Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)

Autores
Ituarte, Santiago; Dreon, Marcos Sebastián; Ceolín, Marcelo Raúl; Heras, Horacio
Año de publicación
2012
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Apple snail perivitellins are emerging as ecologically important reproductive proteins. To elucidate if the protective functions of the egg proteins of Pomacea canaliculata (Caenogastropoda, Ampullariidae), involved in embryo defenses, are present in other Pomacea species we studied scalarin (PsSC), the major perivitellin of Pomacea scalaris. Using small angle X-ray scattering, fluorescence and absorption spectroscopy and biochemical methods, we analyzed PsSC structural stability, agglutinating activity, sugar specificity and protease resistance. PsSC aggluttinated rabbit, and, to a lesser extent, human B and A erythrocytes independently of divalent metals Ca2+ and Mg2+ were strongly inhibited by galactosamine and glucosamine. The protein was structurally stable between pH 2.0 to 10.0, though agglutination occurred only between pH 4.0 to 8.0 (maximum activity at pH 7.0). The agglutinating activity was conserved up to 60°C and completely lost above 80°C, in agreement with the structural thermal stability of the protein (up to 60°C). PsSC was able to withstand in vitro gastrointestinal digestion, and showed no trypsin inhibition activity. The presence of lectin activity has been reported in eggs of other Pomacea snails, but here we link for the first time, this activity to an apple snail multifunctional perivitellin. This novel role for a snail egg storage protein is different from closely related P.canaliculata defensive proteins.
Facultad de Ciencias Exactas
Materia
Ciencias Exactas
Química
calcium
egg protein
galactosamine
glucosamine
lectin
magnesium
proteinase
scalarin protein
vitellin
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/3.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/30080

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oai_identifier_str oai:sedici.unlp.edu.ar:10915/30080
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repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)Ituarte, SantiagoDreon, Marcos SebastiánCeolín, Marcelo RaúlHeras, HoracioCiencias ExactasQuímicacalciumegg proteingalactosamineglucosaminelectinmagnesiumproteinasescalarin proteinvitellinApple snail perivitellins are emerging as ecologically important reproductive proteins. To elucidate if the protective functions of the egg proteins of Pomacea canaliculata (Caenogastropoda, Ampullariidae), involved in embryo defenses, are present in other Pomacea species we studied scalarin (PsSC), the major perivitellin of Pomacea scalaris. Using small angle X-ray scattering, fluorescence and absorption spectroscopy and biochemical methods, we analyzed PsSC structural stability, agglutinating activity, sugar specificity and protease resistance. PsSC aggluttinated rabbit, and, to a lesser extent, human B and A erythrocytes independently of divalent metals Ca2+ and Mg2+ were strongly inhibited by galactosamine and glucosamine. The protein was structurally stable between pH 2.0 to 10.0, though agglutination occurred only between pH 4.0 to 8.0 (maximum activity at pH 7.0). The agglutinating activity was conserved up to 60°C and completely lost above 80°C, in agreement with the structural thermal stability of the protein (up to 60°C). PsSC was able to withstand in vitro gastrointestinal digestion, and showed no trypsin inhibition activity. The presence of lectin activity has been reported in eggs of other Pomacea snails, but here we link for the first time, this activity to an apple snail multifunctional perivitellin. This novel role for a snail egg storage protein is different from closely related P.canaliculata defensive proteins.Facultad de Ciencias Exactas2012info: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/10915/30080enginfo:eu-repo/semantics/altIdentifier/url/http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0050115info:eu-repo/semantics/altIdentifier/issn/1932-6203info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0050115info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/3.0/Creative Commons Attribution 3.0 Unported (CC BY 3.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T10:57:12Zoai:sedici.unlp.edu.ar:10915/30080Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 10:57:13.104SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
title Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
spellingShingle Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
Ituarte, Santiago
Ciencias Exactas
Química
calcium
egg protein
galactosamine
glucosamine
lectin
