Peptidomics of Acanthoscurria gomesiana spider venom reveals new toxins with potential antimicrobial activity

Página do item simplificado
dc.citation.volume151
dc.contributor.authorAbreu, Thiago F. [UNIFESP]
dc.contributor.authorSumitomo, Bianca N. [UNIFESP]
dc.contributor.authorNishiyama, Milton Y., Jr.
dc.contributor.authorOliveira, Ursula C.
dc.contributor.authorSouza, Gustavo H. M. F.
dc.contributor.authorKitano, Eduardo S.
dc.contributor.authorZelanis, Andre [UNIFESP]
dc.contributor.authorSerrano, Solange M. T.
dc.contributor.authorJunqueira-de-Azevedo, Inacio
dc.contributor.authorSilva, Pedro I., Jr.
dc.contributor.authorTashima, Alexandre K. [UNIFESP]
dc.coverageAmsterdam
dc.date.accessioned2020-07-17T14:03:14Z
dc.date.available2020-07-17T14:03:14Z
dc.date.issued2017
dc.description.abstractAcanthoscurria gomesiana is a Brazilian spider from the Theraphosidae family inhabiting regions of Southeastern Brazil. Potent antimicrobial peptides as gomesin and acanthoscurrin have been discovered from the spider hemolymph in previous works. Spider venoms are also recognized as sources of biologically active peptides, however the venom peptidome of A. gomesiana remained unexplored to date. In this work, a MS-based workflow was applied to the investigation of the spider venom peptidome. Data-independent and data-dependent LC-MS/MS acquisitions of intact peptides and of peptides submitted to multiple enzyme digestions, followed by automated chromatographic alignment, de novo analysis, database and homology searches with manual validations showed that the venom is composed by <165 features, with masses ranging from 0.4-15.8 kDa. From digestions, 135 peptides were identified from 17 proteins, including three new mature peptides: U1-TRTX-Agm1a, U1-TRTX-Agm2a and Ul-TRTX-Agm3a, containing 3, 4 and 3 disulfide bonds, respectively. The toxins U1-TRTX-Agm1a differed by only one amino acid from Ul-TRTX-Apl a from A. paulensis and U1-TRTX-Agm2a was derived from the genicutoxin-D1 precursor from A. geniculata. These toxins have potential applications as antimicrobial agents, as the peptide fraction of A. gomesiana showed activity against Escherichia coli, Enterobacter cloacae and Candida albicans strains. MS data are available via ProteomeXchange Consortium with identifier PXD003884. Biological significance: Biological fluids of the Acanthoscurria gomesiana spider are sources of active molecules, as is the case of antimicrobial peptides and acylpolyamines found in the hemolymphs. The venom is also a potential source of toxins with pharmacological and biotechnological applications. However, to our knowledge no A. gomesiana venom toxin structure has been determined to date. Using a combination of high resolution mass spectrometry, transcriptomics and bioinformatics, we employed a workflow to fully sequence, determine the number of disulfide bonds of mature peptides and we found new potential antimicrobial peptides. This workflow is suitable for complete peptide toxin sequencing when handling limited amount of venom samples and can accelerate the discovery of peptides with potential biotechnological applications. (C) 2016 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv Fed Sao Paulo, Escola Paulista Med, Dept Bioquim, Rua Botucatu 862, BR-04023901 Sao Paulo, SP, Brazil
dc.description.affiliationInst Butantan, Ctr Toxins Immune Response & Cell Signaling, Lab Especial Toxinol Aplicada, Sao Paulo, SP, Brazil
dc.description.affiliationWaters Corp, Mass Spectrometry Applicat Res & Dev Lab, Sao Paulo, SP, Brazil
dc.description.affiliationUniv Fed Sao Paulo, Dept Ciencia & Tecnol, ICT UNIFESP, Sao Jose Dos Campos, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Escola Paulista Med, Dept Bioquim, Rua Botucatu 862, BR-04023901 Sao Paulo, SP, Brazil
dc.description.affiliationUnifespUniv Fed Sao Paulo, Dept Ciencia & Tecnol, ICT UNIFESP, Sao Jose Dos Campos, SP, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
dc.description.sponsorshipFinanciadora de Estudos e Projetos (FINEP)
dc.description.sponsorshipCoordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Cientifico e Tecnologico/Brazil (CNPq)
dc.description.sponsorshipIDFAPESP: 2012/19321-9
dc.format.extent232-242
dc.identifierhttp://dx.doi.org/10.1016/j.jprot.2016.07.012
dc.identifier.citationJournal Of Proteomics. Amsterdam, v. 151, p. 232-242, 2017.
dc.identifier.doi10.1016/j.jprot.2016.07.012
dc.identifier.issn1874-3919
dc.identifier.urihttps://repositorio.unifesp.br/handle/11600/55240
dc.identifier.wosWOS:000390964900023
dc.language.isoeng
dc.publisherElsevier Science Bv
dc.relation.ispartofJournal Of Proteomics
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectAcanthoscurria gomesianaen
dc.subjectPeptidomicsen
dc.subjectAntimicrobial peptideen
dc.subjectTheraphotoxinen
dc.titlePeptidomics of Acanthoscurria gomesiana spider venom reveals new toxins with potential antimicrobial activityen
dc.typeinfo:eu-repo/semantics/article
Arquivos
Coleções
EPM - Artigos
ICT - Artigos