Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles
- Autores
- Sayegh, Raphael Santa Rosa; De Fatima Correia Batista, Isabel; De Melo, Robson Lopes; Riske, Karin A.; Daffre, Sirlei; Montich, Guillermo Gabriel; Da Silva Junior, Pedro Ismael
- Año de publicación
- 2016
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- In contrast to vertebrate immune systems, invertebrates lack an adaptive response and rely solely on innate immunity in which antimicrobial peptides (AMPs) play an essential role. Most of them are membrane active molecules that are typically unstructured in solution and adopt secondary/tertiary structures upon binding to phospholipid bilayers. This work presents the first characterization of a constitutive AMP from the hemolymph of an Opiliones order animal: the harvestman Acutisoma longipes. This peptide was named longipin. It presents 18 aminoacid residues (SGYLPGKEYVYKYKGKVF) and a positive net charge at neutral pH. No similarity with other AMPs was observed. However, high sequence similarity with heme-lipoproteins from ticks suggested that longipin might be a protein fragment. The synthetic peptide showed enhanced antifungal activity against Candida guilliermondii and C. tropicalis yeasts (MIC: 3.8-7.5 μM) and did not interfered with VERO cells line viability at all concentrations tested (200-0.1 μM). This selectivity against microbial cells is related to the highest affinity of longipin for anionic charged vesicles (POPG:POPC) compared to zwitterionic ones (POPC), once microbial plasma membrane are generally more negatively charged compared to mammalian cells membrane. Dye leakage from carboxyfluoresceinloaded POPG:POPC vesicles suggested that longipin is a membrane active antimicrobial peptide and FT-IR spectroscopy showed that the peptide chain is mainly unstructured in solution or in the presence of POPC vesicles. However, upon binding to POPG:POPC vesicles, the FT-IR spectrum showed bands related to β-sheet and amyloid-like fibril conformations in agreement with thioflavin-T binding assays, indicating that longipin is an amyloid antimicrobial peptide.
Fil: Sayegh, Raphael Santa Rosa. Universidade de Sao Paulo; Brasil. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
Fil: De Fatima Correia Batista, Isabel. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
Fil: De Melo, Robson Lopes. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil
Fil: Riske, Karin A.. Universidade de Sao Paulo; Brasil
Fil: Daffre, Sirlei. Universidade de Sao Paulo; Brasil
Fil: Montich, Guillermo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Da Silva Junior, Pedro Ismael. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil. Universidade de Sao Paulo; Brasil - Materia
-
AMYLOYD
ANTIMICROBIAL
PEPTIDE
VESICLE - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/57385
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oai:ri.conicet.gov.ar:11336/57385 |
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CONICET Digital (CONICET) |
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Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesiclesSayegh, Raphael Santa RosaDe Fatima Correia Batista, IsabelDe Melo, Robson LopesRiske, Karin A.Daffre, SirleiMontich, Guillermo GabrielDa Silva Junior, Pedro IsmaelAMYLOYDANTIMICROBIALPEPTIDEVESICLEhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1In contrast to vertebrate immune systems, invertebrates lack an adaptive response and rely solely on innate immunity in which antimicrobial peptides (AMPs) play an essential role. Most of them are membrane active molecules that are typically unstructured in solution and adopt secondary/tertiary structures upon binding to phospholipid bilayers. This work presents the first characterization of a constitutive AMP from the hemolymph of an Opiliones order animal: the harvestman Acutisoma longipes. This peptide was named longipin. It presents 18 aminoacid residues (SGYLPGKEYVYKYKGKVF) and a positive net charge at neutral pH. No similarity with other AMPs was observed. However, high sequence similarity with heme-lipoproteins from ticks suggested that longipin might be a protein fragment. The synthetic peptide showed enhanced antifungal activity against Candida guilliermondii and C. tropicalis yeasts (MIC: 3.8-7.5 μM) and did not interfered with VERO cells line viability at all concentrations tested (200-0.1 μM). This selectivity against microbial cells is related to the highest affinity