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dc.contributor.author
Giordana, Lucila
dc.contributor.author
Suárez Mantilla, Brian
dc.contributor.author
Santana, Marianela
dc.contributor.author
Silber, Ariel Mariano
dc.contributor.author
Nowicki, Cristina
dc.date.available
2018-01-04T14:26:25Z
dc.date.issued
2014-03
dc.identifier.citation
Nowicki, Cristina; Silber, Ariel Mariano; Santana, Marianela; Suárez Mantilla, Brian; Giordana, Lucila; Cystathionine γ-lyase, an Enzyme Related to the Reverse Transsulfuration Pathway, is Functional in Leishmania spp.; Wiley Blackwell Publishing, Inc; Journal of Eukaryotic Microbiology; 61; 2; 3-2014; 204-213
dc.identifier.issn
1066-5234
dc.identifier.uri
http://hdl.handle.net/11336/32287
dc.description.abstract
Leishmania parasites seem capable of producing cysteine by de novo biosynthesis, similarly to bacteria, some pathogenic protists, and plants. In Leishmania spp., cysteine synthase (CS) and cystathionine β-synthase (CBS) are expected to participate in this metabolic process. Moreover, the reverse transsulfuration pathway (RTP) is also predicted to be operative in this trypanosomatid because CBS also catalyzes the condensation of serine with homocysteine, and a gene encoding a putative cystathionine γ-lyase (CGL) is present in all the sequenced genomes. Our results show that indeed, Leishmania major CGL is able to rescue the wild-type phenotype of a Saccharomyces cerevisiae CGL-null mutant and is susceptible to inhibition by an irreversible CGL inhibitor, DL-propargylglycine (PAG). In Leishmania promastigotes, CGL and CS are cytosolic enzymes. The coexistence of de novo synthesis with the RTP is extremely rare in most living organisms; however, despite this potentially high redundancy in cysteine production, PAG arrests the proliferation of L. major promastigotes with an IC50 of approximately 65 μM. These findings raise new questions regarding the biological role of CGL in these pathogens and indicate the need for understanding the molecular mechanism of PAG action in vivo to identify the potential targets affected by this drug.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Wiley Blackwell Publishing, Inc
dc.rights
info:eu-repo/semantics/restrictedAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Leishmania Parasites
dc.subject
Dl-Propargylglycine
dc.subject.classification
Otras Ciencias Biológicas
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Ciencias Biológicas
dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
dc.title
Cystathionine γ-lyase, an Enzyme Related to the Reverse Transsulfuration Pathway, is Functional in Leishmania spp.
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-01-03T19:05:22Z
dc.journal.volume
61
dc.journal.number
2
dc.journal.pagination
204-213
dc.journal.pais
Reino Unido
dc.journal.ciudad
Londres
dc.description.fil
Fil: Giordana, Lucila. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.description.fil
Fil: Suárez Mantilla, Brian. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Santana, Marianela. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.description.fil
Fil: Silber, Ariel Mariano. Universidade de Sao Paulo; Brasil
dc.description.fil
Fil: Nowicki, Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Química y Físico-Química Biológicas "Prof. Alejandro C. Paladini". Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Química y Físico-Química Biológicas; Argentina
dc.journal.title
Journal of Eukaryotic Microbiology
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://onlinelibrary.wiley.com/doi/10.1111/jeu.12100/abstract
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1111/jeu.12100


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