Proteomic endorsed transcriptomic profiles of venom glands from Tityus obscurus and T. serrulatus scorpions

Abstract

BackgroundExcept for the northern region, where the Amazonian black scorpion, T. obscurus, represents the predominant and most medically relevant scorpion species, Tityus serrulatus, the Brazilian yellow scorpion, is widely distributed throughout Brazil, causing most envenoming and fatalities due to scorpion sting. In order to evaluate and compare the diversity of venom components of Tityus obscurus and T. serrulatus, we performed a transcriptomic investigation of the telsons (venom glands) corroborated by a shotgun proteomic analysis of the venom from the two species.ResultsThe putative venom components represented 11.4% and 16.7% of the total gene expression for T. obscurus and T. serrulatus, respectively. Transcriptome and proteome data revealed high abundance of metalloproteinases sequences followed by sodium and potassium channel toxins, making the toxin core of the venom. The phylogenetic analysis of metalloproteinases from T. obscurus and T. serrulatus suggested an intraspecific gene expansion, as we previously observed for T. bahiensis, indicating that this enzyme may be under evolutionary pressure for diversification. We also identified several putative venom components such as anionic peptides, antimicrobial peptides, bradykinin-potentiating peptide, cysteine rich protein, serine proteinases, cathepsins, angiotensin-converting enzyme, endothelin-converting enzyme and chymotrypsin like protein, proteinases inhibitors, phospholipases and hyaluronidases.ConclusionThe present work shows that the venom composition of these two allopatric species of Tityus are considerably similar in terms of the major classes of proteins produced and secreted, although their individual toxin sequences are considerably divergent. These differences at amino acid level may reflect in different epitopes for the same protein classes in each species, explaining the basis for the poor recognition of T. obscurus venom by the antiserum raised against other species.

Insights into the Hypertensive Effects of Tityus serrulatus Scorpion Venom: Purification of an Angiotensin-Converting Enzyme-Like Peptidase

“…Thus, the ACE-like enzyme present in Ts v has a molecular mass similar to tACE. Besides the precursor of ACE-like peptidase being sequenced by RNA sequencing (GenBank TserSP00939) and the identification of the ACE-like peptidase from T. serrulatus through mass spectrometric analysis, the isoform sequences are also present in transcripts from the venom gland of T. bahiensis (GenBank JAG85170.1), T. stigmurus [30], and T. obscurus (GenBank Tobs01141 and GenBank Tobs00978) [36]. Thus, these sequences helped to validate the purification of this enzyme, achieving two unique peptides from T. serrulatus ’s ACE-like sequence.…”

Involvement of the Endothelin Receptor Type A in the Cardiovascular Inflammatory Response Following Scorpion Envenomation

“…The etiology of the cardiovascular manifestations observed after scorpion envenomation is due to venom effects on the sympathetic nervous system and/or on the myocardium itself, as well as to the release of cathecholamines, neuropeptide Y(NPY), angiotensin II, and endothelin-1 (ET-1) induced after envenomation [ 6 , 10 , 11 , 12 , 13 , 14 , 15 , 16 ]. Proteases such as the angiotensin-converting enzyme (ACE) and endothelin-converting enzyme (ECE), isolated from Tityus species venom, may also contribute to the cardiovascular perturbations, including hemodynamic disorders, observed in human envenomation victims [ 17 , 18 ]. The inflammatory process and the overproduction of free radicals are frequently triggered by scorpion venom and promote cardiac injury [ 7 , 16 , 19 , 20 ].…”

Purificação e caracterização de peptidases presentes no veneno do escorpião <i>Tityus serrulatus</i>.

“…Thus, the ACE-like enzyme present in Tsv has a molecular mass similar to tACE. Besides the precursor of ACE-like peptidase being sequenced by RNA sequencing (GenBank TserSP00939) and the identification of the ACE-like peptidase from T. serrulatus through mass spectrometric analysis, the isoform sequences are also present in transcripts from the venom gland of T. bahiensis (GenBank JAG85170.1), T. stigmurus [30], and T. obscurus (GenBank Tobs01141 and GenBank Tobs00978) [36]. Thus, these sequences helped to validate the purification of this enzyme, achieving two unique peptides 9 of 16 from T. serrulatus's ACE-like sequence.…”