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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 2 in Expression and immunolocalisation of TpFABP as a candidate antigen for the serodiagnosis of rabbit Taenia pisiformis cysticercosis

Figure 2. Expression of rTpFABP and identification by rabbit antisera in western blotting. Lane (1) molecular weight markers; (2) purified rTpFABP protein; (3) rTpFABP protein reacted with negative rabbit serum (1:100 v/v dilutions) by western blotting analysis; (4) rTpFABP protein reacted with rabbit antisera (1:100 v/v dilutions) by western blotting analysis. Molecular masses (kDa) are indicated on the left.

Figure 1 in Expression and immunolocalisation of TpFABP as a candidate antigen for the serodiagnosis of rabbit Taenia pisiformis cysticercosis

Figure 1. Structural analysis of TpFABP. Alignment of the amino acid residue sequences of Taenia pisiformis FABP with T. solium and Echinococcus granulosus in primary structures. The secondary structure of the TpFABP amino acid residue sequence was predicted and is shown at the top of the alignment. The light-grey shading indicates the identical amino acid sequences, and locations of linear B-cell epitopes are marked with open boxes. TpFABP1, GU205472; TsFABP1, HQ259679; TsFABP2, AFS64570; EgFABP1, 1O8V_A; EgFABP2, AAK12095; H-FABP, NP_004093.

Figure 4 in Expression and immunolocalisation of TpFABP as a candidate antigen for the serodiagnosis of rabbit Taenia pisiformis cysticercosis

Figure 4. Dot-ELISA of naturally infected rabbit experimental sera with rTpFABP. The tan-yellow tint shows the positive reaction: A, negative control sera; B, positive antisera; C, sera at 0 day postinfection; D, sera at 7 days post-infection; E, sera at 14 days post-infection; F, sera at 21 days post-infection; G, sera at 28 days post-infection; H, sera at 35 days post-infection; I, sera at 42 days post-infection; J, sera at 49 days post-infection.

Figure 3 in Expression and immunolocalisation of TpFABP as a candidate antigen for the serodiagnosis of rabbit Taenia pisiformis cysticercosis

Figure 3. Immunolocalisation of TpFABP in T. pisiformis tapeworm and cysticercus. The yellowish-brown tint shows the TpFABP protein location. (A) negative sera in cysticercus; (B) antisera in cysticercus; (C) negative sera in adult tapeworm; (D) antisera in adult tapeworm. Arrows indicate the areas of the parasite: MT, microthrix; DC, distal cytoplasm; PC, perinuclear cytoplasm; GD, gathering duct; M, microtrichia; ICW, inside the layer of cystic wall; OCW, outer layer of cystic wall; MCW, middle layer of cystic wall. Scale bars: 20 µm.

opencc-zeroJul 2024View details →

dryad40/100

Data from: Sequence-based detection of emerging antigenically novel influenza A viruses

The detection of evolutionary transitions in influenza A (H3N2) viruses' antigenicity is a major obstacle to effective vaccine design and development. In this study, we describe NIAViD, an unsupervised machine learning tool, adept at identifying these transitions, using HA1 sequence and associated physicochemical properties. NIAViD, performed with 88.9% (95% CI, 56.5%–98.0%) and 72.7% (95% CI,43.4%– 90.3%) sensitivity in training and validation respectively, outperforming the uncalibrated null model – 33.3% (95% CI,12.1%–64.6%) and does not require the need for potentially biased, time-consuming and costly laboratory assays. The pivotal role of Boman's index, indicative of the virus's cell surface binding potential, is underscored, enhancing the precision of detecting antigenic transitions. NIAViD's efficacy is not only in identifying influenza isolates that belong to novel antigenic clusters, but also in pinpointing potential sites driving significant antigenic changes, without the reliance on explicit modeling of hemagglutinin inhibition titers. Our approach holds immense promise to augment existing surveillance networks, offering timely insights for the development of updated, effective influenza vaccines. Consequently, NIAViD, in conjunction with other resources, could be used to support surveillance efforts and inform the development of updated influenza vaccines.

Fig. 4. Maximum Likelihood phylogenetic tree generated using N in The African buffalo parasite Theileria. sp. (buffalo) can infect and immortalize cattle leukocytes and encodes divergent orthologues of Theileria parva antigen genes

Fig. 4. Maximum Likelihood phylogenetic tree generated using N-terminal sequences of T. sp. (buffalo) and T. parva PIM antigen genes. Maximum composite likelihood trees were constructed using 1000 bootstrap replicates as implemented in MEGA5; the optimal nucleotide substitution model was identified using data monkey. The tree constructed with RAxML (Stamatakis et al., 2014) using a GTR/G/I model with 100 bootstrap iterations.

