New proposal for the systematic nomenclature of scorpion peptides.

The systematic annotation of novel peptides found in the venom of scorpions needs revision. The commonly used two-letter acronym with the initials of the genus and the species is not discriminative and induces confusion. A new universal five-letter abbreviated code is here proposed.

Toxic Peptides from the Mexican Scorpion : Chemical Structure and Evaluation of Recognition by Human Single-Chain Antibodies.

Alternative recombinant sources of antivenoms have been successfully generated. The application of such strategies requires the characterization of the venoms for the development of specific neutralizing molecules against the toxic components. Five toxic peptides to mammals from the Mexican scorpion were isolated by chromatographic procedures by means of gel filtration on Sephadex G-50, followed by ion-exchange columns on carboxy-methyl-cellulose (CMC) resins and finally purified by high-performance chromatography (HPLC) columns.

Neutralization of Centruroides tecomanus scorpion venom by the use of two human recombinant antibody fragments.

The first toxic component identified against mammals in the venom from Centruroides tecomanus scorpion from Colima, Mexico was Ct1a toxin, which was neutralized by human single chain variable fragment (scFv) RAS27. Venom characterization from these scorpions collected on the Pacific coast of Colima, enabled the identification of a second component of medical importance named Ct71 toxin. Amino acid sequence of Ct71 shares a high identity with Chui5 toxin from C.

Of Seven New K Channel Inhibitor Peptides of , α-KTx 2.24 Has a Picomolar Affinity for Kv1.2.

Seven new peptides denominated CboK1 to CboK7 were isolated from the venom of the Mexican scorpion and their primary structures were determined. The molecular weights ranged between 3760.4 Da and 4357.

Indolealkylamines in the venom of the scorpion Thorellius intrepidus.

Scorpions are a group of arthropods that strike fear in many people due to their severe medical symptoms, even death, caused by their venomous stings. Even so, not all scorpion species contain harmful venoms against humans but still have valuable bioactive molecules, which could be used in developing new pharmaceutical leads for treating important diseases. This work conducted a comprehensive analysis of the venom from the scorpion Thorellius intrepidus.

A proteomic overview of the major venom components from Tityus championi from Panama.

In recent years, morbidity caused by scorpion sting of the species Tityus championi has increased in Panama. Therefore, the LD was determined by intravenous injection in 2.9 mg/kg and the venom of T.

Development of a human antibody fragment cross-neutralizing scorpion toxins.

Previously, it was demonstrated that from the single chain fragment variable (scFv) 3F it is possible to generate variants capable of neutralizing the Cn2 and Css2 toxins, as well as their respective venoms (Centruroides noxius and Centruroides suffusus). Despite this success, it has not been easy to modify the recognition of this family of scFvs toward other dangerous scorpion toxins. The analysis of toxin-scFv interactions and in vitro maturation strategies allowed us to propose a new maturation pathway for scFv 3F to broaden recognition toward other Mexican scorpion toxins.

Characterization and Chemical Synthesis of Cm39 (α-KTx 4.8): A Scorpion Toxin That Inhibits Voltage-Gated K Channel K1.2 and Small- and Intermediate-Conductance Ca-Activated K Channels K2.2 and K3.1.

A novel peptide, Cm39, was identified in the venom of the scorpion . Its primary structure was determined. It consists of 37 amino acid residues with a MW of 3980.

Expression in Pichia pastoris of human antibody fragments that neutralize venoms of Mexican scorpions.

The methylotrophic yeast Pichia pastoris has been one of the most widely used organisms in recent years as an expression system for a wide variety of recombinant proteins with therapeutic potential. Its popularity as an alternative system to Escherichia coli is mainly due to the easy genetic manipulation and the ability to produce high levels of heterologous proteins, either intracellularly or extracellularly. Being a eukaryotic organism, P.

Structural and functional studies of scorpine: A channel blocker and cytolytic peptide.

Scorpine is an antimicrobial and antimalarial peptide isolated from Pandinus imperator scorpion venom. As there are few functional and structural studies reported on scorpine-like peptides, we investigated the recombinant truncated N- and C-terminal domains as well as complete scorpine using biological assays and determined the N- and C-terminal structures using solution nuclear magnetic resonance. The study was conducted using recombinant N- and C-terminal peptides and complete scorpine expressed in Escherichia coli.

Flow cytometry analysis of CD11c-positive peripheral blood mononuclear cells in horses.

