Cloning, expression, purification, and kinetic characterization of mitochondrial thioredoxin (TsTrx2), cytosolic thioredoxin (TsTrx1), and glutaredoxin (TsGrx1) from Taenia solium.
Identifieur interne : 000186 ( Main/Exploration ); précédent : 000185; suivant : 000187Cloning, expression, purification, and kinetic characterization of mitochondrial thioredoxin (TsTrx2), cytosolic thioredoxin (TsTrx1), and glutaredoxin (TsGrx1) from Taenia solium.
Auteurs : Gabriela Nava [Mexique] ; Gerardo Maldonado [Mexique] ; Agustin Plancarte [Mexique]Source :
- Parasitology research [ 1432-1955 ] ; 2019.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Cadres ouverts de lecture (MeSH), Cinétique (MeSH), Clonage moléculaire (MeSH), Cysticercus (génétique), Cysticercus (isolement et purification), Cysticercus (métabolisme), Cytosol (composition chimique), Cytosol (métabolisme), Disulfures (métabolisme), Escherichia coli (génétique), Escherichia coli (métabolisme), Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (isolement et purification), Glutarédoxines (métabolisme), Glutathion (métabolisme), Lapins (MeSH), Mitochondries (composition chimique), Mitochondries (génétique), Mitochondries (métabolisme), Séquence d'acides aminés (MeSH), Taenia solium (génétique), Taenia solium (métabolisme), Thiorédoxines (composition chimique), Thiorédoxines (génétique), Thiorédoxines (isolement et purification), Thiorédoxines (métabolisme), Éthanol (analogues et dérivés), Éthanol (métabolisme).
- MESH :
- analogues et dérivés : Éthanol.
- composition chimique : Cytosol, Glutarédoxines, Mitochondries, Thiorédoxines.
- génétique : Cysticercus, Escherichia coli, Glutarédoxines, Mitochondries, Taenia solium, Thiorédoxines.
- isolement et purification : Cysticercus, Glutarédoxines, Thiorédoxines.
- métabolisme : Cysticercus, Cytosol, Disulfures, Escherichia coli, Glutarédoxines, Glutathion, Mitochondries, Taenia solium, Thiorédoxines, Éthanol.
- Animaux, Cadres ouverts de lecture, Cinétique, Clonage moléculaire, Lapins, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Cloning, Molecular (MeSH), Cysticercus (genetics), Cysticercus (isolation & purification), Cysticercus (metabolism), Cytosol (chemistry), Cytosol (metabolism), Disulfides (metabolism), Escherichia coli (genetics), Escherichia coli (metabolism), Ethanol (analogs & derivatives), Ethanol (metabolism), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (isolation & purification), Glutaredoxins (metabolism), Glutathione (metabolism), Kinetics (MeSH), Mitochondria (chemistry), Mitochondria (genetics), Mitochondria (metabolism), Open Reading Frames (MeSH), Rabbits (MeSH), Taenia solium (genetics), Taenia solium (metabolism), Thioredoxins (chemistry), Thioredoxins (genetics), Thioredoxins (isolation & purification), Thioredoxins (metabolism).
- MESH :
- chemical , analogs & derivatives : Ethanol.
- chemical , chemistry : Glutaredoxins, Thioredoxins.
- chemical , genetics : Glutaredoxins, Thioredoxins.
- chemical , isolation & purification : Glutaredoxins, Thioredoxins.
- chemical , metabolism : Disulfides, Ethanol, Glutaredoxins, Glutathione, Thioredoxins.
- chemistry : Cytosol, Mitochondria.
- genetics : Cysticercus, Escherichia coli, Mitochondria, Taenia solium.
- isolation & purification : Cysticercus.
- metabolism : Cysticercus, Cytosol, Escherichia coli, Mitochondria, Taenia solium.
- Amino Acid Sequence, Animals, Cloning, Molecular, Kinetics, Open Reading Frames, Rabbits.
