cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.34808/05q1-q432
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC1-MIC3-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 MIC1, MIC3 and ROP1. The produced and purified proteins are composed of amino acid residues from:  A) 25-182 of the MIC1 antigen, 67-359 of the MIC3 antigen, 85-396 of the ROP1 antigen; B) 25-456 of the MIC1 antigen, 67-359 of the MIC3 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/s9mg-w154
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen AMA1-MIC1-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 AMA1, MIC1 and ROP1. The produced and purified proteins are composed of amino acid residues from:  A) 67-483 of the AMA1 antigen, 25-182 of the MIC1 antigen, 85-396 of the ROP1 antigen; B) 67-483 of the AMA1 antigen, 25-456 of the MIC1 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: 10.34808/1bn5-wt83
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen AMA1-MIC1-MIC3

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 AMA1, MIC1 and MIC3. The produced and purified proteins are composed of amino acid residues from:  A) 67-483 of the AMA1 antigen, 25-182 of the MIC1 antigen, 67-359 of the MIC3 antigen; B) 67-483 of the AMA1 antigen, 25-456 of the MIC1 antigen, 67-359 of the MIC3 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.14579697.v4
title: Figures_Tables_Supplementary materials-MDPI

description: Molecular characteristics and minimum inhibitory concentration values of C. difficile clinical isolates in Thailand
DOI: 10.25919/079m-xw73
title: Parkes observations for project P1101 semester 2021APRS_03

description: We propose to carry out fortnightly monitoring of a very active repeater, FRB~190520, with the Parkes UWL system. Our current observations show that FRB~190520 is not only the most active FRB that can be observed with Parkes, but also shows unique behaviour at 2 to 3 GHz frequency. This makes UWL the ideal instrument to carry out in-depth studies of this repeating FRB. With this program, we expect to detect a large sample of bursts from FRB~190520, and in collaboration with the FAST telescope we will search for potential periodicity and study emission properties over an extremely wide bandwidth with high sensitivity.
DOI: 10.34808/f1f8-sq28
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC3-MAG1-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 MIC3, MAG1 and ROP1. The produced and purified proteins are composed of amino acid residues from:  A) 67-359 of the MIC3 antigen, 30-452 of the MAG1 antigen, 85-396 of the ROP1 antigen; B) 67-359 of the MIC3 antigen, 30-222 of the MAG1 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: 10.34808/9fxs-6702
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC3-MAG1-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 MIC3, MAG1 and AMA1. The produced and purified proteins are composed of amino acid residues from:  A) 67-359 of the MIC3 antigen, 30-452 of the MAG1 antigen, 67-483 of the AMA1 antigen; B) 67-359 of the MIC3 antigen, 30-222 of the MAG1 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: 10.34808/7b3s-t445
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC1-MAG1-MIC3

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 MIC1, MAG1 and MIC3. The produced and purified proteins are composed of amino acid residues from:  A) 25-182 of the MIC1 antigen, 30-452 of the MAG1 antigen, 67-359 of the MIC3 antigen; B) 25-456 of the MIC1 antigen, 30-452 of the MAG1 antigen, 67-359 of the MIC3 antigen; C) 25-456 of the MIC1 antigen, 30-222 of the MAG1 antigen, 67-359 of the MIC3 antigen; D) 25-182 of the MIC1 antigen, 30-222 of the MAG1 antigen, 67-359 of the MIC3 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/frys-cc18
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC1-MAG1-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 MIC1, MAG1 and AMA1. The produced and purified proteins are composed of amino acid residues from:  A) 25-182 of the MIC1 antigen, 30-452 of the MAG1 antigen, 67-483 of the AMA1 antigen; B) 25-456 of the MIC1 antigen, 30-452 of the MAG1 antigen, 67-483 of the AMA1 antigen; C) 25-456 of the MIC1 antigen, 30-222 of the MAG1 antigen, 67-483 of the AMA1 antigen; D) 25-182 of the MIC1 antigen, 30-222 of the MAG1 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: 10.34808/e0t7-e466
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen MIC1-MAG1-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 MIC1, MAG1 and ROP1. The produced and purified proteins are composed of amino acid residues from:  A) 25-182 of the MIC1 antigen, 30-452 of the MAG1 antigen, 85-396 of the ROP1 antigen; B) 25-456 of the MIC1 antigen, 30-452 of the MAG1 antigen, 85-396 of the ROP1 antigen; C) 25-456 of the MIC1 antigen, 30-222 of the MAG1 antigen, 85-396 of the ROP1 antigen; D) 25-182 of the MIC1 antigen, 30-222 of the MAG1 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: 10.34808/136s-gb90
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-GRA6

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 GRA6. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 30-230 of the GRA6 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: 10.34808/44ze-kk97
title: Construction, production and evaluation of the diagnostic utility of a recombinant Toxoplasma gondii chimeric antigen SAG1-SAG2-MIC1L

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 MIC1. The produced and purified protein is composed of amino acid residues from: 49-311 of the SAG1 antigen, 30-170 of the SAG2 antigen, 25-456 of the MIC1 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: 10.34808/8se4-1387
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/ndha-bz79
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.