Function of duck (Anas platyrhynchos) major histocompatibility complex class I (Anpl-MHC I) molecules in binding peptides is through the peptide binding groove (PBG), which is thought to be influenced by the high polymorphism of α1 and α2 domains. However, little is known about the polymorphism of Anpl-MHC I peptide binding domain (PBD), especially in the domestic duck. Here, we analyzed the polymorphism of forty-eight Anpl-MHC I α1 and α2 domains from domestic duck breeds previously reported. All sequences were analyzed through multiple sequence alignment and a phylogenetic tree was constructed. The coefficient of variance of the peptide binding domains (PBDs) from WS, CV, JD, and SX duck breeds was estimated based on the Wu-Kabat variability index, followed by the location of the highly variable sites (HVSs) on reported crystal structure models. Analysis of α1 and α2 domains showed common features of classical MHC class I and high polymorphism, especially in α1 domain. The constructed phylogenetic tree showed that PBDs of domestic ducks did not segregate based on breeds and had a close phylogenetic relationship, even with wild ducks. In each breed, HVSs were mostly located in the PBG, suggesting that they might determine peptide-binding characteristics and subsequently influence peptide presentation and recognition. The combined results of sequence data and crystal structure provide novel valuable insights into the polymorphism and diversity of Anpl-MHC I PBDs that will facilitate further studies on disease resistance differences between duck breeds and the development of cytotoxic T-lymphocyte (CTL) epitope vaccines suited for preventing diseases in domestic ducks.
Senecavirus A (SVA) the only member of the Senecavirus genus within the Picornaviridae family, is an emerging pathogen causing swine idiopathic vesicular disease and epidemic transient neonatal losses. Here, SVA strain (CH-HNKZ-2017) was isolated from a swine farm exhibiting vesicular disease in Henan Province of Central China. A phylogenetic analysis based on complete genome sequence indicated that CH-HNKZ-2017 was closely related to US-15-40381IA, indica- ting that a new SVA isolate had emerged in China.
An integrated Z-source inverter for the single-phase single-stage grid-connected photovoltaic system is proposed in this paper. The inverter integrates three functional blocks including maximum-power-point-tracking, step-up/down DC-side voltage and output grid-connected current. According to the non-minimum-phase characteristic presented in DC-side and the functional demands of the system, two constant-frequency sliding-mode controllers with integral compensation are proposed to guarantee the system robustness. By using two controllers, the effects caused by the non-minimum-phase characteristic are mitigated. Under the circumstance of that the input voltage or the grid-connected current changes suddenly, the notches/protrusions following the over-shoot/ under-shoot of the DC-bus voltage are eliminated. The quality of grid-connected current is ensured. Also, a small-signal modelling method is employed to analyze the close-loop system. A 300W prototype is built in the laboratory. A solar-array simulator (SAS) is used to verify the systematic responses in the experiment. The correctness and validity of the inverter and proposed control algorithm are proved by simulation and experimental results.
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.