Polyamine-Based Thiols in Trypanosomatids: Evolution, Protein Structural Adaptations, and Biological Functions.
Identifieur interne : 000236 ( Main/Exploration ); précédent : 000235; suivant : 000237Polyamine-Based Thiols in Trypanosomatids: Evolution, Protein Structural Adaptations, and Biological Functions.
Auteurs : Bruno Manta [Uruguay] ; Mariana Bonilla [Uruguay] ; Lucía Fiestas [Uruguay] ; Mattia Sturlese [Italie] ; Gustavo Salinas [Uruguay] ; Massimo Bellanda [Italie] ; Marcelo A. Comini [Uruguay]Source :
- Antioxidants & redox signaling [ 1557-7716 ] ; 2018.
Descripteurs français
- KwdFr :
- Glutarédoxines (composition chimique), Glutarédoxines (génétique), Glutarédoxines (métabolisme), Oxydoréduction (MeSH), Polyamines (composition chimique), Polyamines (métabolisme), Spermidine (composition chimique), Spermidine (métabolisme), Thiols (composition chimique), Thiols (métabolisme), Thiorédoxines (composition chimique), Thiorédoxines (génétique), Thiorédoxines (métabolisme), Trypanosomatina (composition chimique), Trypanosomatina (génétique), Trypanosomatina (métabolisme), Évolution moléculaire (MeSH).
- MESH :
- composition chimique : Glutarédoxines, Polyamines, Spermidine, Thiols, Thiorédoxines, Trypanosomatina.
- génétique : Glutarédoxines, Thiorédoxines, Trypanosomatina.
- métabolisme : Glutarédoxines, Polyamines, Spermidine, Thiols, Thiorédoxines, Trypanosomatina.
- Oxydoréduction, Évolution moléculaire.
English descriptors
- KwdEn :
- Evolution, Molecular (MeSH), Glutaredoxins (chemistry), Glutaredoxins (genetics), Glutaredoxins (metabolism), Oxidation-Reduction (MeSH), Polyamines (chemistry), Polyamines (metabolism), Spermidine (chemistry), Spermidine (metabolism), Sulfhydryl Compounds (chemistry), Sulfhydryl Compounds (metabolism), Thioredoxins (chemistry), Thioredoxins (genetics), Thioredoxins (metabolism), Trypanosomatina (chemistry), Trypanosomatina (genetics), Trypanosomatina (metabolism).
- MESH :
- chemical , chemistry : Glutaredoxins, Polyamines, Spermidine, Sulfhydryl Compounds, Thioredoxins.
- chemical , genetics : Glutaredoxins, Thioredoxins.
- chemical , metabolism : Glutaredoxins, Polyamines, Spermidine, Sulfhydryl Compounds, Thioredoxins.
- chemistry : Trypanosomatina.
- genetics : Trypanosomatina.
- metabolism : Trypanosomatina.
- Evolution, Molecular, Oxidation-Reduction.
Abstract
SIGNIFICANCE
Major pathogenic enterobacteria and protozoan parasites from the phylum Euglenozoa, such as trypanosomatids, are endowed with glutathione (GSH)-spermidine (Sp) derivatives that play important roles in signaling and metal and thiol-redox homeostasis. For some Euglenozoa lineages, the GSH-Sp conjugates represent the main redox cosubstrates around which entire new redox systems have evolved. Several proteins underwent molecular adaptations to synthesize and utilize the new polyamine-based thiols. Recent Advances: The genomes of closely related organisms have recently been sequenced, which allows mining and analysis of gene sequences that belong to these peculiar redox systems. Similarly, the three-dimensional structures of several of these proteins have been solved, which allows for comparison with their counterparts in classical redox systems that rely on GSH/glutaredoxin and thioredoxin.
CRITICAL ISSUES
The evolutionary and structural aspects related to the emergence and use of GSH-Sp conjugates in Euglenozoa are reviewed focusing on unique structural specializations that proteins developed to use N
FUTURE DIRECTIONS
A thiol-redox system strictly dependent on trypanothione is a feature unique to trypanosomatids. The physicochemical properties of the polyamine-GSH conjugates were a major driving force for structural adaptation of proteins that use these thiols as ligand and redox cofactor. In fact, the structural differences of indispensable components of this system can be exploited toward selective drug development. Future research should clarify whether additional cellular processes are regulated by the trypanothione system. Antioxid. Redox Signal. 28, 463-486.
