The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris

Autores
Pasquevich, María Yanina; Dreon, Marcos Sebastian; Heras, Horacio
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Snails from the genus Pomacea lay conspicuous masses of brightly colored eggs above the water. Coloration is given by carotenoproteins that also which play important roles in protection against sun radiation, stabilizing and transporting antioxidant molecules and helping to protect embryos from desiccation and predators. They seem a key acquisition, but have been little studied. Here we report the characteristics of the major carotenoprotein from Pomacea maculata and the first comparison among these egg proteins. This particle, hereafter PmPV1, represents ~. 52% of perivitellin fluid protein. It is a glyco-lipo-carotenoprotein responsible for the bright reddish egg coloration. With VHDL characteristics, PmPV1 apparent molecular mass is 294. kDa, composed of five non-covalently bound subunits of pI 4.7-9.8 and masses between 26 and 36. kDa whose N-terminal sequences were obtained. It is a glyco-lipo-carotenoprotein scarcely lipidated (<. 1%) but highly glycosilated (13% by wt). Lipids include phospholipids, free fatty acids and carotenoids; mannose and galactose predominate over other monosaccharides. Main carotenoids are esterified and non-esterified astaxanthin (71 and 25%, respectively). Carotenoid removal does not seem to affect the structural characteristics of the oligomer, while deglycosilation reduces subunit number from five to a single one. The carotenoid-protein association protected the former against oxidation. PmPV1 cross reacts with polyclonal antibodies against the PcOvo, the major carotenoprotein from Pomacea canaliculata. The characterization of PmPV1 allows the first comparisons among snail carotenoproteins and further highlights the importance of these perivitellins in the reproductive strategy of Pomacea.
Fil: Pasquevich, María Yanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Dreon, Marcos Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Heras, Horacio. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Materia
ANTIOXIDANT
CAROTENOID
CAROTENOPROTEIN
EGG
PERIVITELLIN
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/100510
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/100510
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalarisPasquevich, María YaninaDreon, Marcos SebastianHeras, HoracioANTIOXIDANTCAROTENOIDCAROTENOPROTEINEGGPERIVITELLINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Snails from the genus Pomacea lay conspicuous masses of brightly colored eggs above the water. Coloration is given by carotenoproteins that also which play important roles in protection against sun radiation, stabilizing and transporting antioxidant molecules and helping to protect embryos from desiccation and predators. They seem a key acquisition, but have been little studied. Here we report the characteristics of the major carotenoprotein from Pomacea maculata and the first comparison among these egg proteins. This particle, hereafter PmPV1, represents ~. 52% of perivitellin fluid protein. It is a glyco-lipo-carotenoprotein responsible for the bright reddish egg coloration. With VHDL characteristics, PmPV1 apparent molecular mass is 294. kDa, composed of five non-covalently bound subunits of pI 4.7-9.8 and masses between 26 and 36. kDa whose N-terminal sequences were obtained. It is a glyco-lipo-carotenoprotein scarcely lipidated (<. 1%) but highly glycosilated (13% by wt). Lipids include phospholipids, free fatty acids and carotenoids; mannose and galactose predominate over other monosaccharides. Main carotenoids are esterified and non-esterified astaxanthin (71 and 25%, respectively). Carotenoid removal does not seem to affect the structural characteristics of the oligomer, while deglycosilation reduces subunit number from five to a single one. The carotenoid-protein association protected the former against oxidation. PmPV1 cross reacts with polyclonal antibodies against the PcOvo, the major carotenoprotein from Pomacea canaliculata. The characterization of PmPV1 allows the first comparisons among snail carotenoproteins and further highlights the importance of these perivitellins in the reproductive strategy of Pomacea.Fil: Pasquevich, María Yanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Dreon, Marcos Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaFil: Heras, Horacio. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; ArgentinaElsevier Science Inc2014-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/100510Pasquevich, María Yanina; Dreon, Marcos Sebastian; Heras, Horacio; The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris; Elsevier Science Inc; Comparative Biochemistry And Physiology. Part B, Biochemistry & Molecular Biology.; 169; 1; 1-2014; 63-711096-4959CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1096495913001966info:eu-repo/semantics/altIdentifier/doi/10.1016/j.cbpb.2013.11.008info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T15:44:23Zoai:ri.conicet.gov.ar:11336/100510instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-15 15:44:23.446CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris
title The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris
spellingShingle The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris
Pasquevich, María Yanina
ANTIOXIDANT
CAROTENOID
CAROTENOPROTEIN
EGG
PERIVITELLIN
title_short The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris
title_full The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris
title_fullStr The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris
title_full_unstemmed The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris
