Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>

Autores
Giorello, Alejandra Nahili; Kennedy, Malcom W.; Butti, Marcos Javier; Córsico, Betina; Radman, Nilda Ester; Franchini, Gisela Raquel
Año de publicación
2017
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Background: The giant kidney worm, Dioctophyme renale, is a debilitating and potentially lethal parasite that inhabits and destroys, typically host’s right kidney, and may also be found in ectopic sites. It is circumglobally distributed, mainly in dogs, and is increasingly regarded as a threat to other domestic animals and humans. There is little information on the parasite’s true incidence, or immune responses to it, and none on its biochemistry and molecular biology. Results: We characterised the soluble proteins of body wall, intestine, gonads and pseudocelomic fluid (PCF) of adult parasites. Two proteins, P17 and P44, dominate the PCF of both male and females. P17 is of 16,622 Da by mass spectrometry, and accounts for the intense red colour of the adult parasites. It may function to carry or scavenge oxygen and be related to the ‘nemoglobins’ found in other nematode clades. P44 is of 44,460 Da and was found to associate with fatty acids by thin layer chromatography. Using environment-sensitive fluorescent lipid probes, P44 proved to be a hydrophobic ligand-binding protein with a binding site that is highly apolar, and competitive displacement experiments showed that P44 binds fatty acids. It may therefore have a role in distributing lipids within the parasites and, if also secreted, might influence local inflammatory and tissue responses. N-terminal and internal peptide amino-acid sequences of P44 indicate a relationship with a cysteine- and histidinerich protein of unknown function from Trichinella spiralis. Conclusions: The dominant proteins of D. renale PCF are, like those of large ascaridids, likely to be involved in lipid and oxygen handling, although there is evidence of strong divergence between the two groups.
Facultad de Ciencias Veterinarias
Materia
Ciencias Veterinarias
Dioctophyme renale
Nematodos
Parasitología
lipid-binding proteins
nematodes
emerging zoonose
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/62745

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network_name_str SEDICI (UNLP)
spelling Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>Giorello, Alejandra NahiliKennedy, Malcom W.Butti, Marcos JavierCórsico, BetinaRadman, Nilda EsterFranchini, Gisela RaquelCiencias VeterinariasDioctophyme renaleNematodosParasitologíalipid-binding proteinsnematodesemerging zoonoseBackground: The giant kidney worm, Dioctophyme renale, is a debilitating and potentially lethal parasite that inhabits and destroys, typically host’s right kidney, and may also be found in ectopic sites. It is circumglobally distributed, mainly in dogs, and is increasingly regarded as a threat to other domestic animals and humans. There is little information on the parasite’s true incidence, or immune responses to it, and none on its biochemistry and molecular biology. Results: We characterised the soluble proteins of body wall, intestine, gonads and pseudocelomic fluid (PCF) of adult parasites. Two proteins, P17 and P44, dominate the PCF of both male and females. P17 is of 16,622 Da by mass spectrometry, and accounts for the intense red colour of the adult parasites. It may function to carry or scavenge oxygen and be related to the ‘nemoglobins’ found in other nematode clades. P44 is of 44,460 Da and was found to associate with fatty acids by thin layer chromatography. Using environment-sensitive fluorescent lipid probes, P44 proved to be a hydrophobic ligand-binding protein with a binding site that is highly apolar, and competitive displacement experiments showed that P44 binds fatty acids. It may therefore have a role in distributing lipids within the parasites and, if also secreted, might influence local inflammatory and tissue responses. N-terminal and internal peptide amino-acid sequences of P44 indicate a relationship with a cysteine- and histidinerich protein of unknown function from Trichinella spiralis. Conclusions: The dominant proteins of D. renale PCF are, like those of large ascaridids, likely to be involved in lipid and oxygen handling, although there is evidence of strong divergence between the two groups.Facultad de Ciencias Veterinarias2017info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://sedici.unlp.edu.ar/handle/10915/62745enginfo:eu-repo/semantics/altIdentifier/url/https://parasitesandvectors.biomedcentral.com/articles/10.1186/s13071-017-2388-xinfo:eu-repo/semantics/altIdentifier/issn/1756-3305info:eu-repo/semantics/altIdentifier/doi/10.1186/s13071-017-2388-xinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-03T10:40:41Zoai:sedici.unlp.edu.ar:10915/62745Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-03 10:40:42.027SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>
title Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>
spellingShingle Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>
Giorello, Alejandra Nahili
Ciencias Veterinarias
Dioctophyme renale
Nematodos
Parasitología
lipid-binding proteins
nematodes
emerging zoonose
title_short Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>
title_full Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>
title_fullStr Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>
title_full_unstemmed Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>
title_sort Identification and characterization of the major pseudocoelomic proteins of the giant kidney worm, <i>Dioctophyme renale</i>
dc.creator.none.fl_str_mv Giorello, Alejandra Nahili
Kennedy, Malcom W.