Abstract
We report the complete coding sequences of mitochondrial thioredoxin (TsTrx2) and glutaredoxin (TsGrx1) from the cysticerci of T. solium. The full-length DNA of the TsTrx2 gene shows two introns of 88 and 77 bp and three exons. The TsTrx2 gene contains a single ORF of 423 bp, encoding 140 amino acid residues with an estimated molecular weight of 15,560 Da. A conserved C64NPC67 active site and a 30-amino acid extension at its N-terminus were identified. An insulin reduction reaction was used to determine whether it was a functional recombinant protein. The full-length DNA of the TsGrx1 gene shows one intron of 39 bp and a single ORF of 315 bp, encoding 105 amino acid residues with an estimated molecular weight of 12,582 Da. Sequence analysis revealed a conserved dithiol C34PYC37 active site, GSH-binding motifs (CXXC, Lys and Gln/Arg, TVP, and CXD), and a conserved Gly-Gly motif. The r-TsGrx1 kinetic constants for glutathione (GSH) and 2-hydroxyethyl disulfide (HED) were determined. In addition, cytosolic thioredoxin (TsTrx1), as reported by (Jiménez et al., Biomed Res Int 2015:453469, 2015), was cloned and expressed, and its catalytic constants were obtained along with those of the other two reductases. Rabbit-specific antibodies showed immune cross-reactions between TsTrx1 and TsTrx2 but not with TsGrx1. Both TsTGRs as reported by (Plancarte and Nava, Exp Parasitol 149:65-73, 2015) were biochemically purified to obtain and compare the catalytic constants for their natural substrates, r-TsTrx1, and r-TsTrx2, compared to those for Trx-S2E. coli. In addition, we determined the catalytic differences between the glutaredoxin activity of the TsTGRs compared with r-TsGrx1. These data increase the knowledge of the thioredoxin and GSH systems in T. solium, which is relevant for detoxification and immune evasion.
DOI: 10.1007/s00436-019-06336-4
PubMed: 31062084
Affiliations:
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México</wicri:noRegion></affiliation></author><author><name sortKey="Maldonado, Gerardo" sort="Maldonado, Gerardo" uniqKey="Maldonado G" first="Gerardo" last="Maldonado">Gerardo Maldonado</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, UNAM, Edificio "A" de Investigación, 6° piso, 04510, Ciudad de México, Mexico.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, UNAM, Edificio "A" de Investigación, 6° piso, 04510, Ciudad de México</wicri:regionArea><wicri:noRegion>Ciudad de México</wicri:noRegion></affiliation></author><author><name sortKey="Plancarte, Agustin" sort="Plancarte, Agustin" uniqKey="Plancarte A" first="Agustin" last="Plancarte">Agustin Plancarte</name><affiliation wicri:level="1"><nlm:affiliation>Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, UNAM, Edificio "A" de Investigación, 6° piso, 04510, Ciudad de México, Mexico. apc@unam.mx.</nlm:affiliation><country xml:lang="fr">Mexique</country><wicri:regionArea>Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, UNAM, Edificio "A" de Investigación, 6° piso, 04510, Ciudad de México</wicri:regionArea><wicri:noRegion>Ciudad de México</wicri:noRegion></affiliation></author></analytic><series><title level="j">Parasitology research</title><idno type="eISSN">1432-1955</idno><imprint><date when="2019" type="published">2019</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Cloning, Molecular (MeSH)</term><term>Cysticercus (genetics)</term><term>Cysticercus (isolation & purification)</term><term>Cysticercus (metabolism)</term><term>Cytosol (chemistry)</term><term>Cytosol (metabolism)</term><term>Disulfides (metabolism)</term><term>Escherichia coli (genetics)</term><term>Escherichia coli (metabolism)</term><term>Ethanol (analogs & derivatives)</term><term>Ethanol (metabolism)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (isolation & purification)</term><term>Glutaredoxins (metabolism)</term><term>Glutathione (metabolism)</term><term>Kinetics (MeSH)</term><term>Mitochondria (chemistry)</term><term>Mitochondria (genetics)</term><term>Mitochondria (metabolism)</term><term>Open Reading Frames (MeSH)</term><term>Rabbits (MeSH)</term><term>Taenia solium (genetics)</term><term>Taenia solium (metabolism)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (isolation & purification)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Cadres ouverts de lecture (MeSH)</term><term>Cinétique (MeSH)</term><term>Clonage moléculaire (MeSH)</term><term>Cysticercus (génétique)</term><term>Cysticercus (isolement et purification)</term><term>Cysticercus (métabolisme)</term><term>Cytosol (composition chimique)</term><term>Cytosol (métabolisme)</term><term>Disulfures (métabolisme)</term><term>Escherichia coli (génétique)</term><term>Escherichia coli (métabolisme)</term><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (isolement et purification)</term><term>Glutarédoxines (métabolisme)</term><term>Glutathion (métabolisme)</term><term>Lapins (MeSH)</term><term>Mitochondries (composition chimique)</term><term>Mitochondries (génétique)</term><term>Mitochondries (métabolisme)</term><term>Séquence d'acides aminés (MeSH)</term><term>Taenia solium (génétique)</term><term>Taenia solium (métabolisme)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (isolement et purification)</term><term>Thiorédoxines (métabolisme)</term><term>Éthanol (analogues et dérivés)</term><term>Éthanol (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Ethanol</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Glutaredoxins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Glutaredoxins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Ethanol</term><term>Glutaredoxins</term><term>Glutathione</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="analogues et dérivés" xml:lang="fr"><term>Éthanol</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Cytosol</term><term>Mitochondria</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cytosol</term><term>Glutarédoxines</term><term>Mitochondries</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Cysticercus</term><term>Escherichia coli</term><term>Mitochondria</term><term>Taenia solium</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Cysticercus</term><term>Escherichia coli</term><term>Glutarédoxines</term><term>Mitochondries</term><term>Taenia solium</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="isolation & purification" xml:lang="en"><term>Cysticercus</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Cysticercus</term><term>Glutarédoxines</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Cysticercus</term><term>Cytosol</term><term>Escherichia coli</term><term>Mitochondria</term><term>Taenia solium</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysticercus</term><term>Cytosol</term><term>Disulfures</term><term>Escherichia coli</term><term>Glutarédoxines</term><term>Glutathion</term><term>Mitochondries</term><term>Taenia solium</term><term>Thiorédoxines</term><term>Éthanol</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Cloning, Molecular</term><term>Kinetics</term><term>Open Reading Frames</term><term>Rabbits</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Cadres ouverts de lecture</term><term>Cinétique</term><term>Clonage moléculaire</term><term>Lapins</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We report the complete coding sequences of mitochondrial thioredoxin (TsTrx2) and glutaredoxin (TsGrx1) from the cysticerci of T. solium. The full-length DNA of the TsTrx2 gene shows two introns of 88 and 77 bp and three exons. The TsTrx2 gene contains a single ORF of 423 bp, encoding 140 amino acid residues with an estimated molecular weight of 15,560 Da. A conserved C64NPC67 active site and a 30-amino acid extension at its N-terminus were identified. An insulin reduction reaction was used to determine whether it was a functional recombinant protein. The full-length DNA of the TsGrx1 gene shows one intron of 39 bp and a single ORF of 315 bp, encoding 105 amino acid residues with an estimated molecular weight of 12,582 Da. Sequence analysis revealed a conserved dithiol C34PYC37 active site, GSH-binding motifs (CXXC, Lys and Gln/Arg, TVP, and CXD), and a conserved Gly-Gly motif. The r-TsGrx1 kinetic constants for glutathione (GSH) and 2-hydroxyethyl disulfide (HED) were determined. In addition, cytosolic thioredoxin (TsTrx1), as reported by (Jiménez et al., Biomed Res Int 2015:453469, 2015), was cloned and expressed, and its catalytic constants were obtained along with those of the other two reductases. Rabbit-specific antibodies showed immune cross-reactions between TsTrx1 and TsTrx2 but not with TsGrx1. Both TsTGRs as reported by (Plancarte and Nava, Exp Parasitol 149:65-73, 2015) were biochemically purified to obtain and compare the catalytic constants for their natural substrates, r-TsTrx1, and r-TsTrx2, compared to those for Trx-S<sub>2</sub>E. coli. In addition, we determined the catalytic differences between the glutaredoxin activity of the TsTGRs compared with r-TsGrx1. These data increase the knowledge of the thioredoxin and GSH systems in T. solium, which is relevant for detoxification and immune evasion.