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
- Institución
- Universidad Nacional de La Plata
- OAI Identificador
- oai:sedici.unlp.edu.ar:10915/181867
Ver los metadatos del registro completo
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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 |
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info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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openAccess |
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http://creativecommons.org/licenses/by/4.0/ Creative Commons Attribution 4.0 International (CC BY 4.0) |
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application/pdf |
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SEDICI (UNLP) - Universidad Nacional de La Plata |
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