Characterization of 14-3‑3 Isoforms Expressed in the Echinococcus granulosus Pathogenic Larval Stage
Author
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Teichmann, Aline
Author
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Vargas, Daiani M.
Author
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Monteiro, Karina M.
Author
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Meneghetti, Bruna V.
Author
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Dutra, Cristine S.
Author
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Paredes, Rodolfo
Author
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Galanti Garrone, Norbel
Author
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Zaha, Arnaldo
Author
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Ferreira, Henrique B.
Admission date
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2015-08-18T20:22:26Z
Available date
dc.date.available
2015-08-18T20:22:26Z
Publication date
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2015
Cita de ítem
dc.identifier.citation
Journal of Proteome Research. 2015, 14, 1700−1715
en_US
Identifier
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DOI: 10.1021/pr5010136
Identifier
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https://repositorio.uchile.cl/handle/2250/132894
General note
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Artículo de publicación ISI
en_US
Abstract
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The 14-3-3 protein family of eukaryotic
regulators was studied in Echinococcus granulosus, the causative
agent of cystic hydatid disease. These proteins mediate
important cellular processes in eukaryotes and are expected
to play important roles in parasite biology. Six isoforms of E.
granulosus 14-3-3 genes and proteins (Eg14-3-3.1−6) were
analyzed, and their phylogenetic relationships were established
with bona f ide 14-3-3 orthologous proteins from eukaryotic
species. Eg14-3-3 isoforms with previous evidence of
expression (Eg14-3-3.1−4) in E. granulosus pathogenic larval
stage (metacestode) were cloned, and recombinant proteins
were used for functional studies. These protein isoforms were
detected in different components of E. granulosus metacestode,
including interface components with the host. The roles that are played by Eg14-3-3 proteins in parasite biology were inferred
from the repertoires of interacting proteins with each isoform, as assessed by gel overlay, cross-linking, and affinity
chromatography assays. A total of 95 Eg14-3-3 protein ligands were identified by mass spectrometry. Eg14-3-3 isoforms have
shared partners (44 proteins), indicating some overlapping functions; however, they also bind exclusive partners (51 proteins),
suggesting Eg14-3-3 functional specialization. These ligand repertoires indicate the involvement of Eg14-3-3 proteins in multiple
biochemical pathways in the E. granulosus metacestode and note some degree of isoform specialization.