Dataset Information

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

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 less than 165 features, with masses ranging from 0.4-15.8 kDa. A total of 135 peptides from 17 proteins were identified, including three new mature peptides: U1-TRTX-Agm1a, U1-TRTX-Agm2a and U1-TRTX-Agm3a, containing 3, 4 and 3 disulfide bonds, respectively. U1-TRTX-Agm1a differed by only one amino acid from U1-TRTX-Ap1a 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 strains.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Acanthoscurria Gomesiana (tarantula Spider) (phormictopus Pheopygus)

SUBMITTER: Alexandre Keiji Tashima

LAB HEAD: Alexandre Keiji Tashima

PROVIDER: PXD003884 | Pride | 2016-08-02

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20151218_AGF_Peptidoma_R001_CID_PEAK.pkl	Other
	20151218_AGF_Peptidoma_R001_RAW.raw.zip	Raw
	20151218_AGF_Peptidoma_R002_CID_PEAK.pkl	Other
	20151218_AGF_Peptidoma_R002_RAW.raw.zip	Raw
	20151218_AGF_Peptidoma_R003_CID_PEAK.pkl	Other

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Publications

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

Abreu Thiago F TF Sumitomo Bianca N BN Nishiyama Milton Y MY Oliveira Ursula C UC Souza Gustavo H M F GH Kitano Eduardo S ES Zelanis André A Serrano Solange M T SM Junqueira-de-Azevedo Inácio I Silva Pedro I PI Tashima Alexandre K AK

Journal of proteomics 20160717

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- ...[more]

PMID: 27436114

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Project description:Spider venoms are a unique source of bioactive peptides displaying remarkable structural stability and potent neuroactivity. Phoneutria nigriventer, often referred to as Brazilian wandering spider, banana spider or “armed” spider, is endemic from South America and amongst the most dangerous venomous spiders in the world. Envenomation accidents with P. nigriventer often occur in Brazil with approximately 4,000 cases per year and which symptoms include priapism, hypertension, blurred vision, sweating, and vomiting, amongst others. Besides its clinical relevance, P. nigriventer venom comprises promising peptide drug leads providing therapeutic effects in a range of disease models. In this study, we further explored the neuroactivity and molecular diversity of the venom from P. nigriventer using fractionation-guided high-throughput cellular assays coupled to proteomics analysis and multi-pharmacology activity to broaden the knowledge and therapeutic potential of this venom, as well as a proof-of-concept for an investigative pipeline to study spider-venom derived neuroactive peptides. We applied ion channel assays in a neuroblastoma cell line to investigate modulation of voltage-gated sodium and calcium channels, and nicotinic acetylcholine α7 receptor. We then investigated the venom components using mass spectrometry to identify peptide masses and sequences associated to the observed neuromodulations. Our findings showed this venom is highly complex compared to other neurotoxin-rich venoms and comprises potent modulators of voltage-gated sodium and calcium channels which were classified into 4 families of neuroactive peptides based on their activities and structures. In addition to the reported P. nigriventer neuroactive peptides, we identified at least 27 novel cysteine-rich venom peptides in which neuroactivities are still to be elucidated in voltage-gated ion channels and other potential targets. Our findings provide a new basis for studying non-explored bioactivities of known and novel neuroactive components in P. nigriventer venom, and further supports the successful application of our discovery pipeline for identifying ion channel-targeting venom peptides with potential to become drug leads with diverse exploratory and therapeutic applications.