DOI: 10.1089/ars.2017.7133
PubMed: 29048199
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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xml:lang="fr">Uruguay</country><wicri:regionArea>2 Laboratorio de Fisicoquímica Biológica, Instituto de Química Biológica , Facultad de Ciencias, Universidad de la República, Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation></author><author><name sortKey="Bonilla, Mariana" sort="Bonilla, Mariana" uniqKey="Bonilla M" first="Mariana" last="Bonilla">Mariana Bonilla</name><affiliation wicri:level="1"><nlm:affiliation>1 Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo , Montevideo, Uruguay .</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>1 Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo , Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>2 Laboratorio de Fisicoquímica Biológica, Instituto de Química Biológica , Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay 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wicri:level="1"><nlm:affiliation>3 Department of Chemical Sciences, Università degli Studi di Padova , Padova, Italy .</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>3 Department of Chemical Sciences, Università degli Studi di Padova , Padova</wicri:regionArea><wicri:noRegion>Padova</wicri:noRegion></affiliation></author><author><name sortKey="Salinas, Gustavo" sort="Salinas, Gustavo" uniqKey="Salinas G" first="Gustavo" last="Salinas">Gustavo Salinas</name><affiliation wicri:level="1"><nlm:affiliation>4 Worm Biology Lab, Institut Pasteur de Montevideo , Montevideo, Uruguay .</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>4 Worm Biology Lab, Institut Pasteur de Montevideo , Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation><affiliation wicri:level="1"><nlm:affiliation>5 Departamento de Biociencias, Facultad de Química, Universidad de la República , Montevideo, Uruguay .</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>5 Departamento de Biociencias, Facultad de Química, Universidad de la República , Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation></author><author><name sortKey="Bellanda, Massimo" sort="Bellanda, Massimo" uniqKey="Bellanda M" first="Massimo" last="Bellanda">Massimo Bellanda</name><affiliation wicri:level="1"><nlm:affiliation>3 Department of Chemical Sciences, Università degli Studi di Padova , Padova, Italy .</nlm:affiliation><country xml:lang="fr">Italie</country><wicri:regionArea>3 Department of Chemical Sciences, Università degli Studi di Padova , Padova</wicri:regionArea><wicri:noRegion>Padova</wicri:noRegion></affiliation></author><author><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name><affiliation wicri:level="1"><nlm:affiliation>1 Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo , Montevideo, Uruguay .</nlm:affiliation><country xml:lang="fr">Uruguay</country><wicri:regionArea>1 Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo , Montevideo</wicri:regionArea><wicri:noRegion>Montevideo</wicri:noRegion></affiliation></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="eISSN">1557-7716</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Evolution, Molecular (MeSH)</term><term>Glutaredoxins (chemistry)</term><term>Glutaredoxins (genetics)</term><term>Glutaredoxins (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Polyamines (chemistry)</term><term>Polyamines (metabolism)</term><term>Spermidine (chemistry)</term><term>Spermidine (metabolism)</term><term>Sulfhydryl Compounds (chemistry)</term><term>Sulfhydryl Compounds (metabolism)</term><term>Thioredoxins (chemistry)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (metabolism)</term><term>Trypanosomatina (chemistry)</term><term>Trypanosomatina (genetics)</term><term>Trypanosomatina (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Glutarédoxines (composition chimique)</term><term>Glutarédoxines (génétique)</term><term>Glutarédoxines (métabolisme)</term><term>Oxydoréduction (MeSH)</term><term>Polyamines (composition chimique)</term><term>Polyamines (métabolisme)</term><term>Spermidine (composition chimique)</term><term>Spermidine (métabolisme)</term><term>Thiols (composition chimique)</term><term>Thiols (métabolisme)</term><term>Thiorédoxines (composition chimique)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term><term>Trypanosomatina (composition chimique)</term><term>Trypanosomatina (génétique)</term><term>Trypanosomatina (métabolisme)</term><term>Évolution moléculaire (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Glutaredoxins</term><term>Polyamines</term><term>Spermidine</term><term>Sulfhydryl Compounds</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="metabolism" xml:lang="en"><term>Glutaredoxins</term><term>Polyamines</term><term>Spermidine</term><term>Sulfhydryl