title_sort The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris
dc.creator.none.fl_str_mv Pasquevich, María Yanina
Dreon, Marcos Sebastian
Heras, Horacio
author Pasquevich, María Yanina
author_facet Pasquevich, María Yanina
Dreon, Marcos Sebastian
Heras, Horacio
author_role author
author2 Dreon, Marcos Sebastian
Heras, Horacio
author2_role author
author
dc.subject.none.fl_str_mv ANTIOXIDANT
CAROTENOID
CAROTENOPROTEIN
EGG
PERIVITELLIN
topic ANTIOXIDANT
CAROTENOID
CAROTENOPROTEIN
EGG
PERIVITELLIN
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Snails from the genus Pomacea lay conspicuous masses of brightly colored eggs above the water. Coloration is given by carotenoproteins that also which play important roles in protection against sun radiation, stabilizing and transporting antioxidant molecules and helping to protect embryos from desiccation and predators. They seem a key acquisition, but have been little studied. Here we report the characteristics of the major carotenoprotein from Pomacea maculata and the first comparison among these egg proteins. This particle, hereafter PmPV1, represents ~. 52% of perivitellin fluid protein. It is a glyco-lipo-carotenoprotein responsible for the bright reddish egg coloration. With VHDL characteristics, PmPV1 apparent molecular mass is 294. kDa, composed of five non-covalently bound subunits of pI 4.7-9.8 and masses between 26 and 36. kDa whose N-terminal sequences were obtained. It is a glyco-lipo-carotenoprotein scarcely lipidated (<. 1%) but highly glycosilated (13% by wt). Lipids include phospholipids, free fatty acids and carotenoids; mannose and galactose predominate over other monosaccharides. Main carotenoids are esterified and non-esterified astaxanthin (71 and 25%, respectively). Carotenoid removal does not seem to affect the structural characteristics of the oligomer, while deglycosilation reduces subunit number from five to a single one. The carotenoid-protein association protected the former against oxidation. PmPV1 cross reacts with polyclonal antibodies against the PcOvo, the major carotenoprotein from Pomacea canaliculata. The characterization of PmPV1 allows the first comparisons among snail carotenoproteins and further highlights the importance of these perivitellins in the reproductive strategy of Pomacea.
Fil: Pasquevich, María Yanina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Dreon, Marcos Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
Fil: Heras, Horacio. Universidad Nacional de La Plata. Facultad de Ciencias Naturales y Museo; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner". Universidad Nacional de la Plata. Facultad de Ciencias Médicas. Instituto de Investigaciones Bioquímicas de La Plata "Prof. Dr. Rodolfo R. Brenner"; Argentina
description Snails from the genus Pomacea lay conspicuous masses of brightly colored eggs above the water. Coloration is given by carotenoproteins that also which play important roles in protection against sun radiation, stabilizing and transporting antioxidant molecules and helping to protect embryos from desiccation and predators. They seem a key acquisition, but have been little studied. Here we report the characteristics of the major carotenoprotein from Pomacea maculata and the first comparison among these egg proteins. This particle, hereafter PmPV1, represents ~. 52% of perivitellin fluid protein. It is a glyco-lipo-carotenoprotein responsible for the bright reddish egg coloration. With VHDL characteristics, PmPV1 apparent molecular mass is 294. kDa, composed of five non-covalently bound subunits of pI 4.7-9.8 and masses between 26 and 36. kDa whose N-terminal sequences were obtained. It is a glyco-lipo-carotenoprotein scarcely lipidated (<. 1%) but highly glycosilated (13% by wt). Lipids include phospholipids, free fatty acids and carotenoids; mannose and galactose predominate over other monosaccharides. Main carotenoids are esterified and non-esterified astaxanthin (71 and 25%, respectively). Carotenoid removal does not seem to affect the structural characteristics of the oligomer, while deglycosilation reduces subunit number from five to a single one. The carotenoid-protein association protected the former against oxidation. PmPV1 cross reacts with polyclonal antibodies against the PcOvo, the major carotenoprotein from Pomacea canaliculata. The characterization of PmPV1 allows the first comparisons among snail carotenoproteins and further highlights the importance of these perivitellins in the reproductive strategy of Pomacea.
publishDate 2014
dc.date.none.fl_str_mv 2014-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/100510
Pasquevich, María Yanina; Dreon, Marcos Sebastian; Heras, Horacio; The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris; Elsevier Science Inc; Comparative Biochemistry And Physiology. Part B, Biochemistry & Molecular Biology.; 169; 1; 1-2014; 63-71
1096-4959
CONICET Digital
CONICET
url http://hdl.handle.net/11336/100510
identifier_str_mv Pasquevich, María Yanina; Dreon, Marcos Sebastian; Heras, Horacio; The major egg reserve protein from the invasive apple snail Pomacea maculata is a complex carotenoprotein related to those of Pomacea canaliculata and Pomacea scalaris; Elsevier Science Inc; Comparative Biochemistry And Physiology. Part B, Biochemistry & Molecular Biology.; 169; 1; 1-2014; 63-71
1096-4959
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1096495913001966
info:eu-repo/semantics/altIdentifier/doi/10.1016/j.cbpb.2013.11.008
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science Inc
publisher.none.fl_str_mv Elsevier Science Inc
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.22299

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