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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/57385
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/57385
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling 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 Técnicas2025-10-22T11:42:29Zoai: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:34982025-10-22 11:42:30.263CONICET 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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score 12.982451

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