Tityus serrulatus Hypotensins: A new family of peptides from scorpion venom

Verano‐Braga, Thiago; Rocha‐Resende, Cibele; Silva, D.M.; Ianzer, Danielle; Martin‐Eauclaire, Marie‐France; Bougis, Pierre E.; Lima, Maria Elena de; Santos, Robson A.S.; Pimenta, Adriano M.C.

doi:10.1016/j.bbrc.2008.04.104

Cited by 80 publications

(51 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In scorpions, hypotensin-like peptides have been described for Tityus serrulatus (Rates et al, 2008;VeranoBraga et al, 2008) and Tityus stigmurus (Almeida et al, 2012). Verano-Braga et al (2008, 2010) described a hypotensin-like peptide of Tityus serrulatus venom that acts as an agonist of the receptor B(2) and, unlike other Bradykinin-potentiating peptides (BPPs), did not inhibit angiotensin-converting enzymes. The T. bahiensis hypotensin-like peptide precursor, such as those from T. stigmurus (Almeida et al, 2012), have 24 signal peptide amino acids, pro domain, mature peptide and a post domain, suggesting post translational modifications since the active peptide has only 25 amino acids (Verano-Braga et al, 2008).…”

Section: Other Putative Venom Componentsmentioning

confidence: 96%

“…Verano-Braga et al (2008, 2010) described a hypotensin-like peptide of Tityus serrulatus venom that acts as an agonist of the receptor B(2) and, unlike other Bradykinin-potentiating peptides (BPPs), did not inhibit angiotensin-converting enzymes. The T. bahiensis hypotensin-like peptide precursor, such as those from T. stigmurus (Almeida et al, 2012), have 24 signal peptide amino acids, pro domain, mature peptide and a post domain, suggesting post translational modifications since the active peptide has only 25 amino acids (Verano-Braga et al, 2008). The sequences from T. bahiensis described here presented slight differences compared to T. serrulatus and T. stigmurus, as shown in Fig.…”

Section: Other Putative Venom Componentsmentioning

confidence: 98%

See 1 more Smart Citation

The transcriptome recipe for the venom cocktail of Tityus bahiensis scorpion

Oliveira

Cândido

Dorce

et al. 2015

Toxicon

View full text Add to dashboard Cite

Scorpion venom is a mixture of peptides, including antimicrobial, bradykinin-potentiating and anionic peptides and small to medium proteins, such as ion channel toxins, metalloproteinases and phospholipases that together cause severe clinical manifestation. Tityus bahiensis is the second most medically important scorpion species in Brazil and it is widely distributed in the country with the exception of the North Region. Here we sequenced and analyzed the transcripts from the venom glands of T. bahiensis, aiming at identifying and annotating venom gland expressed genes. A total of 116,027 long reads were generated by pyrosequencing and assembled in 2891 isotigs. An annotation process identified transcripts by similarity to known toxins, revealing that putative venom components represent 7.4% of gene expression. The major toxins identified are potassium and sodium channel toxins, whereas metalloproteinases showed an unexpected high abundance. Phylogenetic analysis of deduced metalloproteinases from T. bahiensis and other scorpions revealed a pattern of ancient and intraspecific gene expansions. Other venom molecules identified include antimicrobial, anionic and bradykinin-potentiating peptides, besides several putative new venom components. This report provides the first attempt to massively identify the venom components of this species and constitutes one of the few transcriptomic efforts on the genus Tityus.

show abstract

Section: Other Putative Venom Componentsmentioning

confidence: 96%

Section: Other Putative Venom Componentsmentioning

confidence: 98%

The transcriptome recipe for the venom cocktail of Tityus bahiensis scorpion

Oliveira

Cândido

Dorce

et al. 2015

Toxicon

View full text Add to dashboard Cite

show abstract

“…The presence of two proline residues at the C-terminal portion was noteworthy, as shown in classic BPPs (92) …”

Section: Ferreira Et Al (91) Isolated and Characterized A Peptmentioning

confidence: 95%

Some arachnidan peptides with potential medical application

Lima¹,

Borges²,

Verano‐Braga³

et al. 2010

J. Venom. Anim. Toxins incl. Trop. Dis

View full text Add to dashboard Cite

ABSTRACT:The search for new active drugs that can alleviate or cure different diseases is a constant challenge to researchers in the biological area and to the pharmaceutical industry. Historically, research has focused on the study of substances from plants. More recently, however, animal venoms have been attracting attention and studies have been successful in addressing treatment of accidents. Furthermore, venoms and their toxins have been considered good tools for prospecting for new active drugs or models for new therapeutic drugs. In this review, we discuss some possibilities of using different toxins, especially those from arachnid venoms, which have shown some potential application in diseases involving pain, hypertension, epilepsy and erectile dysfunction. A new generation of drugs is likely to emerge from peptides, including those found in animal venoms.

show abstract

“…These disulfide bridged peptides interact with Na + and K + channels (see [9] for review). The TsV also contains small and linear molecules without disulfide-bridges such as hypotensins, antimicrobial and hemolytic peptides, as well as immuno-modulating and hormone-like peptides [10][11][12][13]. The scientific community has shown an increasing interest in the study of such small peptides present in animal venoms because of their evolutionarily preserved characteristics, which point to the existence of important functional targets (see [14] for a review).…”

Section: Introductionmentioning

confidence: 98%