Compounds</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Trypanosomatina</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Glutarédoxines</term><term>Polyamines</term><term>Spermidine</term><term>Thiols</term><term>Thiorédoxines</term><term>Trypanosomatina</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Trypanosomatina</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Glutarédoxines</term><term>Thiorédoxines</term><term>Trypanosomatina</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Trypanosomatina</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Glutarédoxines</term><term>Polyamines</term><term>Spermidine</term><term>Thiols</term><term>Thiorédoxines</term><term>Trypanosomatina</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Evolution, Molecular</term><term>Oxidation-Reduction</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Oxydoréduction</term><term>Évolution moléculaire</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>SIGNIFICANCE</b></p><p>Major pathogenic enterobacteria and protozoan parasites from the phylum Euglenozoa, such as trypanosomatids, are endowed with glutathione (GSH)-spermidine (Sp) derivatives that play important roles in signaling and metal and thiol-redox homeostasis. For some Euglenozoa lineages, the GSH-Sp conjugates represent the main redox cosubstrates around which entire new redox systems have evolved. Several proteins underwent molecular adaptations to synthesize and utilize the new polyamine-based thiols. Recent Advances: The genomes of closely related organisms have recently been sequenced, which allows mining and analysis of gene sequences that belong to these peculiar redox systems. Similarly, the three-dimensional structures of several of these proteins have been solved, which allows for comparison with their counterparts in classical redox systems that rely on GSH/glutaredoxin and thioredoxin.</p></div><div type="abstract" xml:lang="en"><p><b>CRITICAL ISSUES</b></p><p>The evolutionary and structural aspects related to the emergence and use of GSH-Sp conjugates in Euglenozoa are reviewed focusing on unique structural specializations that proteins developed to use N</p></div><div type="abstract" xml:lang="en"><p><b>FUTURE DIRECTIONS</b></p><p>A thiol-redox system strictly dependent on trypanothione is a feature unique to trypanosomatids. The physicochemical properties of the polyamine-GSH conjugates were a major driving force for structural adaptation of proteins that use these thiols as ligand and redox cofactor. In fact, the structural differences of indispensable components of this system can be exploited toward selective drug development. Future research should clarify whether additional cellular processes are regulated by the trypanothione system. Antioxid. Redox Signal. 28, 463-486.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29048199</PMID><DateCompleted><Year>2018</Year><Month>08</Month><Day>21</Day></DateCompleted><DateRevised><Year>2018</Year><Month>08</Month><Day>21</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1557-7716</ISSN><JournalIssue CitedMedium="Internet"><Volume>28</Volume><Issue>6</Issue><PubDate><Year>2018</Year><Month>02</Month><Day>20</Day></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Polyamine-Based Thiols in Trypanosomatids: Evolution, Protein Structural Adaptations, and Biological Functions.</ArticleTitle><Pagination><MedlinePgn>463-486</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1089/ars.2017.7133</ELocationID><Abstract><AbstractText Label="SIGNIFICANCE">Major pathogenic enterobacteria and protozoan parasites from the phylum Euglenozoa, such as trypanosomatids, are endowed with glutathione (GSH)-spermidine (Sp) derivatives that play important roles in signaling and metal and thiol-redox homeostasis. For some Euglenozoa lineages, the GSH-Sp conjugates represent the main redox cosubstrates around which entire new redox systems have evolved. Several proteins underwent molecular adaptations to synthesize and utilize the new polyamine-based thiols. Recent Advances: The genomes of closely related organisms have recently been sequenced, which allows mining and analysis of gene sequences that belong to these peculiar redox systems. Similarly, the three-dimensional structures of several of these proteins have been solved, which allows for comparison with their counterparts in classical redox systems that rely on GSH/glutaredoxin and thioredoxin.</AbstractText><AbstractText Label="CRITICAL ISSUES">The evolutionary and structural aspects related to the emergence and use of GSH-Sp conjugates in Euglenozoa are reviewed focusing on unique structural specializations that proteins developed to use N<sup>1</sup>,N<sup>8</sup>-bisglutathionylspermidine (trypanothione) as redox cosubstrate. An updated overview on the biochemical and biological significance of the major enzymatic activities is also provided.</AbstractText><AbstractText Label="FUTURE DIRECTIONS">A thiol-redox system strictly dependent on trypanothione is a feature unique to trypanosomatids. The physicochemical properties of the polyamine-GSH conjugates were a major driving force for structural adaptation of proteins that use these thiols as ligand and redox cofactor. In fact, the structural differences of indispensable components of this system can be exploited toward selective drug development. Future research should clarify whether additional cellular processes are regulated by the trypanothione system. Antioxid. Redox Signal. 