cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.34808/0z0s-ed24
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-GRA5

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and GRA5. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 26-120 of the GRA5 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/svjw-qh50
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-GRA2

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and GRA2. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 51-185 of the GRA2 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/x91n-k467
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-GRA1

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and GRA1. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 24-190 of the GRA1 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/ffvt-q679
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-MAG1L

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and MAG1. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 30-452 of the MAG1 antigen (full length protein). In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/hsz5-k536
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-MAG1S

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and MAG1. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 30-222 of the MAG1 antigen (the immunodominant fragment well recognized by antibodies in the early stage of parasite invasion). In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/cdyk-jm85
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-LDH2

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and LDH2. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 2-326 of the LDH2 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/cazs-t550
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-ROP1

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and ROP1. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 85-396 of the ROP1 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/s324-n354
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-P35

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and P35 The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 26-378 of the P35 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/71gw-qp93
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-AMA1F

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and AMA1. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 67-569 of the AMA1 antigen (full length protein). In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.34808/ebgs-z903
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-AMA1

description: The intracellular parasite Toxoplasma gondii has the ability to infect a wide range of warm-blooded animals, including humans. Currently, diagnosis of toxoplasmosis is based mainly on the use of the native antigens in enzyme immunoassay which allow for detection of IgG, IgM and IgA antibody classes. However, in some cases the performed studies give the ambiguous results. Moreover, the commercially available diagnostic tests due to its price are not generally applicable in the serodiagnosis of toxoplasmosis in animals, which requires the analysis of a large number of samples. For this reason, many research groups are currently working on new diagnostic tools, which are mainly recombinant antigens. Compared to the native antigens their production is much easier, cheaper, faster and safer. An additional advantage of the recombinant antigens is easier way to standardize assays.This study presents the construction of an efficient Escherichia coli expression system for the production of recombinant chimeric protein composed of the immunodominant regions of three Toxoplasma gondii antigens SAG1, SAG2 and AMA1. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 67-483 of the AMA1 antigen. In the next part of the work the diagnostic usefulness of obtaining proteins for detection of anti-T. gondii antibodies were evaluated in the IgG ELISA assay and agglutination test using animal sera (e.g. horses, ovine, and pigs) and human serum samples.
DOI: 10.6084/m9.figshare.14346008
title: Supplementary Material for: Total Dietary Fat Intake, Fat Quality, and Health Outcomes: A Scoping Review of Systematic Reviews of Prospective Studies

description: <b><i>Introduction:</i></b> We conducted a scoping review of systematic reviews (SRs) on dietary fat intake and health outcomes in human adults within the context of a position paper by the “International Union of Nutritional Sciences Task force on Dietary Fat Quality” tasked to summarize the available evidence and provide dietary recommendations. <b><i>Methods:</i></b> We systematically searched several databases for relevant SRs of randomized controlled trials (RCTs) and/or prospective cohort studies published between 2015 and 2019 assessing the association between dietary fat and health outcomes. <b><i>Results:</i></b> Fifty-nine SRs were included. The findings from SRs of prospective cohort studies, which frequently compare the highest versus lowest intake categories, found mainly no association of total fat, monounsaturated fatty acid (MUFA), polyunsaturated fatty acid (PUFA), and saturated fatty acid (SFA) with risk of chronic diseases. SRs of RCTs applying substitution analyses indicate that SFA replacement with PUFA and/or MUFA improves blood lipids and glycemic control, with the effect of PUFA being more pronounced. A higher intake of total trans-fatty acid (TFA), but not ruminant TFA, was probably associated with an increased risk of mortality and cardiovascular disease based on existing SRs. <b><i>Conclusion:</i></b> Overall, the available published evidence deems it reasonable to recommend replacement of SFA with MUFA and PUFA and avoidance of consumption of industrial TFA.
DOI: 10.34840/sp3r-h702
title: Periodontal disease diagnosed in dogs in the UK: epidemiology and associations with breed and body conformation
DOI: 10.6084/m9.figshare.14346011
title: Supplementary Material for: Ambient Air Pollution and Mortality among Older Patients Initiating Maintenance Dialysis