Fig. 5 in The African buffalo parasite Theileria. sp. (buffalo) can infect and immortalize cattle leukocytes and encodes divergent orthologues of Theileria parva antigen genes

Fig. 5. Maximum Likelihood Phylogenetic trees illustrating the genetic relationships of T. parva CD8 T target antigen gene orthologues from T. sp. (buffalo). Panel (A) Tp6; Panel B Tp7: Panel C Tp8. Sequences were aligned and used to construct a maximum likelihood tree, at which the nodes were confirmed using 1000 bootstrap replications. The bootstrap values indicating the degree of support for each node are shown and also the GenBank accession numbers of the sequences. For Tp6, the tree was rooted using the prohibitin gene sequences present in Babesia bovis (XM001609045) and Theileria orientalis (AB161472). For Tp7, the tree was rooted using the putative Heat shock protein 90 gene sequences from Toxoplasma gondii (AY344115), Babesia bovis (AK442026) and Theileria annulata (XM_947380). For Tp8, the tree was rooted using an orthologue of Tp8 found in Theileria equi (CP001669).

Fig. 3 in The African buffalo parasite Theileria. sp. (buffalo) can infect and immortalize cattle leukocytes and encodes divergent orthologues of Theileria parva antigen genes

Fig. 3. PCR amplification of genes encoding Theileria parva antigens from Marula schizont-infected leukocyte cultures. Panel A, p104 primers; Panel B PIM, primers; Panel C p67 primers. The order of the schizont-infected lymphocyte samples is (1) N6; (2). N13; (3). N18; (4). N20; (5). N33; (6). N36; (7). N38; (8). N43; (9). N50; (10). N55; (11). N69; (12). N76; (13). N77, (14). N79; (15). N86, (16). N88; (17). N99; (18). N100; (19). N102; (20). N103; (21). N106; (22). N107.

Fig. 2 in The African buffalo parasite Theileria. sp. (buffalo) can infect and immortalize cattle leukocytes and encodes divergent orthologues of Theileria parva antigen genes

Fig. 2. Results of a semi-nested PCR assay used to amplify 18S ribosomal subunit DNA using primers specific for T. parva and T. sp. (buffalo). Samples are as follows: 1)N13 2)N18 3) N20 4)N33 5)N36 6) N43 7)N50 8)N55 9) N69 10)N76 11) N79 12) N86 13) N88 14) N99 15)N100 16) N102 17) N103 18)N107 19—21) T. parva clones 22—24) T. sp. (buffalo) clones (documented in Table 2).

Fig. 1 in The African buffalo parasite Theileria. sp. (buffalo) can infect and immortalize cattle leukocytes and encodes divergent orthologues of Theileria parva antigen genes

Fig. 1. Reverse line blot analysis of schizont cultures containing parasites isolated from Marula farm. The following species-specific oligonucleotide probes were used (a) T. annulata, (b) T. parva, (c) T. mutans, (d) T. velifera, (e) T. taurotragi, (f) T. buffeli, (g) T. sp. (buffalo). (h) B. bigemina, (i) B. bovis. The order of the experimental samples hybridized is DNA from cell culture isolates in lanes 1—22 was lane 1; (1) N6, (2) N13, (3) N18, (4) N20, (5) N33, (6) N36, (7) N38 (8) N43, (9) N50 (10) N55, (11) N69, (12) N76, (13) N77, (14) N79, (15) N88, (16) N99, (17) N100 (18) N103, (19) N106, (20) N107, (21) N86, (22) N102 and DNA extracted from whole cattle blood (23) N106 (24) N69 (25) N86.

opencc-by-sa-4.0Jun 2018View details →

Diffraction images of a crystal of the complex formed by fragments of the integrin beta4 and the bullous pemphigoid antigen 1 (BP230, BPAG1e). PDB entry 6GVL.

Data were collected on a single crystal at the beamline i03 of the Diamond synchrotron facility (Didcot, UK) using radiation of 0.97625 Å wavelength and a PILATUS3 6M detector. The dataset consists of 2400 images (0.15 degree oscillation per image).

opencc-by-sa-4.0Jun 2018View details →

Diffraction images of a crystal of the complex formed by fragments of the integrin beta4 and the bullous pemphigoid antigen 1 (BP230, BPAG1e). Integrin high affinity point mutant. PDB entry 6GVK.

Data were collected on a single crystal at the beamline XALOC of the ALBA-CELLS synchrotron facility (Cerdanyola del Vallés, Barcelona, Spain) using radiation of 0.97915 Å wavelength and a PILATUS 6M detector. The complete dataset is build up of three sub-sets measured at three different positions of a single crystal. Each sub-set consists of 1800 images (0.2 degree oscillation per image).

opencc-by-4.0Dec 2022View details →

Fig. 6 in Plasmodium relictum MSP-1 capture antigen-based ELISA for detection of avian malaria antibodies in African penguins (Spheniscus demersus)

Fig. 6. Analysis of the sensitivity and specificity of the P. relictum MSP-1 capture antigen-based ELISA. Serial dilutions of normal chicken serum and three sera samples from P. relictum-infected penguins (8776, 8783 and 8784) were used for coating the assay wells. Each dilution was performed in triplicate, and the data shown represent means of three independent experiments with standard error bars and levels of statistical significance (****: P <0.0001).