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

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),...

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Detalles Bibliográficos
Autores principales:	Ituarte, Santiago, Dreon, Marcos Sebastián, Ceolín, Marcelo Raúl, Heras, Horacio
Formato:	Articulo
Lenguaje:	Inglés
Publicado:	2012
Materias:	Ciencias Exactas Química calcium egg protein galactosamine glucosamine lectin magnesium proteinase scalarin protein vitellin
Acceso en línea:	http://sedici.unlp.edu.ar/handle/10915/30080 http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0050115
Aporte de:	SEDICI (UNLP) de Universidad Nacional de La Plata

id	I19-R120-10915-30080
record_format	dspace
institution	Universidad Nacional de La Plata
institution_str	I-19
repository_str	R-120
collection	SEDICI (UNLP)
language	Inglés
topic	Ciencias Exactas Química calcium egg protein galactosamine glucosamine lectin magnesium proteinase scalarin protein vitellin
spellingShingle	Ciencias Exactas Química calcium egg protein galactosamine glucosamine lectin magnesium proteinase scalarin protein vitellin Ituarte, Santiago Dreon, Marcos Sebastián Ceolín, Marcelo Raúl Heras, Horacio Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
topic_facet	Ciencias Exactas Química calcium egg protein galactosamine glucosamine lectin magnesium proteinase scalarin protein vitellin
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.
format	Articulo Articulo
author	Ituarte, Santiago Dreon, Marcos Sebastián Ceolín, Marcelo Raúl Heras, Horacio
author_facet	Ituarte, Santiago Dreon, Marcos Sebastián Ceolín, Marcelo Raúl Heras, Horacio
author_sort	Ituarte, Santiago
title	Agglutinating activity and structural characterization of Scalarin, the major egg protein of the snail <i>Pomacea scalaris</i> (d'Orbigny, 1832)
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)
publishDate	2012
url	http://sedici.unlp.edu.ar/handle/10915/30080 http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0050115
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bdutipo_str	Repositorios
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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)

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