of longipin for anionic charged vesicles (POPG:POPC) compared to zwitterionic ones (POPC), once microbial plasma membrane are generally more negatively charged compared to mammalian cells membrane. Dye leakage from carboxyfluoresceinloaded POPG:POPC vesicles suggested that longipin is a membrane active antimicrobial peptide and FT-IR spectroscopy showed that the peptide chain is mainly unstructured in solution or in the presence of POPC vesicles. However, upon binding to POPG:POPC vesicles, the FT-IR spectrum showed bands related to β-sheet and amyloid-like fibril conformations in agreement with thioflavin-T binding assays, indicating that longipin is an amyloid antimicrobial peptide.Fil: Sayegh, Raphael Santa Rosa. Universidade de Sao Paulo; Brasil. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilFil: De Fatima Correia Batista, Isabel. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilFil: De Melo, Robson Lopes. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; BrasilFil: Riske, Karin A.. Universidade de Sao Paulo; BrasilFil: Daffre, Sirlei. Universidade de Sao Paulo; BrasilFil: Montich, Guillermo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Da Silva Junior, Pedro Ismael. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil. Universidade de Sao Paulo; BrasilPublic Library of Science2016-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/57385Sayegh, Raphael Santa Rosa; De Fatima Correia Batista, Isabel; De Melo, Robson Lopes; Riske, Karin A.; Daffre, Sirlei; et al.; Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles; Public Library of Science; Plos One; 11; 12; 12-20161932-6203CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0167953info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0167953info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:12:35Zoai:ri.conicet.gov.ar:11336/57385instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:12:36.279CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles |
title |
Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles |
spellingShingle |
Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles Sayegh, Raphael Santa Rosa AMYLOYD ANTIMICROBIAL PEPTIDE VESICLE |
title_short |
Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles |
title_full |
Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles |
title_fullStr |
Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles |
title_full_unstemmed |
Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles |
title_sort |
Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles |
dc.creator.none.fl_str_mv |
Sayegh, Raphael Santa Rosa De Fatima Correia Batista, Isabel De Melo, Robson Lopes Riske, Karin A. Daffre, Sirlei Montich, Guillermo Gabriel Da Silva Junior, Pedro Ismael |
author |
Sayegh, Raphael Santa Rosa |
author_facet |
Sayegh, Raphael Santa Rosa De Fatima Correia Batista, Isabel De Melo, Robson Lopes Riske, Karin A. Daffre, Sirlei Montich, Guillermo Gabriel Da Silva Junior, Pedro Ismael |
author_role |
author |
author2 |
De Fatima Correia Batista, Isabel De Melo, Robson Lopes Riske, Karin A. Daffre, Sirlei Montich, Guillermo Gabriel Da Silva Junior, Pedro Ismael |
author2_role |
author author author author author author |
dc.subject.none.fl_str_mv |
AMYLOYD ANTIMICROBIAL PEPTIDE VESICLE |
topic |
AMYLOYD ANTIMICROBIAL PEPTIDE VESICLE |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
In contrast to vertebrate immune systems, invertebrates lack an adaptive response and rely solely on innate immunity in which antimicrobial peptides (AMPs) play an essential role. Most of them are membrane active molecules that are typically unstructured in solution and adopt secondary/tertiary structures upon binding to phospholipid bilayers. This work presents the first characterization of a constitutive AMP from the hemolymph of an Opiliones order animal: the harvestman Acutisoma longipes. This peptide was named longipin. It presents 18 aminoacid residues (SGYLPGKEYVYKYKGKVF) and a positive net charge at neutral pH. No similarity with other AMPs was observed. However, high sequence similarity with heme-lipoproteins from ticks suggested that longipin might be a protein fragment. The synthetic peptide showed enhanced antifungal activity against Candida guilliermondii and C. tropicalis yeasts (MIC: 3.8-7.5 μM) and did not interfered with VERO cells line viability at all concentrations tested (200-0.1 μM). This selectivity against microbial cells