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36 results for “Eimeria tenella”
Figure 6 in Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella
Figure 6. Localization of EtCHP18905 in infected DF-1 cells by indirect immunofluorescence. Parasites incubated with anti-rEtCHP18905, stained with FITC (green)-conjugated secondary antibodies, and counterstained with DAPI (blue). Infected DF-1 cells were collected at indicated time points post-infection. (A) Sporozoites (Spz) in PBS, pRB, posterior refractile body; (B) Spz in complete medium. Infected DF-1 cells were collected at the indicated time points post-infection (pi); (C) 2 hours pi (hpi); (D) immature schizonts (iSC) 48 hpi; (E) mature schizonts (mSC) 72 hpi; (F) merozoites (Mrz) in PBS.
Figure 3 in Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella
Figure 3. Expression and purification of rEtCHP18905. (A) SDS-PAGE analysis of the 5rEtCHP18905. Lanes 1, protein marker; 2, negative control (not induced with IPTG); 3, the rEtCHP18905 protein with the GST-tag protein of the vector (induced with IPTG for 6 h). (B) Western blot analysis of purified rEtCHP18905 protein. Lane 2, protein recognized by an anti GST-Tag monoclonal antibody. (C) Western blot analysis of purified rEtCHP18905 protein. Lane 2, protein recognized by rabbit sera against sporozoite, lane 4 incubated with naïve rabbit serum.
Figure 2 in Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella
Figure 2. Bioinformatic analysis of EtCHP18905. The stop codon is indicated with an asterisk. N-myristoylation sites are double underlined. The transmembrane domain is shaded yellow with black lettering. N-glycosylation sites are surrounded by a black box. cAMP- and cGMP-dependent protein kinase phosphorylation sites are shaded black with white lettering. Tyrosine kinase phosphorylation site is shaded grey with black lettering. Casein kinase II phosphorylation sites are indicated with red lettering. Protein kinase C phosphorylation sites are underlined by a wavy line.
Figure 1 in Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella
Figure 1. Multiple alignment analysis of EtCHP18905 with other Eimeria proteins. DNAMAN was used to analyze the deduced protein sequences. The identical amino acids are listed at the bottom. NCBI reference sequence accession numbers: Eimeria tenella, XP_013231819, Eimeria necatrix, XP_013438465, Eimeria mitis, XP_013355934, Eimeria maxima, XP_013336337, Eimeria acervulina, XP_013251133; GenBank accession numbers: Eimeria praecox, CDI76926, Eimeria brunetti, CDJ52365.
Figure 7 in Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella
Figure 7. Inhibition of sporozoite invasion in vitro by antirEtCHP18905. Anti-rEtCHP18905, rabbit anti-rEtCHP18905 IgG; NA, naïve rabbit sera IgG; GST control, rabbit anti-GST IgG. The symbol "*" represents p <0.05, "**" represents p <0.01, and "***" represents p <0.001 for comparison of treatment with antirEtCHP18905 and naïve rabbit sera IgG and anti-GST IgG at the same concentration. The error bars indicate the standard deviation. All assays were performed in triplicate.
Figure 4 in Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella
Figure 4. Transcription levels of EtCHP18905 in different developmental stages of E. tenella. UO, unsporulated oocysts; SO, sporulated oocysts; Spz, sporozoites; Mrz, merozoites. Bars with different letters indicate significantly different expression levels (p <0.05) and the error bars indicate standard deviations.
Figure 5 in Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella
Figure 5. Expression levels of EtCHP18905 in different developmental stages of E. tenella. (A) Western blot of the internal reference tubulin and EtCHP18905 protein. (B) Relative expression levels of the EtCHP18905 protein. Bars with different letters indicate significantly different expression levels (p <0.05) and the error bars indicate standard deviations.
Figure 6 in Further investigation of the characteristics and biological function of Eimeria tenella apical membrane antigen 1
Figure 6. KEGG pathway classification of differentially expressed proteins in DF-1 cells transiently transfected with EtAMA1.