28, 463-486.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Manta</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>1 Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>2 Laboratorio de Fisicoquímica Biológica, Instituto de Química Biológica , Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bonilla</LastName><ForeName>Mariana</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>1 Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>2 Laboratorio de Fisicoquímica Biológica, Instituto de Química Biológica , Facultad de Ciencias, Universidad de la República, Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fiestas</LastName><ForeName>Lucía</ForeName><Initials>L</Initials><AffiliationInfo><Affiliation>1 Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Sturlese</LastName><ForeName>Mattia</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>3 Department of Chemical Sciences, Università degli Studi di Padova , Padova, Italy .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Salinas</LastName><ForeName>Gustavo</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>4 Worm Biology Lab, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>5 Departamento de Biociencias, Facultad de Química, Universidad de la República , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bellanda</LastName><ForeName>Massimo</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>3 Department of Chemical Sciences, Università degli Studi di Padova , Padova, Italy .</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Comini</LastName><ForeName>Marcelo A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>1 Laboratory Redox Biology of Trypanosomes, Institut Pasteur de Montevideo , Montevideo, Uruguay .</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>11</Month><Day>27</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011073">Polyamines</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013438">Sulfhydryl Compounds</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>U87FK77H25</RegistryNumber><NameOfSubstance UI="D013095">Spermidine</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D019143" MajorTopicYN="N">Evolution, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011073" MajorTopicYN="N">Polyamines</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013095" MajorTopicYN="N">Spermidine</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013438" MajorTopicYN="N">Sulfhydryl Compounds</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014351" MajorTopicYN="N">Trypanosomatina</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">glutathione</Keyword><Keyword MajorTopicYN="Y">kinetoplastid</Keyword><Keyword MajorTopicYN="Y">oxidoreductase</Keyword><Keyword MajorTopicYN="Y">redox</Keyword><Keyword MajorTopicYN="Y">spermidine</Keyword><Keyword MajorTopicYN="Y">trypanothione</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>10</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>8</Month><Day>22</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>10</Month><Day>20</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29048199</ArticleId><ArticleId IdType="doi">10.1089/ars.2017.7133</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Italie</li><li>Uruguay</li></country></list><tree><country name="Uruguay"><noRegion><name sortKey="Manta, Bruno" sort="Manta, Bruno" uniqKey="Manta B" first="Bruno" last="Manta">Bruno Manta</name></noRegion><name sortKey="Bonilla, Mariana" sort="Bonilla, Mariana" uniqKey="Bonilla M" first="Mariana" last="Bonilla">Mariana Bonilla</name><name sortKey="Bonilla, Mariana" sort="Bonilla, Mariana" uniqKey="Bonilla M" first="Mariana" last="Bonilla">Mariana Bonilla</name><name sortKey="Comini, Marcelo A" sort="Comini, Marcelo A" uniqKey="Comini M" first="Marcelo A" last="Comini">Marcelo A. Comini</name><name sortKey="Fiestas, Lucia" sort="Fiestas, Lucia" uniqKey="Fiestas L" first="Lucía" last="Fiestas">Lucía Fiestas</name><name sortKey="Manta, Bruno" sort="Manta, Bruno" uniqKey="Manta B" first="Bruno" last="Manta">Bruno Manta</name><name sortKey="Salinas, Gustavo" sort="Salinas, Gustavo" uniqKey="Salinas G" first="Gustavo" last="Salinas">Gustavo Salinas</name><name sortKey="Salinas, Gustavo" sort="Salinas, Gustavo" uniqKey="Salinas G" first="Gustavo" last="Salinas">Gustavo Salinas</name></country><country name="Italie"><noRegion><name sortKey="Sturlese, Mattia" sort="Sturlese, Mattia" uniqKey="Sturlese M" first="Mattia" last="Sturlese">Mattia Sturlese</name></noRegion><name sortKey="Bellanda, Massimo" sort="Bellanda, Massimo" uniqKey="Bellanda M" first="Massimo" last="Bellanda">Massimo Bellanda</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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