A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggs
- Autores
- Brola, Tabata Romina; Dreon, Marcos Sebastián; Qiu, Jian-Wen; Heras, Horacio
- Año de publicación
- 2020
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The acquisition of egg protection is vital for species survival. Poisonous eggs from Pomacea apple snails have defensive macromolecules for protection. Here we isolated and characterized a novel lectin called PdPV1 that is massively accumulated in the eggs of Pomacea diffusa and seems part of its protective cocktail. The native protein, an oligomer of ca. 256 kDa, has high structural stability, withstanding 15 min boiling and denaturing by sodium dodecyl sulphate. It resists in vitro proteinase digestion and displays structural stability between pH 2.0-12.0 and up to 85 °C. These properties, as well as its subunit sequences, glycosylation pattern, presence of carotenoids, size, and global shape resemble those of its orthologs from other Pomacea. Further, like members of the canaliculata clade, PdPV1 is recovered unchanged in faeces of mice ingesting it, supporting an antinutritive defensive function. PdPV1 also displays a strong hemagglutinating activity specifically recognizing selected ganglioside motifs with high affinity. This activity is only shared with PsSC, a perivitelline from the same clade (bridgesii clade). As a whole, these results indicate that species in the genus Pomacea have diversified their eggs defences: Those from the bridgesii clade are protected mostly by non-digestible lectins that lower the nutritional value of eggs, in contrast with protection by neurotoxins of other Pomacea clades, indicating apple snail egg defensive strategies are clade-specific. The harsh gastrointestinal environment of predators would have favoured their appearance, extending by convergent evolution the presence of plant-like highly stable lectins, a strategy not reported in other animals.
Instituto de Investigaciones Bioquímicas de La Plata
Facultad de Ciencias Naturales y Museo - Materia
-
Biología
Ampullariidae
Egg defense
Gastropods
Glycan array
Lectin activity
Protein structure - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- http://creativecommons.org/licenses/by-nc-sa/4.0/
- Repositorio
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/126164
Ver los metadatos del registro completo
id |
SEDICI_b0b521f8cc2e30d42ff6a8a605bee83f |
---|---|
oai_identifier_str |
oai:sedici.unlp.edu.ar:10915/126164 |
network_acronym_str |
SEDICI |
repository_id_str |
1329 |
network_name_str |
SEDICI (UNLP) |
spelling |
A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggsBrola, Tabata RominaDreon, Marcos SebastiánQiu, Jian-WenHeras, HoracioBiologíaAmpullariidaeEgg defenseGastropodsGlycan arrayLectin activityProtein structureThe acquisition of egg protection is vital for species survival. Poisonous eggs from Pomacea apple snails have defensive macromolecules for protection. Here we isolated and characterized a novel lectin called PdPV1 that is massively accumulated in the eggs of Pomacea diffusa and seems part of its protective cocktail. The native protein, an oligomer of ca. 256 kDa, has high structural stability, withstanding 15 min boiling and denaturing by sodium dodecyl sulphate. It resists in vitro proteinase digestion and displays structural stability between pH 2.0-12.0 and up to 85 °C. These properties, as well as its subunit sequences, glycosylation pattern, presence of carotenoids, size, and global shape resemble those of its orthologs from other Pomacea. Further, like members of the canaliculata clade, PdPV1 is recovered unchanged in faeces of mice ingesting it, supporting an antinutritive defensive function. PdPV1 also displays a strong hemagglutinating activity specifically recognizing selected ganglioside motifs with high affinity. This activity is only shared with PsSC, a perivitelline from the same clade (bridgesii clade). As a whole, these results indicate that species in the genus Pomacea have diversified their eggs defences: Those from the bridgesii clade are protected mostly by non-digestible lectins that lower the nutritional value of eggs, in contrast with protection by neurotoxins of other Pomacea clades, indicating apple snail egg defensive strategies are clade-specific. The harsh gastrointestinal environment of predators would have favoured their appearance, extending by convergent evolution the presence of plant-like highly stable lectins, a strategy not reported in other animals.Instituto de Investigaciones Bioquímicas de La PlataFacultad de Ciencias Naturales y Museo2020-10-08info: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/10915/126164enginfo:eu-repo/semantics/altIdentifier/issn/1477-9145info:eu-repo/semantics/altIdentifier/issn/0022-0949info:eu-repo/semantics/altIdentifier/pmid/32719049info:eu-repo/semantics/altIdentifier/doi/10.1242/jeb.231878info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:30:17Zoai:sedici.unlp.edu.ar:10915/126164Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:30:18.155SEDICI (UNLP) - Universidad Nacional de La Platafalse |
dc.title.none.fl_str_mv |
A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggs |
title |
A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggs |
spellingShingle |
