Duck viral hepatitis (DVH) is an acute and fatal disease of young ducklings characterized by rapid transmission and damages. The most important agent of DVH is duck hepatitis virus 1 (DHV-1). The effective control of DVH was achieved by active immunization of 1-day-old duck- lings with an attenuated DHV-1 virus vaccine. However, the attenuated virus might reverse to virulence. In this study, a DHV-1 strain, Du/CH/LBJ/090809, was identified and its genomic se- quences were determined. The genome of Du/CH/LBJ/090809 is composed of 7,692 nt excluding poly A and the virus was clustered into genotype A by comparing with other referenced DHV-1 strains. Du/CH/LBJ/090809 could lead to 30% mortality of 10-day-old specific pathogen free (SPF) ducklings. The virus was passaged serially in SPF chicken embryonated eggs and three vi- ruses, passage 16 (P16), P29 and P40, were selected for genomic analysis. P29 and P40 were used to evaluate the attenuation in duckling by inoculating the virus to 10-day-old SPF ducklings. Re- sults of vaccination-challenge assay showed that the inactivated virus P40 could evoke protection against the pathogenic parent virus. Nucleotide and amino acid sequences of the genomes of Du/ CH/LBJ/090809, P16, P29 and P40 were compared. Changes both in nucleotides and amino acids, which might be contributed to the decreasing in virulence by chicken embryo-passaging of DHV- 1, were observed. We speculated that these changes might be important in the adaption and at- tenuation of the virulent virus. Additionally, strains obtained in this study will provide potential candidate in the development of vaccines against DHV-1.
Faecal Enterococcus hirae from domestic ducks were studied for their bioactivity to select bioactive strain for more detailed study with its probable use in poultry and also to bring novelty in basic research. After defecation, faeces (n=23, faecal mixture of 40 ducks) were sampled from domestic ducks in eastern Slovakia; birds were aged from eight to 14 weeks. E. hirae strains were identified using Matrix-assisted laser desorption/ionization time-of flight mass spectrometry with a highly probable species identification score (2.300-3.000) or a secure genus identification/ /probable species identification score (2.000-2.299), confirmed by polymerase chain reaction and phenotypization in accordance with the properties for the type strain E. hirae ATCC 9790. Strains were hemolysis negative (γ-hemolysis), and did not have active enzyme stimulating disorders. Enterocin genes were detected in three strains out of seven. Three out of four Enterocin genes were detected in Kč1/b (Ent A, P, L50A); the most frequently detected was the Ent P gene. The strains inhibited indicator strains E. faecalis, listeriae, but also Escherichia coli and Buttiauxiella strains. Lactic-acid producing E. hirae were mostly susceptible to antibiotics. Based on parameter evaluation, E. hirae Kč1/b, Kč6 can be additionally studied to select the type of bioactive substance.
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.