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dc.contributor.authorDINIZ, M. R. V.
dc.contributor.authorPAIVA, A. L. B.
dc.contributor.authorGUERRA-DUARTE, C.
dc.contributor.authorNISHIYAMA JÚNIOR, M. Y.
dc.contributor.authorMUDADU, M. de A.
dc.contributor.authorOLIVEIRA, U. de
dc.contributor.authorBORGES, M. H.
dc.contributor.authorYATES, J. R.
dc.contributor.authorJUNQUEIRA-DE-AZEVEDO, I. de
dc.date.accessioned2018-12-23T23:30:29Z-
dc.date.available2018-12-23T23:30:29Z-
dc.date.created2018-12-20
dc.date.issued2018
dc.identifier.citationPlos One, v. 13, n. 8, p. 1-29, 2018.
dc.identifier.urihttp://www.alice.cnptia.embrapa.br/alice/handle/doc/1102272-
dc.descriptionAbstract. Phoneutria nigriventer is one of the largest existing true spiders and one of the few considered medically relevant. Its venom contains several neurotoxic peptides that act on different ion channels and chemical receptors of vertebrates and invertebrates. Some of these venom toxins have been shown as promising models for pharmaceutical or biotechnological use. However, the large diversity and the predominance of low molecular weight toxins in this venom have hampered the identification and deep investigation of the less abundant toxins and the proteins with high molecular weight. Here, we combined conventional and next-generation cDNA sequencing with Multidimensional Protein Identification Technology (MudPIT), to obtain an in-depth panorama of the composition of P. nigriventer spider venom. The results from these three approaches showed that cysteine-rich peptide toxins are the most abundant components in this venom and most of them contain the Inhibitor Cysteine Knot (ICK) structural motif. Ninety-eight sequences corresponding to cysteine-rich peptide toxins were identified by the three methodologies and many of them were considered as putative novel toxins, due to the low similarity to previously described toxins. Furthermore, using next-generation sequencing we identified families of several other classes of toxins, including CAPs (Cysteine Rich Secretory ProteinÐCRiSP, antigen 5 and Pathogenesis-Related 1ÐPR-1), serine proteinases, TCTPs (translationally controlled tumor proteins), proteinase inhibitors, metalloproteinases and hyaluronidases, which have been poorly described for this venom. This study provides an overview of the molecular diversity of P. nigriventer venom, revealing several novel components and providing a better basis to understand its toxicity and pharmacological activities.
dc.language.isoengeng
dc.rightsopenAccesseng
dc.subjectProteômica
dc.subjectTranscriptoma
dc.titleAn overview of Phoneutria nigriventer spider venom using combined transcriptomic and proteomic approaches.
dc.typeArtigo de periódico
dc.date.updated2018-12-23T23:30:29Zpt_BR
dc.subject.nalthesaurusPhoneutria nigriventer
dc.subject.nalthesaurusProteomics
dc.subject.nalthesaurusTranscriptomics
dc.description.notesArtigo e0200628. Na publicação: Mauricio A. Mudadu.
riaa.ainfo.id1102272
riaa.ainfo.lastupdate2020-12-30 -02:00:00
dc.identifier.doihttps://doi.org/10.1371/journal. pone.0200628
dc.contributor.institutionMARCELO R. V. DINIZ, Fundação Ezequiel Dias, Belo Horizonte; ANA L. B. PAIVA, Fundação Ezequiel Dias, Belo Horizonte; CLARA GUERRA-DUARTE, Fundação Ezequiel Dias, Belo Horizonte; MILTON Y. NISHIYAMA JÚNIOR, Instituto Butantan, São Paulo; MAURICIO DE ALVARENGA MUDADU, CNPTIA; URSULA DE OLIVEIRA, Instituto Butantan, São Paulo; MÁRCIA H. BORGES, Fundação Ezequiel Dias, Belo Horizonte; JOHN R. YATES, The Scripps Research Institute; INÁCIO DE L. JUNQUEIRA-DE-AZEVEDO, Instituto Butantan, São Paulo.
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