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Galloway, R.

Publications and source records attributed to Galloway, R..

2 recordsLinked to original sources

Pathogenic Leptospira are widespread in the urban wildlife of southern California

Leptospirosis is the most widespread zoonotic disease in the world, yet it is broadly understudied in multi-host wildlife systems. Knowledge gaps regarding Leptospira circulation in wildlife, particularly in densely populated areas, contribute to frequent misdiagnoses in humans and domestic animals. We assessed Leptospira prevalence levels and risk factors in five target wildlife species across the greater Los Angeles region: striped skunks (Mephitis mephitis), Northern raccoons (Procyon lotor), coyotes (Canis latrans), Virginia opossums (Didelphis virginiana), and fox squirrels (Sciurus niger). We sampled more than 960 individual animals, including over 700 from target species in the greater Los Angeles region, and an additional 260 sampled opportunistically from other regions and species. In the five target species, seroprevalences ranged from 5-60% and active infection prevalences ranged from 0.8-15.2% in all except fox squirrels (0%). Patterns of serologic reactivity suggest that mainland terrestrial wildlife, particularly mesocarnivores, could be the source of repeated observed introductions of Leptospira into local marine and island ecosystems. Overall, we found evidence of widespread Leptospira exposure in wildlife across Los Angeles and surrounding regions. This indicates exposure risk for humans and domestic animals and highlights that this pathogen can circulate endemically in many wildlife species even in densely populated urban areas.

ecology↗

Methods for the Refolding of Disulfide-Rich Proteins.

Eschericia coli remains the workhorse producing recombinant proteins given its ease of handling, access and genetic manipulation using standard laboratory techniques. However, disulfide-rich proteins can be difficult to produce in E. coli, in large part due to the reducing environment of the bacterial cytoplasm. Refolding from insoluble inclusion bodies can be a viable strategy for generating substantial quantities of disulfide-rich protein. For the best chance of successfully refolding a protein, it is vital to carry out a variety of small-scale test refolds under a swathe of conditions including altering the concentration of urea, salts, reduced and oxidized glutathione, temperature, length of refold time and protein dilution factor. Once a protein has undergone refolding it is vital to determine that the final product is natively folded given the chance of soluble misfolded protein. For determination of correct folding, a variety of techniques can be employed, and ideally, numerous should be used together. For proteins that possess enzymatic function the gold standard to assess correct folding is an activity assay. Non-enzymatic proteins can be assessed using a combination of circular dichroism and nuclear magnetic resonance spectroscopy. These techniques should be utilized alongside mass spectrometry, Western blotting and SDS-PAGE.

biochemistry↗