We review additional challenges and successes in achieving cross-sector collaboration and engaging at-risk groups in the resilience versus preparedness coalitions. The LACCDR example can inform strategies for uptake and implementation of community resilience and uptake of the resilience concept and methods

A Salmonella virulence factor activates the NOD1/NOD2 signaling pathway.

The invasion-associated type III secretion system (T3SS-1) of Salmonella enterica serotype Typhimurium (S. Typhimurium) activates the transcription factor NF-κB in tissue culture cells and induces inflammatory responses in animal models through unknown mechanisms. Here we show that bacterial delivery or ectopic expression of SipA, a T3SS-1-translocated protein, led to the activation of the NOD1/NOD2 signaling pathway and consequent RIP2-mediated induction of NF-κB-dependent inflammatory responses. SipA-mediated activation of NOD1/NOD2 signaling was independent of bacterial invasion in vitro but required an intact T3SS-1. In the mouse colitis model, SipA triggered mucosal inflammation in wild-type mice but not in NOD1/NOD2-deficient mice. These findings implicate SipA-driven activation of the NOD1/NOD2 signaling pathway as a mechanism by which the T3SS-1 induces inflammatory responses in vitro and in vivo

Traumatic Endophthalmitis due to Cellulosimicrobium cellulans

Purpose. To report a case of traumatic endophthalmitis due to Cellulosimicrobium cellulans. Design. Case report. Methods. Retrospective chart review. Results. To our knowledge, this is the first report of traumatic endophthalmitis due to C. cellulans, which did not respond to intravitreal antibiotics or repeat vitrectomy and ultimately led to the discovery of an occult intraocular foreign body. Conclusions. C. cellulans is a rare cause of endophthalmitis. Greater awareness of this bacterium in the ophthalmic literature as a cause of endophthalmitis and its association with foreign bodies may allow earlier and more purposeful intervention in future cases

Characterization of DNA binding, transcriptional activation, and regulated nuclear association of recombinant human NFATp

BACKGROUND: NFATp is one member of a family of transcriptional activators whose nuclear accumulation and hence transcriptional activity is regulated in mammalian cells. Human NFATp exists as a phosphoprotein in the cytoplasm of naive T cells. Upon antigen stimulation, NFATp is dephosphorylated, accumulates in nuclei, and functions to regulate transcription of genes including those encoding cytokines. While the properties of the DNA binding domain of NFATp have been investigated in detail, biochemical studies of the transcriptional activation and regulated association with nuclei have remained unexplored because of a lack of full length, purified recombinant NFATp. RESULTS: We developed methods for expressing and purifying full length recombinant human NFATp that has all of the properties known to be associated with native NFATp. The recombinant NFATp binds DNA on its own and cooperatively with AP-1 proteins, activates transcription in vitro, is phosphorylated, can be dephosphorylated by calcineurin, and exhibits regulated association with nuclei in vitro. Importantly, activation by recombinant NFATp in a reconstituted transcription system required regions of the protein outside of the central DNA binding domain. CONCLUSIONS: We conclude that NFATp is a bona fide transcriptional activator. Moreover, the reagents and methods that we developed will facilitate future studies on the mechanisms of transcriptional activation and nuclear accumulation by NFATp, a member of an important family of transcriptional regulatory proteins

Imagining a Future in PreK: How Professional Identity Shapes Notions of Early Mathematics

Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/110548/1/aeq12086.pd