Two Novel Ergtoxins, Blockers of K+-channels, Purified from the Mexican Scorpion Centruroides elegans elegans

Restano-Cassulini, Rita; Olamendi-Portugal, Timoteo; Zamudio, Fernando Z.; Becerril, Baltazar; Possani, Lourival D.

doi:10.1007/s11064-008-9634-8

Cited by 14 publications

(4 citation statements)

References 47 publications

(65 reference statements)

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“…It is also closely related to CeErgTx5, from Centruroides elegans , differing in just one amino acid. CeErgTx5 is active on mammalian ERG K + channels [46]. CliKTxGam02 is similar to CnErg1 (Q86QT3) identified in the venom of C. noxius , a peptide with activity on mammalian ERG K + channels [47].…”

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

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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.

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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

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“…These peptides were found in scorpions of the genus Centruroides, Mesobuthus and Buthus (Zeng et al, 2006; Jiménez-Vargas et al, 2012). The first peptide isolated was ErgTx1 ( C. noxius; Gurrola et al, 1999a), followed by the BeKm-1 ( B. eupeus; Korolkova et al, 2001); other 26 members of this subfamily were Ergtoxin-like peptides isolated from scorpions of the genus Centruroides (Lecchi et al, 2002; Nastainzky et al, 2002; Corona et al, 2002; Coronas et al, 2005; Restano-Cassulini et al, 2008; Jiménez-Vargas et al, 2012) and BmKKx2 (from M. martensii; Zeng et al, 2006). The γ-KTxs were described as mainly targeting hERG channels (Coronas et al, 2002).…”

Section: K+-channel Specific Scorpion Toxinsmentioning

confidence: 99%

Scorpion venom components that affect ion-channels function

Quintero-Hernández

Jiménez-Vargas

Gurrola

et al. 2013

Toxicon

226

168

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SUMMARY The number and types of venom components that affect ion-channel function are reviewed. These are the most important venom components responsible for human intoxication, deserving medical attention, often requiring the use of specific anti-venoms. Special emphasis is given to peptides that recognize Na+-, K+- and Ca++-channels of excitable cells. Knowledge generated by direct isolation of peptides from venom and components deduced from cloned genes, whose amino acid sequences are deposited into databanks are now adays in the order of 1.5 thousands, out of an estimate biodiversity closed to 300,000. Here the diversity of components is briefly reviewed with mention to specific references. Structural characteristic are discussed with examples taken from published work. The principal mechanisms of action of the three different types of peptides are also reviewed. Na+-channel specific venom components usually are modifier of the open and closing kinetic mechanisms of the ion-channels, whereas peptides affecting K+-channels are normally pore blocking agents. The Ryanodine Ca++-channel specific peptides are known for causing sub-conducting stages of the channels conductance and some were shown to be able to internalize penetrating inside the muscle cells.

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“…To identify the toxic components, the toxicity of the fractions and sub-fractions that typically contain the toxins isolated in the different chromatographic steps was evaluated in mice. It is known that the FII fraction contains the peptides that are toxic to mammals [21][22][23]. This toxic fraction was subsequently processed by ion exchange chromatography on a carboxymethylcellulose (CMC) column, obtaining 14 sub-fractions (Figure 1b).…”

Section: Characterization Of Toxic Componentsmentioning

confidence: 99%

Characterization of Four Medically Important Toxins from Centruroides huichol Scorpion Venom and Its Neutralization by a Single Recombinant Antibody Fragment

Valencia-Martínez

Olamendi-Portugal

Restano-Cassulini

et al. 2022

Toxins

Self Cite

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Centruroides huichol scorpion venom is lethal to mammals. Analysis of the venom allowed the characterization of four lethal toxins named Chui2, Chui3, Chui4, and Chui5. scFv 10FG2 recognized well all toxins except Chui5 toxin, therefore a partial neutralization of the venom was observed. Thus, scFv 10FG2 was subjected to three processes of directed evolution and phage display against Chui5 toxin until obtaining scFv HV. Interaction kinetic constants of these scFvs with the toxins were determined by surface plasmon resonance (SPR) as well as thermodynamic parameters of scFv variants bound to Chui5. In silico models allowed to analyze the molecular interactions that favor the increase in affinity. In a rescue trial, scFv HV protected 100% of the mice injected with three lethal doses 50 (LD50) of venom. Moreover, in mix-type neutralization assays, a combination of scFvs HV and 10FG2 protected 100% of mice injected with 5 LD50 of venom with moderate signs of intoxication. The ability of scFv HV to neutralize different toxins is a significant achievement, considering the diversity of the species of Mexican venomous scorpions, so this scFv is a candidate to be part of a recombinant anti-venom against scorpion stings in Mexico.

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Two Novel Ergtoxins, Blockers of K+-channels, Purified from the Mexican Scorpion Centruroides elegans elegans

Cited by 14 publications

References 47 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)

Scorpion venom components that affect ion-channels function

Characterization of Four Medically Important Toxins from Centruroides huichol Scorpion Venom and Its Neutralization by a Single Recombinant Antibody Fragment

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