description: <b><i>Background:</i></b> Fine particulate matter (particulate matter with diameter &lt;2.5 µm [PM<sub>2.5</sub>]) is associated with CKD progression and may impact the health of patients living with kidney failure. While older (aged ≥65 years) adults are most vulnerable to the impact of PM<sub>2.5</sub>, it is unclear whether older patients on dialysis are at elevated risk of mortality when exposed to fine particulate matter. <b><i>Methods:</i></b> Older adults initiating dialysis (2010–2016) were identified from US Renal Data System (USRDS). PM<sub>2.5</sub> concentrations were obtained from NASA’s Socioeconomic Data and Application Center (SEDAC) Global Annual PM<sub>2.5</sub> Grids. We investigated the association between PM<sub>2.5</sub> and all-cause mortality using Cox proportional hazard models with linear splines [knot at the current Environmental Protection Agency (EPA) National Ambient Air Quality Standard for PM<sub>2.5</sub> of 12 μg/m<sup>3</sup>] and robust variance. <b><i>Results:</i></b> For older dialysis patients who resided in areas with high PM<sub>2.5</sub>, a 10 μg/m<sup>3</sup> increase in PM<sub>2.5</sub> was associated with 1.16-fold (95% CI: 1.08–1.25) increased risk of mortality; furthermore, those who were female (aHR = 1.26, 95% CI: 1.13–1.42), Black (aHR = 1.31, 95% CI: 1.09–1.59), or had diabetes as a primary cause of kidney failure (aHR = 1.25, 95% CI: 1.13–1.38) were most vulnerable to high PM<sub>2.5</sub>. While the mortality risk associated with PM<sub>2.5</sub> was stronger at higher levels (aHR = 1.19, 95% CI: 1.08–1.32), at lower levels (≤12 μg/m<sup>3</sup>), PM<sub>2.5</sub> was significantly associated with mortality risk (aHR = 1.04, 95% CI: 1.00–1.07) among patients aged ≥75 years (P<sub>slope difference</sub> = 0.006). <b><i>Conclusions:</i></b> Older adults initiating dialysis who resided in ZIP codes with PM<sub>2.5</sub> levels &gt;12 μg/m<sup>3</sup> are at increased risk of mortality. Those aged &gt;75 were at elevated risk even at levels below the EPA Standard for PM<sub>2.5</sub>.
DOI: 10.6084/m9.figshare.14346011.v1
title: Supplementary Material for: Ambient Air Pollution and Mortality among Older Patients Initiating Maintenance Dialysis

description: <b><i>Background:</i></b> Fine particulate matter (particulate matter with diameter &lt;2.5 µm [PM<sub>2.5</sub>]) is associated with CKD progression and may impact the health of patients living with kidney failure. While older (aged ≥65 years) adults are most vulnerable to the impact of PM<sub>2.5</sub>, it is unclear whether older patients on dialysis are at elevated risk of mortality when exposed to fine particulate matter. <b><i>Methods:</i></b> Older adults initiating dialysis (2010–2016) were identified from US Renal Data System (USRDS). PM<sub>2.5</sub> concentrations were obtained from NASA’s Socioeconomic Data and Application Center (SEDAC) Global Annual PM<sub>2.5</sub> Grids. We investigated the association between PM<sub>2.5</sub> and all-cause mortality using Cox proportional hazard models with linear splines [knot at the current Environmental Protection Agency (EPA) National Ambient Air Quality Standard for PM<sub>2.5</sub> of 12 μg/m<sup>3</sup>] and robust variance. <b><i>Results:</i></b> For older dialysis patients who resided in areas with high PM<sub>2.5</sub>, a 10 μg/m<sup>3</sup> increase in PM<sub>2.5</sub> was associated with 1.16-fold (95% CI: 1.08–1.25) increased risk of mortality; furthermore, those who were female (aHR = 1.26, 95% CI: 1.13–1.42), Black (aHR = 1.31, 95% CI: 1.09–1.59), or had diabetes as a primary cause of kidney failure (aHR = 1.25, 95% CI: 1.13–1.38) were most vulnerable to high PM<sub>2.5</sub>. While the mortality risk associated with PM<sub>2.5</sub> was stronger at higher levels (aHR = 1.19, 95% CI: 1.08–1.32), at lower levels (≤12 μg/m<sup>3</sup>), PM<sub>2.5</sub> was significantly associated with mortality risk (aHR = 1.04, 95% CI: 1.00–1.07) among patients aged ≥75 years (P<sub>slope difference</sub> = 0.006). <b><i>Conclusions:</i></b> Older adults initiating dialysis who resided in ZIP codes with PM<sub>2.5</sub> levels &gt;12 μg/m<sup>3</sup> are at increased risk of mortality. Those aged &gt;75 were at elevated risk even at levels below the EPA Standard for PM<sub>2.5</sub>.