is related to the highest affinity of longipin for anionic charged vesicles (POPG:POPC) compared to zwitterionic ones (POPC), once microbial plasma membrane are generally more negatively charged compared to mammalian cells membrane. Dye leakage from carboxyfluoresceinloaded POPG:POPC vesicles suggested that longipin is a membrane active antimicrobial peptide and FT-IR spectroscopy showed that the peptide chain is mainly unstructured in solution or in the presence of POPC vesicles. However, upon binding to POPG:POPC vesicles, the FT-IR spectrum showed bands related to β-sheet and amyloid-like fibril conformations in agreement with thioflavin-T binding assays, indicating that longipin is an amyloid antimicrobial peptide. Fil: Sayegh, Raphael Santa Rosa. Universidade de Sao Paulo; Brasil. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil Fil: De Fatima Correia Batista, Isabel. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil Fil: De Melo, Robson Lopes. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil Fil: Riske, Karin A.. Universidade de Sao Paulo; Brasil Fil: Daffre, Sirlei. Universidade de Sao Paulo; Brasil Fil: Montich, Guillermo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina Fil: Da Silva Junior, Pedro Ismael. Governo do Estado de Sao Paulo. Secretaria da Saude. Instituto Butantan; Brasil. Universidade de Sao Paulo; Brasil |
description |
In contrast to vertebrate immune systems, invertebrates lack an adaptive response and rely solely on innate immunity in which antimicrobial peptides (AMPs) play an essential role. Most of them are membrane active molecules that are typically unstructured in solution and adopt secondary/tertiary structures upon binding to phospholipid bilayers. This work presents the first characterization of a constitutive AMP from the hemolymph of an Opiliones order animal: the harvestman Acutisoma longipes. This peptide was named longipin. It presents 18 aminoacid residues (SGYLPGKEYVYKYKGKVF) and a positive net charge at neutral pH. No similarity with other AMPs was observed. However, high sequence similarity with heme-lipoproteins from ticks suggested that longipin might be a protein fragment. The synthetic peptide showed enhanced antifungal activity against Candida guilliermondii and C. tropicalis yeasts (MIC: 3.8-7.5 μM) and did not interfered with VERO cells line viability at all concentrations tested (200-0.1 μM). This selectivity against microbial cells is related to the highest affinity of longipin for anionic charged vesicles (POPG:POPC) compared to zwitterionic ones (POPC), once microbial plasma membrane are generally more negatively charged compared to mammalian cells membrane. Dye leakage from carboxyfluoresceinloaded POPG:POPC vesicles suggested that longipin is a membrane active antimicrobial peptide and FT-IR spectroscopy showed that the peptide chain is mainly unstructured in solution or in the presence of POPC vesicles. However, upon binding to POPG:POPC vesicles, the FT-IR spectrum showed bands related to β-sheet and amyloid-like fibril conformations in agreement with thioflavin-T binding assays, indicating that longipin is an amyloid antimicrobial peptide. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016-12 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion 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://hdl.handle.net/11336/57385 Sayegh, Raphael Santa Rosa; De Fatima Correia Batista, Isabel; De Melo, Robson Lopes; Riske, Karin A.; Daffre, Sirlei; et al.; Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles; Public Library of Science; Plos One; 11; 12; 12-2016 1932-6203 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/57385 |
identifier_str_mv |
Sayegh, Raphael Santa Rosa; De Fatima Correia Batista, Isabel; De Melo, Robson Lopes; Riske, Karin A.; Daffre, Sirlei; et al.; Longipin: An amyloid antimicrobial peptide from the harvestman Acutisoma longipes (Arachnida: Opiliones) with preferential affinity for anionic vesicles; Public Library of Science; Plos One; 11; 12; 12-2016 1932-6203 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.1371/journal.pone.0167953 info:eu-repo/semantics/altIdentifier/url/http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0167953 |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Public Library of Science |
publisher.none.fl_str_mv |
Public Library of Science |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1844614034819645440 |
score |
13.070432 |