Hemagglutinin of the influenza virus is the main external glycoprotein. This very immunogenic protein is the target of the most anti-influenza vaccines. DNA vaccines are new alternative to conventional inactivated ones. Four DNA vaccines were tested. Each tested variant was based on the pCI vector with nucleotide sequence encoding hemagglutinin from A/swan/Poland/305-135V08/2006 (H5N1, clade 2.2). In K3/pCI, GK/pCI and HAneo/pCI the different optimization algorithms of hemagglutinin encoding sequence without amino acids change were tested. In 3NF/pCI the NFkappaB binding sites flanking the expression cassette were included in order to improve the nuclear transfer. Comparative transcriptome analysis of mice vaccinated the following vaccine HAneo/pCI,K3/pCI, GK/pCI or 3NF/pCI versus empty vector demonstrated minor changes in genes expression pattern. Most genes were expressed on the similar level in the vaccinated individuals and in the control mice. Small number of genes in particular variants showed the expression different than in the control mice. In general, the identified genes with the changed expression included some genes involved in metabolic processes and none of them seem to induce any undesirable pathways nor disease.
Immunogenicity of DNA Vaccine against H5N1 Containing Extended Kappa B Site: <i>In Vivo</i> Study in Mice and Chickens.
Sex, Specimen part, Treatment
View SamplesBroilers were immunized with three variants of subunit vaccines, based on the hemagglutinin (HA) DNA and Pichia-produced HA protein from H5N1 virus, in comparison to the control group, which was administered an empty vector (pCI). Gene expression changes in the spleens of chickens were investigated at 7 day post booster dose.
Transcriptional response to a prime/boost vaccination of chickens with three vaccine variants based on HA DNA and Pichia-produced HA protein.
Specimen part, Treatment
View SamplesThis SuperSeries is composed of the SubSeries listed below.
Response to a DNA vaccine against the H5N1 virus depending on the chicken line and number of doses.
Specimen part, Treatment
View SamplesLaying hens Rosa 1 were immunized with two doses of DNA vaccine, based on the hemagglutinin (HA) DNA from H5N1 virus, in comparison to the control group, which was administered an empty vector (pCI). Additional groups of Rosa 1 hens were treated with one dose of above described vaccine or empty vector. Gene expression changes in the spleens of chickens were investigated at 7 day post last vaccination dose.
Response to a DNA vaccine against the H5N1 virus depending on the chicken line and number of doses.
Treatment
View SamplesBackground: Macrophages are important cells in pathogenesis of obstructive lung diseases including asthma and chronic obstructive pulmonary disease (COPD). The aim of the study was a multivariate, genetic, comparative analysis of macrophages from patients with asthma and COPD.
Genetic characterization of macrophages from induced sputum of patients with asthma and chronic obstructive pulmonary disease.
Specimen part, Disease
View SamplesTransposable elements (TEs) make up a large proportion of eukaryotic genomes. As their mobilization creates genetic variation that threatens genome integrity, TEs are epigenetically silenced through several pathways and this may spread to neighboring sequences. JUMONJI (JMJ) proteins can function as anti-silencing factors and prevent silencing of genes next to TEs. Whether TE silencing is counterbalanced by the activity of anti-silencing factors is still unclear. Here, we characterize JMJ24 as a regulator of TE silencing. We show that loss of JMJ24 results in increased silencing of the DNA transposon AtMu1c, while overexpression of JMJ24 reduces silencing. JMJ24 has a JumonjiC (JmjC) domain and two RING domains. JMJ24 auto-ubiquitinates in vitro, demonstrating E3 ligase activity of the RING domain(s). JMJ24-JmjC binds the N-terminal tail of histone H3 and full-length JMJ24 binds histone H3 in vivo. JMJ24 activity is anti-correlated with histone H3 lysine 9 dimethylation (H3K9me2) levels at AtMu1c. Double mutant analyses with epigenetic silencing mutants suggest that JMJ24 antagonizes histone H3K9me2, and requires H3K9 methyltransferases for its activity on AtMu1c. Genome-wide transcriptome analysis indicates that JMJ24 affects silencing at additional TEs. Our results suggest that the JmjC domain of JMJ24 has lost demethylase activity but has been retained as a binding domain for histone H3. This is in line with phylogenetic analyses indicating that JMJ24 [with the mutated JmjC domain] is widely conserved in angiosperms. Taken together, this study assigns a role in TE silencing to a conserved JmjC-domain protein with E3 ligase activity, but no demethylase activity.
A JUMONJI Protein with E3 Ligase and Histone H3 Binding Activities Affects Transposon Silencing in Arabidopsis.
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