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

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

Author Abreu, Thiago F. Autor UNIFESP Google Scholar
Sumitomo, Bianca N. Autor UNIFESP Google Scholar
Nishiyama, Milton Y., Jr. Google Scholar
Oliveira, Ursula C. Google Scholar
Souza, Gustavo H. M. F. Google Scholar
Kitano, Eduardo S. Google Scholar
Zelanis, Andre Autor UNIFESP Google Scholar
Serrano, Solange M. T. Google Scholar
Junqueira-de-Azevedo, Inacio Google Scholar
Silva, Pedro I., Jr. Google Scholar
Tashima, Alexandre K. Autor UNIFESP Google Scholar
Abstract Acanthoscurria 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.
Keywords Acanthoscurria gomesiana
Peptidomics
Antimicrobial peptide
Theraphotoxin
xmlui.dri2xhtml.METS-1.0.item-coverage Amsterdam
Language English
Sponsor Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP)
Financiadora de Estudos e Projetos (FINEP)
Coordenacao de Aperfeicoamento de Pessoal de Nivel Superior (CAPES)
Conselho Nacional de Desenvolvimento Cientifico e Tecnologico/Brazil (CNPq)
Grant number FAPESP: 2012/19321-9
Date 2017
Published in Journal Of Proteomics. Amsterdam, v. 151, p. 232-242, 2017.
ISSN 1874-3919 (Sherpa/Romeo, impact factor)
Publisher Elsevier Science Bv
Extent 232-242
Origin http://dx.doi.org/10.1016/j.jprot.2016.07.012
Access rights Closed access
Type Article
Web of Science ID WOS:000390964900023
URI https://repositorio.unifesp.br/handle/11600/55240

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