A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology

Autores
Ituarte, Santiago; Brola, Tabata Romina; Fernández, Patricia Elena; Mu, Huawei; Qiu, Jian Wen; Heras, Horacio; Dreon, Marcos Sebastián
Año de publicación
2018
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The eggs of the freshwater Pomacea apple snails develop above the water level, exposed to varied physical and biological stressors. Their high hatching success seems to be linked to their proteins or perivitellins, which surround the developing embryo providing nutrients, sunscreens and varied defenses. The defensive mechanism has been unveiled in P. canaliculata and P. maculata eggs, where their major perivitellins are pigmented, non-digestible and provide a warning coloration while another perivitellin acts as a toxin. In P. scalaris, a species sympatric to the former, the defense strategy seems different, since no toxin was found and the major perivitellin, PsSC, while also colored and non-digestible, is a carbohydrate-binding protein. In this study we examine the structure and function of PsSC by sequencing its subunits, characterizing its carbohydrate binding profile and evaluating its effect on gut cells. Whereas cDNA sequencing and database search showed no lectin domain, glycan array carbohydrate binding profile revealed a strong specificity for glycosphingolipids and ABO group antigens. Moreover, PsSC agglutinated bacteria in a dose-dependent manner. Inspired on the defensive properties of seed lectins we evaluated the effects of PsSC on intestinal cells both in vitro (Caco-2 and IEC-6 cells) and in the gastrointestinal tract of rats. PsSC binds to Caco-2 cell membranes without reducing its viability, while a PsSC-containing diet temporarily induces large epithelium alterations and an increased absorptive surface. Based on these results, we propose that PsSC is involved in embryo defenses by altering the gut morphophysiology of potential predators, a convergent role to plant defensive lectins.
Instituto de Investigaciones Bioquímicas de La Plata
Facultad de Ciencias Veterinarias
Facultad de Ciencias Naturales y Museo
Facultad de Ciencias Médicas
Materia
Ciencias Veterinarias
Ciencias Médicas
Biología
lectins
eggs
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/104458
Acceder
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network_name_str SEDICI (UNLP)
spelling A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiologyItuarte, SantiagoBrola, Tabata RominaFernández, Patricia ElenaMu, HuaweiQiu, Jian WenHeras, HoracioDreon, Marcos SebastiánCiencias VeterinariasCiencias MédicasBiologíalectinseggsThe eggs of the freshwater <i>Pomacea</i> apple snails develop above the water level, exposed to varied physical and biological stressors. Their high hatching success seems to be linked to their proteins or perivitellins, which surround the developing embryo providing nutrients, sunscreens and varied defenses. The defensive mechanism has been unveiled in <i>P. canaliculata</i> and <i>P. maculata</i> eggs, where their major perivitellins are pigmented, non-digestible and provide a warning coloration while another perivitellin acts as a toxin. In <i>P. scalaris</i>, a species sympatric to the former, the defense strategy seems different, since no toxin was found and the major perivitellin, PsSC, while also colored and non-digestible, is a carbohydrate-binding protein. In this study we examine the structure and function of PsSC by sequencing its subunits, characterizing its carbohydrate binding profile and evaluating its effect on gut cells. Whereas cDNA sequencing and database search showed no lectin domain, glycan array carbohydrate binding profile revealed a strong specificity for glycosphingolipids and ABO group antigens. Moreover, PsSC agglutinated bacteria in a dose-dependent manner. Inspired on the defensive properties of seed lectins we evaluated the effects of PsSC on intestinal cells both <i>in vitro</i> (Caco-2 and IEC-6 cells) and in the gastrointestinal tract of rats. PsSC binds to Caco-2 cell membranes without reducing its viability, while a PsSC-containing diet temporarily induces large epithelium alterations and an increased absorptive surface. Based on these results, we propose that PsSC is involved in embryo defenses by altering the gut morphophysiology of potential predators, a convergent role to plant defensive lectins.Instituto de Investigaciones Bioquímicas de La PlataFacultad de Ciencias VeterinariasFacultad de Ciencias Naturales y MuseoFacultad de Ciencias Médicas2018info: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/10915/104458enginfo:eu-repo/semantics/altIdentifier/url/http://hdl.handle.net/11336/97864info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0198361info:eu-repo/semantics/altIdentifier/issn/1932-6203info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0198361info:eu-repo/semantics/altIdentifier/hdl/11336/97864info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/Creative Commons Attribution 4.0 International (CC BY 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-10-22T17:03:40Zoai:sedici.unlp.edu.ar:10915/104458Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-10-22 17:03:40.988SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology
title A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology
spellingShingle A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology
Ituarte, Santiago
Ciencias Veterinarias
Ciencias Médicas
Biología
lectins
eggs
title_short A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology
title_full A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology
title_fullStr A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology
title_full_unstemmed A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology
title_sort A lectin of a non-invasive apple snail as an egg defense against predation alters the rat gut morphophysiology
dc.creator.none.fl_str_mv Ituarte, Santiago
Brola, Tabata Romina
Fernández, Patricia Elena
Mu, Huawei
Qiu, Jian Wen
Heras, Horacio
Dreon, Marcos Sebastián
author Ituarte, Santiago
author_facet Ituarte, Santiago
Brola, Tabata Romina
Fernández, Patricia Elena
Mu, Huawei
Qiu, Jian Wen
Heras, Horacio
Dreon, Marcos Sebastián
author_role author
author2 Brola, Tabata Romina
Fernández, Patricia Elena
Mu, Huawei
Qiu, Jian Wen
Heras, Horacio
Dreon, Marcos Sebastián
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Ciencias Veterinarias
Ciencias Médicas
Biología
lectins
eggs
topic Ciencias Veterinarias
Ciencias Médicas
Biología
lectins
eggs
dc.description.none.fl_txt_mv The eggs of the freshwater <i>Pomacea</i> apple snails develop above the water level, exposed to varied physical and biological stressors. Their high hatching success seems to be linked to their proteins or perivitellins, which surround the developing embryo providing nutrients, sunscreens and varied defenses. The defensive mechanism has been unveiled in <i>P. canaliculata</i> and <i>P. maculata</i> eggs, where their major perivitellins are pigmented, non-digestible and provide a warning coloration while another perivitellin acts as a toxin. In <i>P. scalaris</i>, a species sympatric to the former, the defense strategy seems different, since no toxin was found and the major perivitellin, PsSC, while also colored and non-digestible, is a carbohydrate-binding protein. In this study we examine the structure and function of PsSC by sequencing its subunits, characterizing its carbohydrate binding profile and evaluating its effect on gut cells. Whereas cDNA sequencing and database search showed no lectin domain, glycan array carbohydrate binding profile revealed a strong specificity for glycosphingolipids and ABO group antigens. Moreover, PsSC agglutinated bacteria in a dose-dependent manner. Inspired on the defensive properties of seed lectins we evaluated the effects of PsSC on intestinal cells both <i>in vitro</i> (Caco-2 and IEC-6 cells) and in the gastrointestinal tract of rats. PsSC binds to Caco-2 cell membranes without reducing its viability, while a PsSC-containing diet temporarily induces large epithelium alterations and an increased absorptive surface. Based on these results, we propose that PsSC is involved in embryo defenses by altering the gut morphophysiology of potential predators, a convergent role to plant defensive lectins.
Instituto de Investigaciones Bioquímicas de La Plata
Facultad de Ciencias Veterinarias
Facultad de Ciencias Naturales y Museo
Facultad de Ciencias Médicas
description The eggs of the freshwater <i>Pomacea</i> apple snails develop above the water level, exposed to varied physical and biological stressors. Their high hatching success seems to be linked to their proteins or perivitellins, which surround the developing embryo providing nutrients, sunscreens and varied defenses. The defensive mechanism has been unveiled in <i>P. canaliculata</i> and <i>P. maculata</i> eggs, where their major perivitellins are pigmented, non-digestible and provide a warning coloration while another perivitellin acts as a toxin. In <i>P. scalaris</i>, a species sympatric to the former, the defense strategy seems different, since no toxin was found and the major perivitellin, PsSC, while also colored and non-digestible, is a carbohydrate-binding protein. In this study we examine the structure and function of PsSC by sequencing its subunits, characterizing its carbohydrate binding profile and evaluating its effect on gut cells. Whereas cDNA sequencing and database search showed no lectin domain, glycan array carbohydrate binding profile revealed a strong specificity for glycosphingolipids and ABO group antigens. Moreover, PsSC agglutinated bacteria in a dose-dependent manner. Inspired on the defensive properties of seed lectins we evaluated the effects of PsSC on intestinal cells both <i>in vitro</i> (Caco-2 and IEC-6 cells) and in the gastrointestinal tract of rats. PsSC binds to Caco-2 cell membranes without reducing its viability, while a PsSC-containing diet temporarily induces large epithelium alterations and an increased absorptive surface. Based on these results, we propose that PsSC is involved in embryo defenses by altering the gut morphophysiology of potential predators, a convergent role to plant defensive lectins.
publishDate 2018
dc.date.none.fl_str_mv 2018
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/10915/104458
url http://sedici.unlp.edu.ar/handle/10915/104458
dc.language.none.fl_str_mv eng
language eng
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info:eu-repo/semantics/altIdentifier/url/https://journals.plos.org/plosone/article?id=10.1371/journal.pone.0198361
info:eu-repo/semantics/altIdentifier/issn/1932-6203
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0198361
info:eu-repo/semantics/altIdentifier/hdl/11336/97864
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
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Creative Commons Attribution 4.0 International (CC BY 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/4.0/
Creative Commons Attribution 4.0 International (CC BY 4.0)
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
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reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
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