Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin

Autores
Vázquez, Romina Florencia; Daza Millone, María Antonieta; Giglio, Matías Leonel; Brola, Tabata Romina; Maté, Sabina María; Heras, Horacio
Año de publicación
2025
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
The perivitellin-2 (PV2) from snails is an unusual neuro and enterotoxin comprising a pore-forming domain of the Membrane Attack Complex and Perforin Family (MACPF) linked to a lectin. While both domains have membrane binding capabilities, PV2’s mechanism of action remains unclear. We studied the apple snail Pomacea maculata PV2’s (PmPV2’s) interaction with lipid membranes using various biophysical and cell biology approaches. In vitro studies showed that PmPV2 toxicity decreased when cholesterol (Chol) was diminished from enterocyte cell membranes. Chol enhanced PmPV2 association with phosphatidylcholine membranes but did not induce pore formation. In contrast, using rat brain lipid models, rich in glycolipids, PmPV2 exhibited high affinity and induced vesicle permeabilization. Negative stain electron microscopy and atomic force microscopy confirmed the formation of pore-like structures in brain lipid vesicles. Our findings suggest that Chol is a necessary lipid component and point to PmPV2–glycolipid interactions as potential activators critical to triggering PmPV2’s pore-forming activity, providing insights into this novel toxin’s mechanism.
Facultad de Ciencias Naturales y Museo
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
Materia
Bioquímica
MACPF
snail pore-forming toxin
neurotoxin/enterotoxin
lectin
lipid membranes
protein–lipid interaction
cholesterol
brain lipids
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:10915/181867

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oai_identifier_str oai:sedici.unlp.edu.ar:10915/181867
network_acronym_str SEDICI
repository_id_str 1329
network_name_str SEDICI (UNLP)
spelling Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming ToxinVázquez, Romina FlorenciaDaza Millone, María AntonietaGiglio, Matías LeonelBrola, Tabata RominaMaté, Sabina MaríaHeras, HoracioBioquímicaMACPFsnail pore-forming toxinneurotoxin/enterotoxinlectinlipid membranesprotein–lipid interactioncholesterolbrain lipidsThe perivitellin-2 (PV2) from snails is an unusual neuro and enterotoxin comprising a pore-forming domain of the Membrane Attack Complex and Perforin Family (MACPF) linked to a lectin. While both domains have membrane binding capabilities, PV2’s mechanism of action remains unclear. We studied the apple snail Pomacea maculata PV2’s (PmPV2’s) interaction with lipid membranes using various biophysical and cell biology approaches. In vitro studies showed that PmPV2 toxicity decreased when cholesterol (Chol) was diminished from enterocyte cell membranes. Chol enhanced PmPV2 association with phosphatidylcholine membranes but did not induce pore formation. In contrast, using rat brain lipid models, rich in glycolipids, PmPV2 exhibited high affinity and induced vesicle permeabilization. Negative stain electron microscopy and atomic force microscopy confirmed the formation of pore-like structures in brain lipid vesicles. Our findings suggest that Chol is a necessary lipid component and point to PmPV2–glycolipid interactions as potential activators critical to triggering PmPV2’s pore-forming activity, providing insights into this novel toxin’s mechanism.Facultad de Ciencias Naturales y MuseoInstituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas2025-04info: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/10915/181867enginfo:eu-repo/semantics/altIdentifier/issn/2072-6651info:eu-repo/semantics/altIdentifier/doi/10.3390/toxins17040183info: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:UNLP2025-09-29T11:49:38Zoai:sedici.unlp.edu.ar:10915/181867Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:49:39.035SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin
title Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin
spellingShingle Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin
Vázquez, Romina Florencia
Bioquímica
MACPF
snail pore-forming toxin
neurotoxin/enterotoxin
lectin
lipid membranes
protein–lipid interaction
cholesterol
brain lipids
title_short Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin
title_full Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin
title_fullStr Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin
title_full_unstemmed Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin
title_sort Insights into the Protein–Lipid Interaction of Perivitellin-2, an Unusual Snail Pore-Forming Toxin
dc.creator.none.fl_str_mv Vázquez, Romina Florencia
Daza Millone, María Antonieta
Giglio, Matías Leonel
Brola, Tabata Romina
Maté, Sabina María
Heras, Horacio
author Vázquez, Romina Florencia
author_facet Vázquez, Romina Florencia
Daza Millone, María Antonieta
Giglio, Matías Leonel
Brola, Tabata Romina
Maté, Sabina María
Heras, Horacio
author_role author
author2 Daza Millone, María Antonieta
Giglio, Matías Leonel
Brola, Tabata Romina
Maté, Sabina María
Heras, Horacio
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Bioquímica
MACPF
snail pore-forming toxin
neurotoxin/enterotoxin
lectin
lipid membranes
protein–lipid interaction
cholesterol
brain lipids
topic Bioquímica
MACPF
snail pore-forming toxin
neurotoxin/enterotoxin
lectin
lipid membranes
protein–lipid interaction
cholesterol
brain lipids
dc.description.none.fl_txt_mv The perivitellin-2 (PV2) from snails is an unusual neuro and enterotoxin comprising a pore-forming domain of the Membrane Attack Complex and Perforin Family (MACPF) linked to a lectin. While both domains have membrane binding capabilities, PV2’s mechanism of action remains unclear. We studied the apple snail Pomacea maculata PV2’s (PmPV2’s) interaction with lipid membranes using various biophysical and cell biology approaches. In vitro studies showed that PmPV2 toxicity decreased when cholesterol (Chol) was diminished from enterocyte cell membranes. Chol enhanced PmPV2 association with phosphatidylcholine membranes but did not induce pore formation. In contrast, using rat brain lipid models, rich in glycolipids, PmPV2 exhibited high affinity and induced vesicle permeabilization. Negative stain electron microscopy and atomic force microscopy confirmed the formation of pore-like structures in brain lipid vesicles. Our findings suggest that Chol is a necessary lipid component and point to PmPV2–glycolipid interactions as potential activators critical to triggering PmPV2’s pore-forming activity, providing insights into this novel toxin’s mechanism.
Facultad de Ciencias Naturales y Museo
Instituto de Investigaciones Fisicoquímicas Teóricas y Aplicadas
description The perivitellin-2 (PV2) from snails is an unusual neuro and enterotoxin comprising a pore-forming domain of the Membrane Attack Complex and Perforin Family (MACPF) linked to a lectin. While both domains have membrane binding capabilities, PV2’s mechanism of action remains unclear. We studied the apple snail Pomacea maculata PV2’s (PmPV2’s) interaction with lipid membranes using various biophysical and cell biology approaches. In vitro studies showed that PmPV2 toxicity decreased when cholesterol (Chol) was diminished from enterocyte cell membranes. Chol enhanced PmPV2 association with phosphatidylcholine membranes but did not induce pore formation. In contrast, using rat brain lipid models, rich in glycolipids, PmPV2 exhibited high affinity and induced vesicle permeabilization. Negative stain electron microscopy and atomic force microscopy confirmed the formation of pore-like structures in brain lipid vesicles. Our findings suggest that Chol is a necessary lipid component and point to PmPV2–glycolipid interactions as potential activators critical to triggering PmPV2’s pore-forming activity, providing insights into this novel toxin’s mechanism.
publishDate 2025
dc.date.none.fl_str_mv 2025-04
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/10915/181867
url http://sedici.unlp.edu.ar/handle/10915/181867
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/2072-6651
info:eu-repo/semantics/altIdentifier/doi/10.3390/toxins17040183
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
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