Longipin: An Amyloid Antimicrobial Peptide from the Harvestman Acutisoma longipes (Arachnida: Opiliones) with Preferential Affinity for Anionic Vesicles

dc.contributor.authorRosa Sayegh, Raphael Santa
dc.contributor.authorCorreia Batista, Isabel de Fatima
dc.contributor.authorde Melo, Robson Lopes
dc.contributor.authorRiske, Karin do Amaral [UNIFESP]
dc.contributor.authorDaffre, Sirlei
dc.contributor.authorMontich, Guillermo
dc.contributor.authorda Silva Junior, Pedro Ismael
dc.coverageSan Francisco
dc.description.abstractIn 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.en
dc.description.affiliationUniv Sao Paulo, Inst Ciencias Biomed, Programa Interunidades Biotecnol, Sao Paulo, Brazil
dc.description.affiliationInst Butantan, Lab Especial Toxinol Aplicada, Sao Paulo, Brazil
dc.description.affiliationInst Butantan, Unidade Sequenciamento Prot & Peptideos, Sao Paulo, Brazil
dc.description.affiliationInst Butantan, Lab Bioquim & Biofis, Sao Paulo, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Biofis, Sao Paulo, Brazil
dc.description.affiliationUniv Sao Paulo, Inst Ciencias Biomed, Dept Parasitol, Sao Paulo, Brazil
dc.description.affiliationUniv Nacl Cordoba, Fac Ciencias Quim, Dept Quim Biol, Ctr Invest Quim Biol Cordoba CIQUIBIC,CONICET, Cordoba, Argentina
dc.description.affiliationUnifespDepartamento de Biofísica, Universidade Federal de São Paulo, São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.description.sponsorshipRed de Universidades de America Latina y el Caribe
dc.description.sponsorshipIDFAPESP: 2013/07467-1
dc.description.sponsorshipIDCNPq: 472744/2012-7
dc.identifier.citationPlos One. San Francisco, v. 11, n. 12, p. -, 2016.
dc.publisherPublic Library Science
dc.relation.ispartofPlos One
dc.rightsAcesso aberto
dc.titleLongipin: An Amyloid Antimicrobial Peptide from the Harvestman Acutisoma longipes (Arachnida: Opiliones) with Preferential Affinity for Anionic Vesiclesen
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