Evaluation of bithionol as a bath treatment for amoebic gill disease caused by Neoparamoeba spp

This study examined the toxicity of bithionol to Atlantic salmon Salmo salar and rainbow trout Oncorhynchus mykiss in fresh- and seawater and the efficacy of bithionol as a 1h seawater bath treatment for amoebic gill disease (AGD). To examine toxicity, fish were bathed for 1, 3 and 6h in bithionol, an anti-protozoal at 0, 1, 5, 10, 25 and 35mgL(-1) with toxicity determined by time to morbidity. Efficacy was examined by bathing AGD-affected Atlantic salmon and rainbow trout for 1h at bithionol concentrations of 1-25mgL(-1). Efficacy was determined by examining gill amoeba counts and identifying percent lesioned gill filaments at 1 and 24h after bath exposure to bithionol. For both species, bithionol was determined to be toxic at 25 and 35mgL(-1) exhibiting median lethal times (LT50s) ranging from 21 to 84min. Morbidity occurred in the 5 and 10mgL(-1) treatments, however, due to sampling regime there were not enough fish available to calculate LT50s. Only bithionol at 1mgL(-1) was considered non-toxic with no signs of morbidity. Bithionol was more toxic in seawater than freshwater and had no acute effects on gill Na+/K+ ATPase and succinic dehydrogenase, or plasma osmolality and chloride concentration. Bithionol at 1mgL(-1) reduced percent lesioned gill filaments in Atlantic salmon and rainbow trout by 33 and 27 per cent, respectively, compared to the seawater control. Similarly, numbers of amoeba were reduced by 33 and 43 per cent for Atlantic salmon and rainbow trout, respectively, when compared to the seawater control. Furthermore, bithionol reduced percent lesioned gill filaments as much as did the current industry standard of freshwater. This study demonstrated that a 1h seawater bath containing 1mgL(-1) bithionol could be an improvement to the current method of treatment for AGD-affected Atlantic salmon and rainbow trout.     

Complete amino acid sequence of the Mu heavy chain of a human IgM immunoglobulin

The amino acid sequence of the micro, chain of a human IgM immunoglobulin, including the location of all disulfide bridges and oligosaccharides, has been determined. The homology of the constant regions of immunoglobulin micro, gamma, alpha, and epsilon heavy chains reveals evolutionary relationships and suggests that two genes code for each heavy chain.     

Air-snow interactions and atmospheric chemistry

The presence of snow greatly perturbs the composition of near-surface polar air, and the higher concentrations of hydroxyl radicals (OH) observed result in a greater oxidative capacity of the lower atmosphere. Emissions of nitrogen oxides, nitrous acid, light aldehydes, acetone, and molecular halogens have also been detected. Photolysis of nitrate ions contained in the snow appears to play an important role in creating these perturbations. OH formed in the snowpack can oxidize organic matter and halide ions in the snow, producing carbonyl compounds and halogens that are released to the atmosphere or incorporated into snow crystals. These reactions modify the composition of the snow, of the interstitial air, and of the overlying atmosphere. Reconstructing the composition of past atmospheres from ice-core analyses may therefore require complex corrections and modeling for reactive species.     

Thiophanate-methyl and carbendazim resistance in Fusicoccum amygdali,the causal agent of constriction canker of peach and almond

In light of growing environmental concerns, surveys of fungicide resistance are needed to ensure efficient control of fungi and avoid unnecessary treatments. Investigations of fungicide resistance in Fusicoccum amygdali are scarce despite the economic impacts of this pathogen in peach and almond orchards. Thiophanate-methyl has been registered for more than 20 years to control F. amygdali but no resistance has been reported to date. This propesticide is metabolized by fungi into carbendazim, a β-tubulin inhibitor. Sensitivity to carbendazim of nine populations of F. amygdali from French orchards was assessed using germination bioassays. Also, resistance levels of 63 strains isolated from four populations were evaluated using mycelial growth assays. The underlying mechanism of resistance was investigated by sequencing the β-tubulin gene, the molecular target of thiophanate-methyl, in a set of isolates with different levels of sensitivity to carbendazim. Cross-resistance to thiophanate-methyl and to another β-tubulin inhibitor, diethofencarb, was also assessed in carbendazim-sensitive and -resistant strains. Isolates highly resistant to carbendazim were found in one of the nine orchards studied. Sequencing showed that resistant phenotypes carry a mutation in the β-tubulin gene leading to E198K substitution. Positive cross-resistance to thiophanate-methyl was confirmed and no negative cross-resistance to diethofencarb was identified in the phenotyped isolates, which were all resistant to this active substance. To our knowledge, this is the first report of resistance to thiophanate-methyl in F. amygdali. The high level of resistance of isolates sampled in one population is of concern, although the limited geographical scope of resistance suggests its recent emergence.     

Crystal structure of glycoprotein B from herpes simplex virus 1

Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended beta hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes.