Development, characterisation, and deployment of the SNO+ liquid scintillator

A liquid scintillator consisting of linear alkylbenzene as the solvent and 2,5-diphenyloxazole as the fluor was developed for the SNO+ experiment. This mixture was chosen as it is compatible with acrylic and has a competitive light yield to pre-existing liquid scintillators while conferring other advantages including longer attenuation lengths, superior safety characteristics, chemical simplicity, ease of handling, and logistical availability. Its properties have been extensively characterized and are presented here. This liquid scintillator is now used in several neutrino physics experiments in addition to SNO+

The genus Piscirickettsia

The genus Piscirickettsia is part of the Piscirickettsiaceae family, belonging to the Gammaproteobacteria class within the Thiotrichales order. The family contains seven phylogenetically related genera (Cycloclasticus, Hydrogenovibrio, Sulfurivirga, Thioalkalimicrobium, Methylophaga, Thiomicrospira, and Piscirickettsia), with highly diverse characteristics, making them very different from one another. The genus Piscirickettsia comprises a single species called Piscirickettsia salmonis, a Gram-negative facultative intracellular fish pathogen that significantly affects the salmon industry. Since its first isolation in Chile in 1989, the bacterium has been reported in Norway, Scotland, Greece, Canada, and the USA, among others. To date, the complete genome sequence of P. salmonis has not been reported, and relevant aspects of its metabolism, virulence, and life cycle are still poorly understood

Staphylococcus aureus mutants lacking the LytR-CpsA-Psr family of enzymes release cell wall teichoic acids into the extracellular medium

The LytR-CpsA-Psr (LCP) proteins are thought to transfer bactoprenol-linked biosynthetic intermediates of wall teichoic acid (WTA) to the peptidoglycan of Gram-positive bacteria. In Bacillus subtilis, mutants lacking all three LCP enzymes do not deposit WTA in the envelope, while Staphylococcus aureus Δlcp mutants display impaired growth and reduced levels of envelope phosphate. We show here that the S. aureus Δlcp mutant synthesized WTA yet released ribitol phosphate polymers into the extracellular medium. Further, Δlcp mutant staphylococci no longer restricted the deposition of LysM-type murein hydrolases to cell division sites, which was associated with defects in cell shape and increased autolysis. Mutations in S. aureus WTA synthesis genes (tagB, tarF, or tarJ2) inhibit growth, which is attributed to the depletion of bactoprenol, an essential component of peptidoglycan synthesis (lipid II). The growth defect of S. aureus tagB and tarFJ mutants was alleviated by inhibition of WTA synthesis with tunicamycin, whereas the growth defect of the Δlcp mutant was not relieved by tunicamycin treatment or by mutation of tagO, whose product catalyzes the first committed step of WTA synthesis. Further, sortase A-mediated anchoring of proteins to peptidoglycan, which also involves bactoprenol and lipid II, was not impaired in the Δlcp mutant. We propose a model whereby the S. aureus Δlcp mutant, defective in tethering WTA to the cell wall, cleaves WTA synthesis intermediates, releasing ribitol phosphate into the medium and recycling bactoprenol for peptidoglycan synthesis