Figure 5 in Further investigation of the characteristics and biological function of Eimeria tenella apical membrane antigen 1
Figure 5. Gene ontology analysis of 163 proteins differentially expressed in DF-1 cells transiently transfected with EtAMA1. Proteins were annotated based on biological process, cellular component, and molecular function.
Figure 3 in Further investigation of the characteristics and biological function of Eimeria tenella apical membrane antigen 1
Figure 3. Inhibition of sporozoite invasion in vitro by antibodies against rEtAMA1, rEtESP, and rEtRON2. (a) Invasion-inhibition activities of single antibodies. Anti-rEtAMA1, rEtESP, and rEtRON2 rabbit anti-serum against recombinant EtAMA1, EtESP and EtRON2 protein, respectively; IgG, normal rabbit serum. (b) Invasion-inhibition activities of antibody combinations. Combinations of anti-rEtAMA1 and antirEtESP or anti-rEtRON2 were added at a ratio of 1:1 to generate a gradient concentration of IgG. All assays were performed in triplicate. *p <0.05, **p <0.01 and ***p <0.001, as determined by the Student's t-test versus the non-immunized IgG groups at the same concentration.
Figure 2 in Further investigation of the characteristics and biological function of Eimeria tenella apical membrane antigen 1
Figure 2. Colocalization of EtAMA1, EtESP, and EtRON2 in sporozoites by indirect immunofluorescence. Parasites were immunostained with anti-rEtAMA1, and anti-rEtESP or anti-rEtRON2 antibodies, visualized with FITC (green) and counter-stained with DAPI (blue). Scale bar, 10 µm.
Figure 1. EtAMA1 in Further investigation of the characteristics and biological function of Eimeria tenella apical membrane antigen 1
Figure 1. EtAMA1 is secreted by micronemes. (a) EtAMA1 secretion is FCS- and temperature-dependent. Fresh sporozoites were incubated in PBS or complete medium (CM) at 4 °C or 41 °C for 2 h. Supernatants containing excretory-secretory antigens (ESAs) were harvested and analyzed by western blotting to detect EtAMA1 and EtMIC2. (b) EtAMA1 secretion is inhibited by staurosporine. Sporozoites were incubated in CM with various concentrations of staurosporine or DMSO at 41 °C for 2 h. Supernatants containing ESAs was harvested and analyzed by western blotting to detect EtAMA1 and EtMIC2.
Figure 4 in Further investigation of the characteristics and biological function of Eimeria tenella apical membrane antigen 1
Figure 4. In vitro sporozoite invasion of DF-1 cells transiently transfected with EtAMA1. (a) Verification of pcDNA3.1-(+)-EtAMA1 expression in DF-1 cells by IFA. (b) The proliferation of DF-1 cells transfected with pcDNA3.1-(+)-EtAMA1 or pcDNA3.1-(+). (c) Sporozoite invasion rate in DF-1 cells transfected with pcDNA3.1-(+)-EtAMA1 or pcDNA3.1-(+). *p <0.05 and **p <0.01, as determined by the Student's t-test versus the untreated group.
Figure 8 in Molecular characterization and protective efficacy of a new conserved hypothetical protein of Eimeria tenella
Figure 8. Levels of IgG (A), sCD4 (B), sCD8 (C), cytokines IFN-γ (D), IL-10 (E), IL-17 (F) and TGF-β1 (G) in chicken sera were measured using ELISA. Chickens of group rEtCHP18905-50 μg and group rEtCHP18905-100 μg were immunized with 50 μg or 100 μg of rEtCHP18905 protein, respectively. Challenged and unchallenged groups were immunized with PBS and served as controls. The IgG titers and the concentrations of sCD4, sCD8, and cytokines are expressed as Min to Max. (*p <0.05, **p <0.01, ***p <0.001; ns, p> 0.05).
