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dc.contributor.author
Leyria, Jimena
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dc.contributor.author
Fruttero, Leonardo Luis
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dc.contributor.author
Ligabue Braun, Rodrigo
dc.contributor.author
Defferrari, Marina S.
dc.contributor.author
Arrese, Estela L.
dc.contributor.author
Soulages, José L.
dc.contributor.author
Settembrini, Beatriz Patricia
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dc.contributor.author
Carlini, Célia Regina R S
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dc.contributor.author
Canavoso, Lilian Etelvina
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dc.date.available
2020-01-27T18:02:57Z
dc.date.issued
2018-02
dc.identifier.citation
Leyria, Jimena; Fruttero, Leonardo Luis; Ligabue Braun, Rodrigo; Defferrari, Marina S.; Arrese, Estela L.; et al.; DmCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima (Hemiptera: Reduviidae): Purification, bioinformatic analyses and the significance of its interaction with lipophorin in the internalization by developing oocytes; Pergamon-Elsevier Science Ltd; Journal of Insect Physiology; 105; 2-2018; 28-39
dc.identifier.issn
0022-1910
dc.identifier.uri
http://hdl.handle.net/11336/95854
dc.description.abstract
DmCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima, is synthesized by the fat body and the ovary and functions as yolk protein precursor. Functionally, DmCatD is involved in vitellin proteolysis. In this work, we purified and sequenced DmCatD, performed bioinformatic analyses and investigated the events involved in its targeting and storage in developing oocytes. By ion exchange and gel filtration chromatography, DmCatD was purified from egg homogenates and its identity was confirmed by mass spectrometry. Approximately 73% of the full-length transcript was sequenced. The phylogeny indicated that DmCatD has features which suggest its distancing from “classical” cathepsins D. Bioinformatic analyses using a chimeric construct were employed to predict post-translational modifications. Structural modeling showed that DmCatD exhibited the expected folding for this type of enzyme, and an active site with conserved architecture. The interaction between DmCatD and lipophorin in the hemolymph was demonstrated by co-immunoprecipitation. Colocalization of both proteins in developing oocyte membranes and yolk bodies was detected by immunofluorescence. Docking assays favoring the interaction DmCatD-lipophorin were carried out after modeling lipophorin of a related triatomine species. Our results suggest that lipophorin acts as a carrier for DmCatD to facilitate its further internalization by the oocytes. The mechanisms involved in the uptake of peptidases within the oocytes of insects have not been reported. This is the first experimental work supporting the interaction between cathepsin D and lipophorin in an insect species, enabling us to propose a pathway for its targeting and storage in developing oocytes.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Pergamon-Elsevier Science Ltd
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.subject
CATHEPSIN D
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LIPOPHORIN
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OOCYTE
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TRIATOMINAE
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VITELLOGENESIS
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
DmCatD, a cathepsin D-like peptidase of the hematophagous insect Dipetalogaster maxima (Hemiptera: Reduviidae): Purification, bioinformatic analyses and the significance of its interaction with lipophorin in the internalization by developing oocytes
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2019-10-22T16:39:17Z
dc.journal.volume
105
dc.journal.pagination
28-39
dc.journal.pais
Estados Unidos
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dc.description.fil
Fil: Leyria, Jimena. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina
dc.description.fil
Fil: Fruttero, Leonardo Luis. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina. Pontificia Universidade Católica do Rio Grande do Sul; Brasil. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
dc.description.fil
Fil: Ligabue Braun, Rodrigo. Universidade Federal do Rio Grande do Sul; Brasil
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Fil: Defferrari, Marina S.. University of Toronto; Canadá
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Fil: Arrese, Estela L.. Oklahoma State University; Estados Unidos
dc.description.fil
Fil: Soulages, José L.. Oklahoma State University; Estados Unidos
dc.description.fil
Fil: Settembrini, Beatriz Patricia. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Museo Argentino de Ciencias Naturales “Bernardino Rivadavia”; Argentina
dc.description.fil
Fil: Carlini, Célia Regina R S. Pontificia Universidade Católica do Rio Grande do Sul; Brasil
dc.description.fil
Fil: Canavoso, Lilian Etelvina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Departamento de Bioquímica Clínica; Argentina
dc.journal.title
Journal of Insect Physiology
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://doi.org/10.1016/j.jinsphys.2018.01.002
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/sciencedirect.com/science/article/pii/S0022191017303396
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5892828/
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