A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggs Brola, Tabata Romina Biología Ampullariidae Egg defense Gastropods Glycan array Lectin activity Protein structure |
title_short |
A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggs |
title_full |
A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggs |
title_fullStr |
A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggs |
title_full_unstemmed |
A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggs |
title_sort |
A highly stable, nondigestible lectin from Pomacea diffusa unveils clade-related protection systems in apple snail eggs |
dc.creator.none.fl_str_mv |
Brola, Tabata Romina Dreon, Marcos Sebastián Qiu, Jian-Wen Heras, Horacio |
author |
Brola, Tabata Romina |
author_facet |
Brola, Tabata Romina Dreon, Marcos Sebastián Qiu, Jian-Wen Heras, Horacio |
author_role |
author |
author2 |
Dreon, Marcos Sebastián Qiu, Jian-Wen Heras, Horacio |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
Biología Ampullariidae Egg defense Gastropods Glycan array Lectin activity Protein structure |
topic |
Biología Ampullariidae Egg defense Gastropods Glycan array Lectin activity Protein structure |
dc.description.none.fl_txt_mv |
The acquisition of egg protection is vital for species survival. Poisonous eggs from Pomacea apple snails have defensive macromolecules for protection. Here we isolated and characterized a novel lectin called PdPV1 that is massively accumulated in the eggs of Pomacea diffusa and seems part of its protective cocktail. The native protein, an oligomer of ca. 256 kDa, has high structural stability, withstanding 15 min boiling and denaturing by sodium dodecyl sulphate. It resists in vitro proteinase digestion and displays structural stability between pH 2.0-12.0 and up to 85 °C. These properties, as well as its subunit sequences, glycosylation pattern, presence of carotenoids, size, and global shape resemble those of its orthologs from other Pomacea. Further, like members of the canaliculata clade, PdPV1 is recovered unchanged in faeces of mice ingesting it, supporting an antinutritive defensive function. PdPV1 also displays a strong hemagglutinating activity specifically recognizing selected ganglioside motifs with high affinity. This activity is only shared with PsSC, a perivitelline from the same clade (bridgesii clade). As a whole, these results indicate that species in the genus Pomacea have diversified their eggs defences: Those from the bridgesii clade are protected mostly by non-digestible lectins that lower the nutritional value of eggs, in contrast with protection by neurotoxins of other Pomacea clades, indicating apple snail egg defensive strategies are clade-specific. The harsh gastrointestinal environment of predators would have favoured their appearance, extending by convergent evolution the presence of plant-like highly stable lectins, a strategy not reported in other animals. Instituto de Investigaciones Bioquímicas de La Plata Facultad de Ciencias Naturales y Museo |
description |
The acquisition of egg protection is vital for species survival. Poisonous eggs from Pomacea apple snails have defensive macromolecules for protection. Here we isolated and characterized a novel lectin called PdPV1 that is massively accumulated in the eggs of Pomacea diffusa and seems part of its protective cocktail. The native protein, an oligomer of ca. 256 kDa, has high structural stability, withstanding 15 min boiling and denaturing by sodium dodecyl sulphate. It resists in vitro proteinase digestion and displays structural stability between pH 2.0-12.0 and up to 85 °C. These properties, as well as its subunit sequences, glycosylation pattern, presence of carotenoids, size, and global shape resemble those of its orthologs from other Pomacea. Further, like members of the canaliculata clade, PdPV1 is recovered unchanged in faeces of mice ingesting it, supporting an antinutritive defensive function. PdPV1 also displays a strong hemagglutinating activity specifically recognizing selected ganglioside motifs with high affinity. This activity is only shared with PsSC, a perivitelline from the same clade (bridgesii clade). As a whole, these results indicate that species in the genus Pomacea have diversified their eggs defences: Those from the bridgesii clade are protected mostly by non-digestible lectins that lower the nutritional value of eggs, in contrast with protection by neurotoxins of other Pomacea clades, indicating apple snail egg defensive strategies are clade-specific. The harsh gastrointestinal environment of predators would have favoured their appearance, extending by convergent evolution the presence of plant-like highly stable lectins, a strategy not reported in other animals. |
publishDate |
2020 |
dc.date.none.fl_str_mv |
2020-10-08 |
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/10915/126164 |
url |
http://sedici.unlp.edu.ar/handle/10915/126164 |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/issn/1477-9145 info:eu-repo/semantics/altIdentifier/issn/0022-0949 info:eu-repo/semantics/altIdentifier/pmid/32719049 info:eu-repo/semantics/altIdentifier/doi/10.1242/jeb.231878 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
http://creativecommons.org/licenses/by-nc-sa/4.0/ Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 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_ |
1844616182214164480 |
score |
13.070432 |