Butti, Marcos Javier
Córsico, Betina
Radman, Nilda Ester
Franchini, Gisela Raquel
author Giorello, Alejandra Nahili
author_facet Giorello, Alejandra Nahili
Kennedy, Malcom W.
Butti, Marcos Javier
Córsico, Betina
Radman, Nilda Ester
Franchini, Gisela Raquel
author_role author
author2 Kennedy, Malcom W.
Butti, Marcos Javier
Córsico, Betina
Radman, Nilda Ester
Franchini, Gisela Raquel
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Veterinarias
Dioctophyme renale
Nematodos
Parasitología
lipid-binding proteins
nematodes
emerging zoonose
topic Ciencias Veterinarias
Dioctophyme renale
Nematodos
Parasitología
lipid-binding proteins
nematodes
emerging zoonose
dc.description.none.fl_txt_mv Background: The giant kidney worm, Dioctophyme renale, is a debilitating and potentially lethal parasite that inhabits and destroys, typically host’s right kidney, and may also be found in ectopic sites. It is circumglobally distributed, mainly in dogs, and is increasingly regarded as a threat to other domestic animals and humans. There is little information on the parasite’s true incidence, or immune responses to it, and none on its biochemistry and molecular biology. Results: We characterised the soluble proteins of body wall, intestine, gonads and pseudocelomic fluid (PCF) of adult parasites. Two proteins, P17 and P44, dominate the PCF of both male and females. P17 is of 16,622 Da by mass spectrometry, and accounts for the intense red colour of the adult parasites. It may function to carry or scavenge oxygen and be related to the ‘nemoglobins’ found in other nematode clades. P44 is of 44,460 Da and was found to associate with fatty acids by thin layer chromatography. Using environment-sensitive fluorescent lipid probes, P44 proved to be a hydrophobic ligand-binding protein with a binding site that is highly apolar, and competitive displacement experiments showed that P44 binds fatty acids. It may therefore have a role in distributing lipids within the parasites and, if also secreted, might influence local inflammatory and tissue responses. N-terminal and internal peptide amino-acid sequences of P44 indicate a relationship with a cysteine- and histidinerich protein of unknown function from Trichinella spiralis. Conclusions: The dominant proteins of D. renale PCF are, like those of large ascaridids, likely to be involved in lipid and oxygen handling, although there is evidence of strong divergence between the two groups.
Facultad de Ciencias Veterinarias
description Background: The giant kidney worm, Dioctophyme renale, is a debilitating and potentially lethal parasite that inhabits and destroys, typically host’s right kidney, and may also be found in ectopic sites. It is circumglobally distributed, mainly in dogs, and is increasingly regarded as a threat to other domestic animals and humans. There is little information on the parasite’s true incidence, or immune responses to it, and none on its biochemistry and molecular biology. Results: We characterised the soluble proteins of body wall, intestine, gonads and pseudocelomic fluid (PCF) of adult parasites. Two proteins, P17 and P44, dominate the PCF of both male and females. P17 is of 16,622 Da by mass spectrometry, and accounts for the intense red colour of the adult parasites. It may function to carry or scavenge oxygen and be related to the ‘nemoglobins’ found in other nematode clades. P44 is of 44,460 Da and was found to associate with fatty acids by thin layer chromatography. Using environment-sensitive fluorescent lipid probes, P44 proved to be a hydrophobic ligand-binding protein with a binding site that is highly apolar, and competitive displacement experiments showed that P44 binds fatty acids. It may therefore have a role in distributing lipids within the parasites and, if also secreted, might influence local inflammatory and tissue responses. N-terminal and internal peptide amino-acid sequences of P44 indicate a relationship with a cysteine- and histidinerich protein of unknown function from Trichinella spiralis. Conclusions: The dominant proteins of D. renale PCF are, like those of large ascaridids, likely to be involved in lipid and oxygen handling, although there is evidence of strong divergence between the two groups.
publishDate 2017
dc.date.none.fl_str_mv 2017
dc.type.none.fl_str_mv info:eu-repo/semantics/article
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info:eu-repo/semantics/altIdentifier/issn/1756-3305
info:eu-repo/semantics/altIdentifier/doi/10.1186/s13071-017-2388-x
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
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