Effect of environment on biological burden during spacecraft assembly

Determining effects of environment on accumulation of biological burden on spacecraft during assembl

Biological Monitoring of the Capsule Mechanical Training Model During Assembly in the Sterilization Assembly Development Laboratory

Microbial burden sterilization assembly procedure development using rigorous monitoring progra

Human cytomegalovirus US28 facilitates cell-to-cell viral dissemination

Human cytomegalovirus (HCMV) encodes a number of viral proteins with homology to cellular G protein-coupled receptors (GPCRs). These viral GPCRs, including US27, US28, UL33, and UL78, have been ascribed numerous functions during infection, including activating diverse cellular pathways, binding to immunomodulatory chemokines, and impacting virus dissemination. To investigate the role of US28 during virus infection, two variants of the clinical isolate TB40/E were generated: TB40/E-US28(YFP) expressing a C-terminal yellow fluorescent protein tag, and TB40/E-FLAG(YFP) in which a FLAG-YFP cassette replaces the US28 coding region. The TB40/E-US28(YFP) protein localized as large perinuclear fluorescent structures at late times post-infection in fibroblasts, endothelial, and epithelial cells. Interestingly, US28(YFP) is a non-glycosylated membrane protein throughout the course of infection. US28 appears to impact cell-to-cell spread of virus, as the ΔUS28 virus (TB40/E-FLAG(YFP)) generated a log-greater yield of extracellular progeny whose spread could be significantly neutralized in fibroblasts. Most strikingly, in epithelial cells, where dissemination of virus occurs exclusively by the cell-to-cell route, TB40/E-FLAG(YFP) (ΔUS28) displayed a significant growth defect. The data demonstrates that HCMV US28 may contribute at a late stage of the viral life cycle to cell-to-cell dissemination of virus

Balancing Related Model Order Reduction Applied to Linear Controlled Evolution Equations with Lévy Noise

Otto-von-Guericke-Universität Magdeburg, Fakultät für Mathematik, Dissertation, 2016von Martin Redmann, M. Sc.Literaturverzeichnis: Blatt 177-18

Project LOBSTAQ : investigations on lobster (Homarus americanus) aquaculture, ecology and tertiary sewage treatment in controlled environmental systems

Research was based on different aspects of incorporating Homarus Americanus cultural into the multi-trophic level marine aquaculture-wastewater treatment system of the Environmental Systems laboratory at Woods Hole. Experiments were directed .toward optimizing food sources available within the system, developing designs to facilitate high density lobster growth, and elucidating the ecology of Homarus. The aquaculture-wastewater treatment system uses secondary sewage effluent or its equivalent as a nutrient source for marine phytoplankton ponds which in turn are fed into raceways containing racks of bivalves. The bivalves produce soluble nutrients used to raise macroalgae, and solid material (biodeposits) used to raise various deposit feeders. Almost all the N and over 50% of the P is removed from the wastewater by the artificial food chain.Prepared under NSF Grant GY-1154

The proteasome cap RPT5/Rpt5p subunit prevents aggregation of unfolded ricin A chain

The plant cytotoxin ricin enters mammalian cells by receptor-mediated endocytosis, undergoing retrograde transport to the endoplasmic reticulum (ER) where its catalytic A chain (RTA) is reductively separated from the holotoxin to enter the cytosol and inactivate ribosomes. The currently accepted model is that the bulk of ER-dislocated RTA is degraded by proteasomes. We show here that the proteasome has a more complex role in ricin intoxication than previously recognised, that the previously reported increase in sensitivity of mammalian cells to ricin in the presence of proteasome inhibitors simply reflects toxicity of the inhibitors themselves, and that RTA is a very poor substrate for proteasomal degradation. Denatured RTA and casein compete for a binding site on the regulatory particle of the 26S proteasome, but their fates differ. Casein is degraded, but the mammalian 26S proteasome AAA-ATPase subunit RPT5 acts as a chaperone that prevents aggregation of denatured RTA and stimulates recovery of catalytic RTA activity in vitro. Furthermore, in vivo, the ATPase activity of Rpt5p is required for maximal toxicity of RTA dislocated from the Saccharomyces cerevisiae ER. Our results implicate RPT5/Rpt5p in the triage of substrates in which either activation (folding) or inactivation (degradation) pathways may be initiated