Advenovirus type 2 core proteins were studied with the aid of temperature-sensitive (ts) mutants affecting them. Cores prepared from wild-type virions with pyridine contained the structural proteins IVa2, V, VII, and X. Cores from the H2ts3 mutant contained an altered polypeptide V (50 K) of higher molecular weight and additional peptides. Ts1 virions produced at the restrictive temperature contained precores with proteins IVa2, V, pre-VI, pre-VII, and 11 K. This precore could be matured to a wild-type-like core by the adenovirus endoprotease. Of these core proteins only V, pre-VI, pre-VII, VII, and 11 K could be shown to reassociate in vitro with double-stranded heterologous DNA. Proteins IVa2 and X may bind to these core proteins rather than to the DNA directly.

BackgroundA Treat-to-Target (T2T) strategy for inflammatory arthritis, targeting remission or minimal disease activity, is the recommended treatment approach by EULAR and ACR. This strategy relies on “tight monitoring” which necessitates regular clinical examination and measuring acute-phase reactants such as C-reactive protein. Calprotectin (MRP8/14; S100A8/A9), a relatively novel inflammation and disease activity marker in the arthritis field, exhibits several features which fit the “theranostic needs” for accurate therapy monitoring. Those features include discrimination between responders and non-responders [1], detection of subclinical disease activity [2] and prediction of relapse or radiographic progression [3]. The classical method to determine calprotectin in serum (sCAL) is ELISA which is used in service or central laboratories. A rapid and simple determination of sCAL at the point of care is a substantial step forward in supporting clinicians to deliver an efficient T2T strategy. Here, we report on the validation of a quantitative, rapid test which can measure sCAL within 15 minutes.Objectives(1) To demonstrate the performance evaluation of a quantitative lateral flow assay combined with a dedicated test reading device for the rapid quantification of calprotectin in serum; and (2) to compare results to a well-established laboratory reference method using patient samples.MethodsThe Quantum Blue® sCAL sandwich lateral flow immunoassay uses two highly specific monoclonal antibodies immobilized on the test membrane and on the gold label. 10μL of serum was diluted in 90μL of chase buffer, 60μL of this mixture was applied onto the lateral flow test cassette, which was incubated for 12 minutes at ambient temperature and then measured with the BÜHLMANN Quantum Blue® Reader. Performance evaluation (sensitivity, linearity, high-dose hook effect, interferences) was carried out according to CLSI guidelines. A method comparison based on 178 serum samples from RA and PsA patients was performed against the BÜHLMANN sCAL (MRP8/14) reference ELISA.ResultsThe linearity study over the complete measuring range together with the observed limit of quantification (LoQ) of <0.5 μg/mL allowed a quantitative measurement in the clinically relevant range from 0.5 to 10.0 μg/mL calprotectin. No high dose hook effect was observed up to a concentration of 200 μg/mL. Moreover, no interferences were detected with triglycerides (37mmol/L), conjugated bilirubin (342μmol/L), unconjugated bilirubin (342μmol/L), and hemoglobin (200mg/dL). The Quantum Blue® sCAL lateral flow assay showed an excellent linear correlation (r=0.94, slope=1.05) to the BÜHLMANN sCAL (MRP8/14) reference ELISA. There was a negligible bias of -3.1% by Bland-Altman difference plot between the sCAL lateral flow assay and ELISA.ConclusionsRapid quantification of serum calprotectin using the Quantum Blue® sCAL assay represents a fast and reliable method for the determination of inflammation and the disease activity of a patient with inflammatory arthritis at the point of...

The badger (Mêles mêles L.) in the Swiss Jura: trapping success, demographic parameters and ectoparasites. -We studied two badger (Meles mêles L.) populations in western Switzerland between 1993 and 1996. Trapping success was low and probably related to population densities. Metal cages proved to be efficient in trapping cubs, whereas only snares were adapted to catch adult badgers. As in other areas, badger weight was higher in males than in females, and showed an autumnal peak. Almost 70% of the animals were infested with ticks {Ixodes spp.), but loads were generally low. Studied populations consisted of 34% cubs and 66% adults/ subadults. The observed sex ratio was slightly but non significantly biased towards females. Road-traffic was the main mortality factor in adults.

Nucleotide sequences of the hemagglutinin (HA) gene of twelve influenza B strains and their deduced amino acid sequences were extracted from the GenBank and compared to those of early isolates. Separate analyses of nonsynonymous and synonymous substitutions for the HA1 and HA2 regions individually indicate that the percentage of nonsynonymous substitutions in the HA1 ranges from 44.4-56.0% but in the HA2 from 0.0-6.5%. The results suggest that positive selection as well as negative selection played a role in the evolution of the influenza B HA gene with the former acting on the HA1 and the latter on the HA2.

The lactate turnover rate of rainbow trout (Oncorhynchus mykiss) was measured by bolus injection of [U-14C]lactate at rest and during prolonged swimming at 85% Ucrit to determine the importance of this metabolic fuel for endurance locomotion in fish, to assess whether lactate exchange between white and red muscle could be a possible mechanism for supplying oxidizable fuel to their lateral red muscle, and to compare the contribution of lactate to total energy provision between teleost and mammalian species. Turnover rate only increased from 4.41 +/− 0.33 to 9.71 +/− 1.69 mumol kg-1 min-1 between rest and prolonged swimming, and the contribution of lactate oxidation to total metabolism declined during exercise. Lactate exchange between white and red muscle is, therefore, not a significant mechanism to fuel the active lateral red musculature during prolonged swimming. The lactate turnover rate of teleosts is one or two orders of magnitude lower than in mammals of equivalent size, but lactate has the same importance as a fuel in both vertebrate groups. However, lactate turnover rate and oxidation rate do not scale with body mass in the same fashion as does metabolic rate. The slope of the mammalian relationship for whole-body lactate turnover and oxidation is much lower (0.58) than the slope of the classic relationship for metabolic rate (0.75), indicating that lactate is a much more important oxidative substrate for small than for large animals.