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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/104458
Ver los metadatos del registro completo
id |
SEDICI_64bdfeffa5297731d7ebd1b793d957a3 |
---|---|
oai_identifier_str |
oai:sedici.unlp.edu.ar:10915/104458 |
network_acronym_str |
SEDICI |
repository_id_str |
1329 |
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:UNLP2025-09-29T11:22:47Zoai: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:13292025-09-29 11:22:48.264SEDICI (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 |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://hdl.handle.net/11336/97864 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 http://creativecommons.org/licenses/by/4.0/ 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 instacron:UNLP |
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 |
repository.mail.fl_str_mv |
alira@sedici.unlp.edu.ar |
_version_ |
1844616103984103424 |
score |
13.070432 |