Longipin: An Amyloid Antimicrobial Peptide from the Harvestman Acutisoma longipes (Arachnida: Opiliones) with Preferential Affinity for Anionic Vesicles
Autor(a) principal: | |
---|---|
Data de Publicação: | 2016 |
Outros Autores: | , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Institucional da UNIFESP |
Texto Completo: | https://repositorio.unifesp.br/handle/11600/56541 http://dx.doi.org/10.1371/journal.pone.0167953 |
Resumo: | 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 mu M) and did not interfered with VERO cells line viability at all concentrations tested (200-0.1 mu M). 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 carboxyfluorescein-loaded 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 beta-sheet and amyloid-like fibril conformations in agreement with thioflavin-T binding assays, indicating that longipin is an amyloid antimicrobial peptide. |
id |
UFSP_b9b80db24fbcf88ef5247afbbf48e986 |
---|---|
oai_identifier_str |
oai:repositorio.unifesp.br:11600/56541 |
network_acronym_str |
UFSP |
network_name_str |
Repositório Institucional da UNIFESP |
repository_id_str |
3465 |
spelling |
Rosa Sayegh, Raphael SantaCorreia Batista, Isabel de Fatimade Melo, Robson LopesRiske, Karin do Amaral [UNIFESP]Daffre, SirleiMontich, Guillermoda Silva Junior, Pedro Ismael2020-07-31T12:47:02Z2020-07-31T12:47:02Z2016Plos One. San Francisco, v. 11, n. 12, p. -, 2016.1932-6203https://repositorio.unifesp.br/handle/11600/56541http://dx.doi.org/10.1371/journal.pone.0167953WOS000392842900020.pdf10.1371/journal.pone.0167953WOS:000392842900020In 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 mu M) and did not interfered with VERO cells line viability at all concentrations tested (200-0.1 mu M). 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 carboxyfluorescein-loaded 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 beta-sheet and amyloid-like fibril conformations in agreement with thioflavin-T binding assays, indicating that longipin is an amyloid antimicrobial peptide.Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)Red de Universidades de America Latina y el CaribeUniv Sao Paulo, Inst Ciencias Biomed, Programa Interunidades Biotecnol, Sao Paulo, BrazilInst Butantan, Lab Especial Toxinol Aplicada, Sao Paulo, BrazilInst Butantan, Unidade Sequenciamento Prot & Peptideos, Sao Paulo, BrazilInst Butantan, Lab Bioquim & Biofis, Sao Paulo, BrazilUniv Fed Sao Paulo, Dept Biofis, Sao Paulo, BrazilUniv Sao Paulo, Inst Ciencias Biomed, Dept Parasitol, Sao Paulo, BrazilUniv Nacl Cordoba, Fac Ciencias Quim, Dept Quim Biol, Ctr Invest Quim Biol Cordoba CIQUIBIC,CONICET, Cordoba, ArgentinaDepartamento de Biofísica, Universidade Federal de São Paulo, São Paulo, BrazilFAPESP: 2013/07467-1CNPq: 472744/2012-7Web of Science-engPublic Library SciencePlos OneLongipin: An Amyloid Antimicrobial Peptide from the Harvestman Acutisoma longipes (Arachnida: Opiliones) with Preferential Affinity for Anionic Vesiclesinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleSan Francisco1112info:eu-repo/semantics/openAccessreponame:Repositório Institucional da UNIFESPinstname:Universidade Federal de São Paulo (UNIFESP)instacron:UNIFESPORIGINALWOS000392842900020.pdfapplication/pdf2571437${dspace.ui.url}/bitstream/11600/56541/1/WOS000392842900020.pdf52ebccf64946112a20fefa1689cfe94aMD51open accessTEXTWOS000392842900020.pdf.txtWOS000392842900020.pdf.txtExtracted texttext/plain69622${dspace.ui.url}/bitstream/11600/56541/2/WOS000392842900020.pdf.txt150f868a3203c35a339f699e3655056cMD52open accessTHUMBNAILWOS000392842900020.pdf.jpgWOS000392842900020.pdf.jpgIM Thumbnailimage/jpeg7928${dspace.ui.url}/bitstream/11600/56541/4/WOS000392842900020.pdf.jpgd2b70017032c0897f1a92a5658e1d65dMD54open access11600/565412022-07-31 23:51:54.513open accessoai:repositorio.unifesp.br:11600/56541Repositório InstitucionalPUBhttp://www.repositorio.unifesp.br/oai/requestopendoar:34652022-08-01T02:51:54Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP)false |
