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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/30080
Ver los metadatos del registro completo
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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 |
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article |
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publishedVersion |
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http://sedici.unlp.edu.ar/handle/10915/30080 |
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http://sedici.unlp.edu.ar/handle/10915/30080 |
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eng |
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eng |
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http://creativecommons.org/licenses/by/3.0/ Creative Commons Attribution 3.0 Unported (CC BY 3.0) |
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