The welfare and healthy growth of poultry under intensive feeding conditions are closely related to their living environment. In spring, the air quality considerably decreases due to reduced ventilation and aeration in cage systems, which influences the meat quality and health of broilers during normal growth stages. In this study, we analyzed the airborne bacterial communities in PM2.5 and PM10 in cage broiler houses at different broiler growth stages under intensive rearing conditions based on the high-throughput 16S rDNA sequencing technique. Our results revealed that PM2.5, PM10 and airborne microbes gradually increased during the broiler growth cycle in poultry houses. Some potential or opportunistic pathogens, including Acinetobacter, Pseudomonas, Enterococcus, Microbacterium, etc., were found in the broiler houses at different growth stages. Our study evaluated variations in the microbial communities in PM2.5 and PM10 and potential opportunistic pathogens during the growth cycle of broilers in poultry houses in the spring. Our findings may provide a basis for developing technologies for air quality control in caged poultry houses.
In the current study, twenty lambs, aged 4 months, half male and half female, were classified into four groups, with five in each group. The experimental three groups of lambs were given intravenous (IV), intramuscular (IM) and subcutaneous (SC) administrations of recombinant ovine interferon-τ (roIFN-τ). The fourth group (normal control) of lambs was given normal saline injections in the same way. After administrations, blood samples were collected from the tested animals at different time points post injection, and the serum titers of roIFN-τ were measured using cytopathic effect (CPE) inhibition bioassay. The results of calculating pharmacokinetic (PK) parameters using DAS software showed that the PK characteristics of roIFN-τ through IV injection conformed to the two-compartment open model, whose half-life of distribution phases (T1/2α) was 0.33±0.034 h and the elimination half-life(T1/2β) was 5.01±0.24 h. However, the PK features of IM injection and SC injection of roIFN-τ conformed to the one compartment open model, whose Tmax were 3.11±0.26 h and 4.83±0.43 h, respectively, together with an elimination half life(T1/2β) of 9.11±0.76 h and 7. 43±0.58 h, and an absorption half-life (T1/2k(a)) of 1.13±0.31 h and 1.85±0.40 h, respectively. The bioavailability of roIFN-τ after IM administration reaches 73.57%, which is greater than that of SC administration (53.43%). These results indicate that the drug administration effect can be preferably obtained following a single dose IM administration of the roIFN-τ aqueous preparation. This study will facilitate the clinical application of roIFN-τ as a potential antiviral agent in future work.
Owing to the dramatic change in the thermal conductivity of 4He when its temperature crosses the transition of superfluid (HeI) and normalfluid (HeII), a sealed-cell with a capillary is used to realize the lambda transition temperature, Tλ. A small heat flow is controlled through the capillary of the sealed-cell so as to realize the coexistence of HeI and HeII and maintain the stay of HeI/HeII interface in the capillary. A stable and flat lambda transition temperature "plateau" is obtained. Because there is a depression effect of Tλ caused by the heat flow through the capillary, a series of heat flows and several temperature plateaus are made and an extrapolation is applied to determine Tλ with zero heat flow. A rhodium-iron resistance thermometer with series number A34 (RIRT A34) has been used in 24 Tλ -realization experiments to derive Tλ with a standard deviation of 0.022mK, which proves the stability and reproducibility of Tλ.
Sapelovirus A (SV-A) is a positive-sense single-stranded RNA virus which is associated with acute diarrhea, pneumonia and reproductive disorders. The virus capsid is composed of four proteins, and the functions of the structural proteins are unclear. In this study, we expressed SV-A structural protein VP1 and studied its antigenicity and immunogenicity. SDS-PAGE analysis revealed that the target gene was expressed at high levels at 0.6 mM concentration of IPTG for 24 h. The mouse polyclonal antibody against SV-A VP1 protein was produced and reached a high antiserum titer (1: 2,048,000). Immunized mice sera with the recombinant SV-A VP1 protein showed specific recognition of purified VP1 protein by western blot assay and could recognize native SV-A VP1 protein in PK-15 cells infected with SV-A by indirect immunofluorescence assay. The successfully purified recombinant protein was able to preserve its antigenic determinants and the generated mouse anti-SV-A VP1 antibodies could recognize native SV-A, which may have the potential to be used to detect SV-A infection in pigs.