Horses have played a prominent role in shaping our modern world, with important effects on health. Unfortunately, better characterization of the horse immune system is still needed. In this report, using flow cytometry techniques, four monoclonal antibodies against horse CD11c integrin were characterized and described for their ability to provide a positive recognition signal in peripheral blood mononuclear cells.

The Ca Channel Blocker Verapamil Inhibits the In Vitro Activation and Function of T Lymphocytes: A 2022 Reappraisal.

Ca channel blockers (CCBs) are commonly used to treat different cardiovascular conditions. These drugs disrupt the intracellular Ca signaling network, inhibiting numerous cellular functions in different cells, including T lymphocytes. We explored the effect of the CCB verapamil on normal human peripheral blood T cell activation, proliferation, and cytokine production.

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

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.

Cm28, a scorpion toxin having a unique primary structure, inhibits KV1.2 and KV1.3 with high affinity.

The Cm28 in the venom of Centruroides margaritatus is a short peptide consisting of 27 amino acid residues with a mol wt of 2,820 D. Cm28 has <40% similarity with other known α-KTx from scorpions and lacks the typical functional dyad (lysine-tyrosine) required to block KV channels. However, its unique sequence contains the three disulfide-bond traits of the α-KTx scorpion toxin family.

sVmKTx, a transcriptome analysis-based synthetic peptide analogue of Vm24, inhibits Kv1.3 channels of human T cells with improved selectivity.

Kv1.3 K channels play a central role in the regulation of T cell activation and Ca signaling under physiological and pathophysiological conditions. Peptide toxins targeting Kv1.

Heterologous expression of four recombinant toxins from Panamanian scorpions of the genus and for production of antivenom.

Background: The development of more effective antivenoms remains a necessity for countries where scorpionism is a public health problem. Also, the regionalization of antivenoms may be important for some countries with special scorpionism characteristics.

Objective: Production of antibodies capable of neutralizing the lethal effect of the venom of three scorpion species from Panama.

Full Neutralization of Scorpion Venom by Combining Two Human Antibody Fragments.

A fundamental issue of the characterization of single-chain variable fragments (scFvs), capable of neutralizing scorpion toxins, is their cross-neutralizing ability. This aspect is very important in Mexico because all scorpions dangerous to humans belong to the genus, where toxin sequences show high identity. Among toxin-neutralizing antibodies that were generated in a previous study, scFv 10FG2 showed a broad cross-reactivity against several toxins, while the one of scFv LR is more limited.

Colombian Scorpion : Purification and Characterization of a Gamma Potassium Toxin with Full-Block Activity on the hERG1 Channel.

The Colombian scorpion produces a venom considered of low toxicity. Nevertheless, there are known cases of envenomation resulting in cardiovascular disorders, probably due to venom components that target ion channels. Among them, the gene (hERG1) potassium channels are critical for cardiac action potential repolarization and alteration in its functionality are associated with cardiac disorders.

Structural and functional characterization of NDBP-4 family antimicrobial peptides from the scorpion Mesomexovis variegatus.

Six peptides, belonging to the NDBP-4 family of scorpion antimicrobial peptides were structurally and functionally characterized. The sequence of the mature peptides VpCT1, VpCT2, VpCT3 and VpCT4 was inferred by transcriptomic analysis of the venom gland of the scorpion Mesomexovis variegatus. Analysis of their amino acid sequences revealed patterns that are also present in previously reported peptides that show differences in their hemolytic and antimicrobial activities in vitro.

Antiseizure potential of peptides from the venom of social wasp Chartergellus communis against chemically-induced seizures.

Epilepsy is one of the most common neurological diseases in the world. The objective of this research was to investigate a new peptide from the venom of the social wasp Chartergellus communis useful to the study or pharmacotherapy of epilepsy. The wasps were collected, and their venom was extracted.

Head-to-Tail Cyclization after Interaction with Trypsin: A Scorpion Venom Peptide that Resembles Plant Cyclotides.

Peptidase inhibitors (PIs) have been broadly studied due to their wide therapeutic potential for human diseases. A potent trypsin inhibitor from scorpion venom was characterized and named ToPI1, with 33 amino acid residues and three disulfide bonds. The X-ray structure of the ToPI1:trypsin complex, in association with the mass spectrometry data, indicate a sequential set of events: the complex formation with the inhibitor Lys in the trypsin S1 pocket, the inhibitor C-terminal residue Ser cleavage, and the cyclization of ToPI1 via a peptide bond between residues Ile and Lys.