Structure and in vitro activities of a Copper II-chelating anionic peptide from the venom of the scorpion Tityus stigmurus

Melo, Menilla Maria Alves de; Daniele-Silva, Alessandra; Teixeira, Diego Gomes; Estrela, Andréia Bergamo; Melo, Karolline R.T.; Oliveira, Verônica S.; Rocha, Hugo Alexandre Oliveira; Ferreira, Leandro de Santis; Pontes, Daniel L.; Lima, J. A. S.; Silva-Júnior, Arnóbio Antônio da; Barbosa, Euzébio Guimarães; Carvalho, Enéas; Fernandes-Pedrosa, Matheus de Freitas

doi:10.1016/j.peptides.2017.05.009

Cited by 15 publications

(15 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…A transcript for a putative anionic HDP without disulfide bridges is also reported. CliHDPAni01 shows similarities to the genome-derived sequence XP_023227050 from C. sculpturatus , and with TanP (GeneBank ID of the transcript: JK483720), a peptide isolated from the venom of Tityus stigmurus [67]. The predicted precursors translated from these sequences, are shown aligned in Figure 5D.…”

Section: Resultsmentioning

confidence: 99%

Dissecting Toxicity: The Venom Gland Transcriptome and the Venom Proteome of the Highly Venomous Scorpion Centruroides limpidus (Karsch, 1879)

Cid-Uribe

Meneses

Batista

et al. 2019

Toxins

View full text Add to dashboard Cite

Venom glands and soluble venom from the Mexican scorpion Centruroides limpidus (Karsch, 1879) were used for transcriptomic and proteomic analyses, respectively. An RNA-seq was performed by high-throughput sequencing with the Illumina platform. Approximately 80 million reads were obtained and assembled into 198,662 putative transcripts, of which 11,058 were annotated by similarity to sequences from available databases. A total of 192 venom-related sequences were identified, including Na+ and K+ channel-acting toxins, enzymes, host defense peptides, and other venom components. The most diverse transcripts were those potentially coding for ion channel-acting toxins, mainly those active on Na+ channels (NaScTx). Sequences corresponding to β- scorpion toxins active of K+ channels (KScTx) and λ-KScTx are here reported for the first time for a scorpion of the genus Centruroides. Mass fingerprint corroborated that NaScTx are the most abundant components in this venom. Liquid chromatography coupled to mass spectometry (LC-MS/MS) allowed the identification of 46 peptides matching sequences encoded in the transcriptome, confirming their expression in the venom. This study corroborates that, in the venom of toxic buthid scorpions, the more abundant and diverse components are ion channel-acting toxins, mainly NaScTx, while they lack the HDP diversity previously demonstrated for the non-buthid scorpions. The highly abundant and diverse antareases explain the pancreatitis observed after envenomation by this species.

show abstract

Section: Resultsmentioning

confidence: 99%

Dissecting Toxicity: The Venom Gland Transcriptome and the Venom Proteome of the Highly Venomous Scorpion Centruroides limpidus (Karsch, 1879)

Cid-Uribe

Meneses

Batista

et al. 2019

Toxins

View full text Add to dashboard Cite

show abstract

“…Its closest match in terms of sequence similarity was Hta1 (55% identity), from a transcriptome analysis of Hadogenes troglodytes . Highly anionic peptides of this kind have been previously found in scorpions [ 55 , 56 ], and in other phyla. They are integral part of the host defense systems of vertebrates, invertebrates and plants [ 57 ].…”

Section: Resultsmentioning

confidence: 99%

A Deeper Examination of Thorellius atrox Scorpion Venom Components with Omic Technologies

Romero-Gutiérrez

Peguero-Sanchez

Cevallos

et al. 2017

Toxins

View full text Add to dashboard Cite

This communication reports a further examination of venom gland transcripts and venom composition of the Mexican scorpion Thorellius atrox using RNA-seq and tandem mass spectrometry. The RNA-seq, which was performed with the Illumina protocol, yielded more than 20,000 assembled transcripts. Following a database search and annotation strategy, 160 transcripts were identified, potentially coding for venom components. A novel sequence was identified that potentially codes for a peptide with similarity to spider ω-agatoxins, which act on voltage-gated calcium channels, not known before to exist in scorpion venoms. Analogous transcripts were found in other scorpion species. They could represent members of a new scorpion toxin family, here named omegascorpins. The mass fingerprint by LC-MS identified 135 individual venom components, five of which matched with the theoretical masses of putative peptides translated from the transcriptome. The LC-MS/MS de novo sequencing allowed to reconstruct and identify 42 proteins encoded by assembled transcripts, thus validating the transcriptome analysis. Earlier studies conducted with this scorpion venom permitted the identification of only twenty putative venom components. The present work performed with more powerful and modern omic technologies demonstrates the capacity of accomplishing a deeper characterization of scorpion venom components and the identification of novel molecules with potential applications in biomedicine and the study of ion channel physiology.

show abstract

“…The ability to chelate the copper ion from the extracts was determined by the method described by Melo et al [74]. Pyrocatechol violet, the reagent used in this assay, can associate with certain cations, such as aluminum, copper, bismuth and thorium.…”

Section: Methodsmentioning

confidence: 99%

Gallic Acid-Chitosan Conjugate Inhibits the Formation of Calcium Oxalate Crystals

et al. 2019

View full text Add to dashboard Cite

It has recently been shown that chitosan (Chit) induces the formation of calcium oxalate (CaOx) crystals, which are mainly responsible for the appearance of kidney stones, and this might limit the use of Chit in vivo. Here, Chit was conjugated with gallic acid (Chit-Gal) to decrease the formation of CaOx crystal. This conjugation was confirmed by FTIR and NMR analyses. Chit-Gal contains 10.2 ± 1.5 mg GA per g of Chit. Compared to the control group, Chit increased the number of crystals by six-fold, mainly in the number of monohydrated CaOx crystals, which are the most harmful CaOx crystals. In addition, Chit increased the zeta potential (ζ) of CaOx crystals by three-fold, indicating that Chit was associated with the crystals. These alterations were abolished when Chit-gal was used in these tests. As oxidative stress is related to renal calculus formation, Chit and Chit-Gal were also evaluated as antioxidants using total antioxidant Capacity (TAC), reducing power, ferrous chelation, and copper chelation tests. Chit-gal was more efficient antioxidant agent in TAC (2 times), in ferrous chelation (90 times), and in reducing Power (5 times) than Chit. Overall, Chit-gal has higher antioxidant activity than Chit, does not induce the formation of CaOx crystals. Thus, Chit-Gal has potential to be used as a chit substitute.

show abstract

Structure and in vitro activities of a Copper II-chelating anionic peptide from the venom of the scorpion Tityus stigmurus

Cited by 15 publications

References 53 publications

Dissecting Toxicity: The Venom Gland Transcriptome and the Venom Proteome of the Highly Venomous Scorpion Centruroides limpidus (Karsch, 1879)

Dissecting Toxicity: The Venom Gland Transcriptome and the Venom Proteome of the Highly Venomous Scorpion Centruroides limpidus (Karsch, 1879)

A Deeper Examination of Thorellius atrox Scorpion Venom Components with Omic Technologies

Gallic Acid-Chitosan Conjugate Inhibits the Formation of Calcium Oxalate Crystals

Contact Info

Product

Resources

About