Project description:Acanthoscurria juruenicola is an Amazonian tarantula spider described for the first time a century ago. Specimens of both genders are similar in size and in most morphological aspects, but ecological behavior and their venom composition remained unknown to date. Here we present the peptidomics characterization of the spider venom by a combination of mass spectrometric analysis of both native and digested peptides, venom gland transcriptomics and bioinformatics. A total of 367 native features were observed in the venom peptidome. Seventeen cysteine-rich peptides were simultaneously observed in the transcriptome and in the mass spectrometric experiments, from which fourteen were completely sequenced in the mature forms. The mature peptides have 3-5 disulfide bonds and cover the 3.7-8.6 kDa mass range. Moreover, in vivo paralytic activities of the whole venom were observed in crickets. In silico analysis indicated that all mature peptides are potentially antimicrobial and two may be potential anticancer agents. The antimicrobial activity was experimentally confirmed for the peptide Ap1a against Micrococcus luteus, Pseudomonas aeruginosa and Candida albicans.

2022-10-20 | PXD013149 | Pride

Venom proteomics of the Amazonian spider Acanthoscurria juruenicola

2021-07-08 | MSV000087777 | MassIVE

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

Project description: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.

2016-08-02 | PXD003884 | Pride

A multi-omics approach unravels new toxins with potential antimicrobial, antiviral and antitumoral activities in the venom of Acanthoscurria rondoniae

Project description:The Araneae order is considered one of the most successful group among venomous animals in the world. An important factor for this success is the production of venoms, a refined biological fluid rich in proteins, short peptides and cysteine-rich peptides (CRPs). These toxins may present pharmacologically relevant biological actions, as antimicrobial, antiviral and anticancer activities, for instance. Therefore, there is an increasing interest in the exploration of venom toxins for therapeutic reasons, such as drug development. However, the process of peptide sequencing and mainly the evaluation of potential biological activities of these peptides is laborious, considering the low yield of venom extraction and the high variability of toxins present in spider venoms. Here we show a robust methodology for identification, sequencing, and initial screening of potential bioactive peptides found in the venom of Acanthoscurria rondoniae. This methodology consists in a multi-omics approach involving proteomics, peptidomics and transcriptomics analyses allied to in silico predictions of antibacterial, antifungal, antiviral and anticancer activities. Through the application of this strategy, a total of 92,889 venom gland transcripts were assembled and 84 novel toxins were identified at the protein level, including 7 short peptides and 10 fully sequenced CRPs (belonging to 7 toxin families). In silico analysis revealed that 7 CRPs families have potential antimicrobial or antiviral activities, while 2 CRPs and four short peptides are potentially anticancer. Taken together, our results demonstrate an effective multi-omics strategy for the discovery of new toxins and in silico screening of potential bioactivities. This strategy may be useful in toxin discovery, as well as in the screening of activities for the vast diversity of molecules produced by venomous animals.

2020-07-20 | PXD019343 | Pride