dc.title.en.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 Rosa Sayegh, Raphael Santa |
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 |
author |
Rosa Sayegh, Raphael Santa |
author_facet |
Rosa Sayegh, Raphael Santa Correia Batista, Isabel de Fatima de Melo, Robson Lopes Riske, Karin do Amaral [UNIFESP] Daffre, Sirlei Montich, Guillermo da Silva Junior, Pedro Ismael |
author_role |
author |
author2 |
Correia Batista, Isabel de Fatima de Melo, Robson Lopes Riske, Karin do Amaral [UNIFESP] Daffre, Sirlei Montich, Guillermo da Silva Junior, Pedro Ismael |
author2_role |
author author author author author author |
dc.contributor.author.fl_str_mv |
Rosa Sayegh, Raphael Santa Correia Batista, Isabel de Fatima de Melo, Robson Lopes Riske, Karin do Amaral [UNIFESP] Daffre, Sirlei Montich, Guillermo da Silva Junior, Pedro Ismael |
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 mu M) and did not interfered with VERO cells line viability at all concentrations tested (200-0.1 mu M). 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 carboxyfluorescein-loaded 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 beta-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.issued.fl_str_mv |
2016 |
dc.date.accessioned.fl_str_mv |
2020-07-31T12:47:02Z |
dc.date.available.fl_str_mv |
2020-07-31T12:47:02Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.citation.fl_str_mv |
Plos One. San Francisco, v. 11, n. 12, p. -, 2016. |
dc.identifier.uri.fl_str_mv |
https://repositorio.unifesp.br/handle/11600/56541 http://dx.doi.org/10.1371/journal.pone.0167953 |
dc.identifier.issn.none.fl_str_mv |
1932-6203 |
dc.identifier.file.none.fl_str_mv |
WOS000392842900020.pdf |
dc.identifier.doi.none.fl_str_mv |
10.1371/journal.pone.0167953 |
dc.identifier.wos.none.fl_str_mv |
WOS:000392842900020 |
identifier_str_mv |
Plos One. San Francisco, v. 11, n. 12, p. -, 2016. 1932-6203 WOS000392842900020.pdf 10.1371/journal.pone.0167953 WOS:000392842900020 |
url |
https://repositorio.unifesp.br/handle/11600/56541 http://dx.doi.org/10.1371/journal.pone.0167953 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.ispartof.none.fl_str_mv |
Plos One |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
- |
dc.coverage.none.fl_str_mv |
San Francisco |
dc.publisher.none.fl_str_mv |
Public Library Science |
publisher.none.fl_str_mv |
Public Library Science |
dc.source.none.fl_str_mv |
reponame:Repositório Institucional da UNIFESP instname:Universidade Federal de São Paulo (UNIFESP) instacron:UNIFESP |
instname_str |
Universidade Federal de São Paulo (UNIFESP) |
instacron_str |
UNIFESP |
institution |
UNIFESP |
reponame_str |
Repositório Institucional da UNIFESP |
collection |
Repositório Institucional da UNIFESP |
bitstream.url.fl_str_mv |
${dspace.ui.url}/bitstream/11600/56541/1/WOS000392842900020.pdf ${dspace.ui.url}/bitstream/11600/56541/2/WOS000392842900020.pdf.txt ${dspace.ui.url}/bitstream/11600/56541/4/WOS000392842900020.pdf.jpg |
bitstream.checksum.fl_str_mv |
52ebccf64946112a20fefa1689cfe94a 150f868a3203c35a339f699e3655056c d2b70017032c0897f1a92a5658e1d65d |
bitstream.checksumAlgorithm.fl_str_mv |
MD5 MD5 MD5 |
repository.name.fl_str_mv |
Repositório Institucional da UNIFESP - Universidade Federal de São Paulo (UNIFESP) |
repository.mail.fl_str_mv |
|
_version_ |
1802764118248128512 |