Fish Eating Birds Can Spread Bacterial Diseases Between Catfish Ponds

Severe outbreaks of Motile Aeromonad Septicemia disease in commercial catfish aquaculture ponds have been associated with a virulent Aeromonas hydrophila strain (VAh) that is genetically distinct from less virulent strains. We demonstrated that Great Egrets (Arde alba), Double-crested Cormorants (Phalacrocorax auritus), American White Pelicans (Pelecanus erythrorhynchos), and Wood Storks (Mycteria americana) can carry and shed viable VAh after consuming fish infected with Vah. Edwardsiella ictaluri and E. tarda are considered the primary species of Edwardsiella to cause disease outbreaks in North American catfish aquaculture. Genetic analysis has determined that most isolates designated as E. tarda were actually a new species, E. piscicida. There has been an increase in E. piscicida diagnostic cases in recent years possibly due to an increase in hybrid (Channel x blue) catfish production. We conducted a study to determine if Great Egrets (Ardea alba) shed viable E. piscicida when fed catfish infected with the bacteria. Great Egrets fed infected fish shed viable E. piscicida bacteria for multiple days, (Table 1), after last consuming infected fish on day 2 of the study. Great Egrets in the control group did not shed the bacteria. Given that Great Egrets can shed viable E. piscicida after consuming diseased fish, we hypothesize that they could also serve as a reservoir for E. piscicida and could spread the pathogen while predating fish in catfish ponds. Additional research is needed to determine if this shedding could cause disease in these ponds

Using Needs Assessment to Understand Continuing Disability in Patients with Enduring Mental Illness. Implications for Considerations of Service Development

Particular strengths of the MRC Needs for Care Assessment Schedule have been used to investigate the treatment status of patients with persistent psychiatric disability in ways that other needs assessment tools are unable to. One hundred and seventy-nine such patients from three settings; a private sector psychiatric hospital, two public sector day hospitals situated in the same town, and a high security hospital, were found to have a high level of need. Although there were differences between settings, overall these needs were well met in all three. The high level of persistent disability found amongst these patients could not be attributed to failure on the part of those treating them to use the best available methods, or to failures to comply or engage with treatment on the patient's part. In some two thirds of instances persistent disability was best explained by the fact that even the most suitable available treatments have to be considered only partially effective

Time-resolved studies define the nature of toxic IAPP intermediates, providing insight for anti-amyloidosis therapeutics

Islet amyloidosis by IAPP contributes to pancreatic β-cell death in diabetes, but the nature of toxic IAPP species remains elusive. Using concurrent time-resolved biophysical and biological measurements, we define the toxic species produced during IAPP amyloid formation and link their properties to induction of rat INS-1 β-cell and murine islet toxicity. These globally flexible, low order oligomers upregulate pro-inflammatory markers and induce reactive oxygen species. They do not bind 1-anilnonaphthalene-8-sulphonic acid and lack extensive β-sheet structure. Aromatic interactions modulate, but are not required for toxicity. Not all IAPP oligomers are toxic; toxicity depends on their partially structured conformational states. Some anti-amyloid agents paradoxically prolong cytotoxicity by prolonging the lifetime of the toxic species. The data highlight the distinguishing properties of toxic IAPP oligomers and the common features that they share with toxic species reported for other amyloidogenic polypeptides, providing information for rational drug design to treat IAPP induced β-cell death

The strength of earthquake-generating faults

NERC, ESR

Using Needs Assessment to Understand Continuing Disability in Patients with Enduring Mental Illness. Implications for Considerations of Service Development

Particular strengths of the MRC Needs for Care Assessment Schedule have been used to investigate the treatment status of patients with persistent psychiatric disability in ways that other needs assessment tools are unable to. One hundred and seventy-nine such patients from three settings; a private sector psychiatric hospital, two public sector day hospitals situated in the same town, and a high security hospital, were found to have a high level of need. Although there were differences between settings, overall these needs were well met in all three. The high level of persistent disability found amongst these patients could not be attributed to failure on the part of those treating them to use the best available methods, or to failures to comply or engage with treatment on the patient's part. In some two thirds of instances persistent disability was best explained by the fact that even the most suitable available treatments have to be considered only partially effective

Two-dimensional infrared spectroscopy reveals the complex behaviour of an amyloid fibril inhibitor.

Amyloid formation has been implicated in the pathology of over 20 human diseases, but the rational design of amyloid inhibitors is hampered by a lack of structural information about amyloid-inhibitor complexes. We use isotope labelling and two-dimensional infrared spectroscopy to obtain a residue-specific structure for the complex of human amylin (the peptide responsible for islet amyloid formation in type 2 diabetes) with a known inhibitor (rat amylin). Based on its sequence, rat amylin should block formation of the C-terminal β-sheet, but at 8 h after mixing, rat amylin blocks the N-terminal β-sheet instead. At 24 h after mixing, rat amylin blocks neither β-sheet and forms its own β-sheet, most probably on the outside of the human fibrils. This is striking, because rat amylin is natively disordered and not previously known to form amyloid β-sheets. The results show that even seemingly intuitive inhibitors may function by unforeseen and complex structural processes