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" IndexingMethod="Curated" Owner="NLM"><PMID Version="1">31062084</PMID><DateCompleted><Year>2019</Year><Month>08</Month><Day>12</Day></DateCompleted><DateRevised><Year>2020</Year><Month>02</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1432-1955</ISSN><JournalIssue CitedMedium="Internet"><Volume>118</Volume><Issue>6</Issue><PubDate><Year>2019</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Parasitology research</Title><ISOAbbreviation>Parasitol Res</ISOAbbreviation></Journal><ArticleTitle>Cloning, expression, purification, and kinetic characterization of mitochondrial thioredoxin (TsTrx2), cytosolic thioredoxin (TsTrx1), and glutaredoxin (TsGrx1) from Taenia solium.</ArticleTitle><Pagination><MedlinePgn>1785-1797</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1007/s00436-019-06336-4</ELocationID><Abstract><AbstractText>We report the complete coding sequences of mitochondrial thioredoxin (TsTrx2) and glutaredoxin (TsGrx1) from the cysticerci of T. solium. The full-length DNA of the TsTrx2 gene shows two introns of 88 and 77 bp and three exons. The TsTrx2 gene contains a single ORF of 423 bp, encoding 140 amino acid residues with an estimated molecular weight of 15,560 Da. A conserved C64NPC67 active site and a 30-amino acid extension at its N-terminus were identified. An insulin reduction reaction was used to determine whether it was a functional recombinant protein. The full-length DNA of the TsGrx1 gene shows one intron of 39 bp and a single ORF of 315 bp, encoding 105 amino acid residues with an estimated molecular weight of 12,582 Da. Sequence analysis revealed a conserved dithiol C34PYC37 active site, GSH-binding motifs (CXXC, Lys and Gln/Arg, TVP, and CXD), and a conserved Gly-Gly motif. The r-TsGrx1 kinetic constants for glutathione (GSH) and 2-hydroxyethyl disulfide (HED) were determined. In addition, cytosolic thioredoxin (TsTrx1), as reported by (Jiménez et al., Biomed Res Int 2015:453469, 2015), was cloned and expressed, and its catalytic constants were obtained along with those of the other two reductases. Rabbit-specific antibodies showed immune cross-reactions between TsTrx1 and TsTrx2 but not with TsGrx1. Both TsTGRs as reported by (Plancarte and Nava, Exp Parasitol 149:65-73, 2015) were biochemically purified to obtain and compare the catalytic constants for their natural substrates, r-TsTrx1, and r-TsTrx2, compared to those for Trx-S<sub>2</sub>E. coli. In addition, we determined the catalytic differences between the glutaredoxin activity of the TsTGRs compared with r-TsGrx1. These data increase the knowledge of the thioredoxin and GSH systems in T. solium, which is relevant for detoxification and immune evasion.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Nava</LastName><ForeName>Gabriela</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, UNAM, Edificio "A" de Investigación, 6° piso, 04510, Ciudad de México, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Maldonado</LastName><ForeName>Gerardo</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, UNAM, Edificio "A" de Investigación, 6° piso, 04510, Ciudad de México, Mexico.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Plancarte</LastName><ForeName>Agustin</ForeName><Initials>A</Initials><Identifier Source="ORCID">http://orcid.org/0000-0001-9151-4063</Identifier><AffiliationInfo><Affiliation>Departamento de Microbiología y Parasitología, Facultad de Medicina, Universidad Nacional Autónoma de Mexico, UNAM, Edificio "A" de Investigación, 6° piso, 04510, Ciudad de México, Mexico. apc@unam.mx.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2019</Year><Month>05</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>Parasitol Res</MedlineTA><NlmUniqueID>8703571</NlmUniqueID><ISSNLinking>0932-0113</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>3K9958V90M</RegistryNumber><NameOfSubstance UI="D000431">Ethanol</NameOfSubstance></Chemical><Chemical><RegistryNumber>45543L74BS</RegistryNumber><NameOfSubstance UI="C031319">2-hydroxyethyl disulfide</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003001" MajorTopicYN="N">Cloning, 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