Figure 5 in Quantitative phosphoproteomic analysis of chicken DF-1 cells infected with Eimeria tenella, using tandem mass tag (TMT) and parallel reaction monitoring (PRM) mass spectrometry
Figure 5. KEGG pathways of the differentially expressed phosphorylated proteins. The abscissa indicates the first 10 significantly enriched KEGG pathways and the ordinate indicates the significance of enriched KEGG pathways, the more left, the more significant.
Figure 4 in Quantitative phosphoproteomic analysis of chicken DF-1 cells infected with Eimeria tenella, using tandem mass tag (TMT) and parallel reaction monitoring (PRM) mass spectrometry
Figure 4. Gene ontology annotations of the differentially expressed phosphorylated proteins. The abscissa indicates the enriched GO functional classification, including biological process (A), cellular component (B), and molecular function (C). The ordinate indicates the size of the significance of corresponding to each entry, the more left, the more significant.
Figure 3 in Quantitative phosphoproteomic analysis of chicken DF-1 cells infected with Eimeria tenella, using tandem mass tag (TMT) and parallel reaction monitoring (PRM) mass spectrometry
Figure 3. Clustering heatmap of different expression phosphorylated peptides. Each row represents a phosphorylated peptide segment, each column represents a group of samples. The logarithmic value (logarithmic transformation based on 2) of the significantly differentially expressed phosphorylated peptides in different samples is displayed in the clustering heatmap in different colors. Red represents significant upregulation of phosphorylated peptides; blue represents significant down-regulation of phosphorylated peptides.
Figure 2 in Quantitative phosphoproteomic analysis of chicken DF-1 cells infected with Eimeria tenella, using tandem mass tag (TMT) and parallel reaction monitoring (PRM) mass spectrometry
Figure 2. Volcano plots from different group comparisons. The abscissa indicates difference multiple (logarithmic transformation based on 2), the ordinate indicates the significant of difference (logarithmic transformation based on 10). The red point is significantly upregulated phosphorylated peptide segment, the blue point is significantly downregulated phosphorylated peptide segment and the gray point is a phosphorylated peptide segment with no significant difference.
Reduction of chickens use to perform in vitro pre-screening of novel anticoccidials by miniaturisation and increased throughput of the current Eimeria tenella compound-screening model
<p>In vitro models have supported important advances in biomedical sciences and have significantly contributed to reduce the use of experimental animals in different disciplines. We have developed an in vitro model for the evaluation of potential anticoccidial properties of novel compounds aimed to control chicken coccidiosis, a costly disease for the poultry industry. This disease is caused by protozoan parasites of the genus <em>Eimeria</em> (Apicomplexa), and it is mainly controlled by chemoprophylaxis with ionophors and chemical anticoccidials; however, there is an overall agreement about the limitation of these classical drugs and the need to improve current methods of control. Anticoccidial activities of novel compounds is currently evaluated by expensive experiments that involve large numbers of chickens. The use of our in vitro model for the pre-screening of essential oils led to a reduction of 67% of the chickens used in the vivo trials for validation. In this study, we describe how further optimisation of this in vitro model by miniaturisation can have an additional impact on the number of chickens used for the generation of parasite stocks for provision of the in vitro model (which cannot be done in vitro). We have estimated that the use of one chicken could support the evaluation of ten compounds with a 96-well plate format vs. only two with a 24-well plate format, which means an 80% of chicken use reduction. In this study, we have proved that the miniaturisation into a 96-well plate format has perfectly mimicked the invasion and replication observed before in the 24-well plate format. In addition, this format has allowed the simultaneous pre-screening of higher numbers of anticoccidial drugs at different concentrations following streamlined protocols in a more cost-effective way, factors that are beneficial for a wider uptake of the model by other researchers investigating anticoccidial compounds. </p>
Figure 1 in Quantitative phosphoproteomic analysis of chicken DF-1 cells infected with Eimeria tenella, using tandem mass tag (TMT) and parallel reaction monitoring (PRM) mass spectrometry
Figure 1. Proportion of serine, threonine, and tyrosine in phosphorylation sites.
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