magnesium
proteinase
scalarin protein
vitellin
title_short Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
title_full Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
title_fullStr Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
title_full_unstemmed Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
title_sort Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
dc.creator.none.fl_str_mv Ituarte, Santiago
Dreon, Marcos Sebastián
Ceolín, Marcelo Raúl
Heras, Horacio
author Ituarte, Santiago
author_facet Ituarte, Santiago
Dreon, Marcos Sebastián
Ceolín, Marcelo Raúl
Heras, Horacio
author_role author
author2 Dreon, Marcos Sebastián
Ceolín, Marcelo Raúl
Heras, Horacio
author2_role author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Química
calcium
egg protein
galactosamine
glucosamine
lectin
magnesium
proteinase
scalarin protein
vitellin
topic Ciencias Exactas
Química
calcium
egg protein
galactosamine
glucosamine
lectin
magnesium
proteinase
scalarin protein
vitellin
dc.description.none.fl_txt_mv Apple snail perivitellins are emerging as ecologically important reproductive proteins. To elucidate if the protective functions of the egg proteins of Pomacea canaliculata (Caenogastropoda, Ampullariidae), involved in embryo defenses, are present in other Pomacea species we studied scalarin (PsSC), the major perivitellin of Pomacea scalaris. Using small angle X-ray scattering, fluorescence and absorption spectroscopy and biochemical methods, we analyzed PsSC structural stability, agglutinating activity, sugar specificity and protease resistance. PsSC aggluttinated rabbit, and, to a lesser extent, human B and A erythrocytes independently of divalent metals Ca2+ and Mg2+ were strongly inhibited by galactosamine and glucosamine. The protein was structurally stable between pH 2.0 to 10.0, though agglutination occurred only between pH 4.0 to 8.0 (maximum activity at pH 7.0). The agglutinating activity was conserved up to 60°C and completely lost above 80°C, in agreement with the structural thermal stability of the protein (up to 60°C). PsSC was able to withstand in vitro gastrointestinal digestion, and showed no trypsin inhibition activity. The presence of lectin activity has been reported in eggs of other Pomacea snails, but here we link for the first time, this activity to an apple snail multifunctional perivitellin. This novel role for a snail egg storage protein is different from closely related P.canaliculata defensive proteins.
Facultad de Ciencias Exactas
description Apple snail perivitellins are emerging as ecologically important reproductive proteins. To elucidate if the protective functions of the egg proteins of Pomacea canaliculata (Caenogastropoda, Ampullariidae), involved in embryo defenses, are present in other Pomacea species we studied scalarin (PsSC), the major perivitellin of Pomacea scalaris. Using small angle X-ray scattering, fluorescence and absorption spectroscopy and biochemical methods, we analyzed PsSC structural stability, agglutinating activity, sugar specificity and protease resistance. PsSC aggluttinated rabbit, and, to a lesser extent, human B and A erythrocytes independently of divalent metals Ca2+ and Mg2+ were strongly inhibited by galactosamine and glucosamine. The protein was structurally stable between pH 2.0 to 10.0, though agglutination occurred only between pH 4.0 to 8.0 (maximum activity at pH 7.0). The agglutinating activity was conserved up to 60°C and completely lost above 80°C, in agreement with the structural thermal stability of the protein (up to 60°C). PsSC was able to withstand in vitro gastrointestinal digestion, and showed no trypsin inhibition activity. The presence of lectin activity has been reported in eggs of other Pomacea snails, but here we link for the first time, this activity to an apple snail multifunctional perivitellin. This novel role for a snail egg storage protein is different from closely related P.canaliculata defensive proteins.
publishDate 2012
dc.date.none.fl_str_mv 2012
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/30080
url http://sedici.unlp.edu.ar/handle/10915/30080
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0050115
info:eu-repo/semantics/altIdentifier/issn/1932-6203
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0050115
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/3.0/
Creative Commons Attribution 3.0 Unported (CC BY 3.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/3.0/
Creative Commons Attribution 3.0 Unported (CC BY 3.0)
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repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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