Recombinant expression of the toxic peptide ErgTx1 and role of Met35 on its stability and function

  title={Recombinant expression of the toxic peptide ErgTx1 and role of Met35 on its stability and function},
  author={Juana Mar{\'i}a Jim{\'e}nez-Vargas and Rita Restano-Cassulini and Ver{\'o}nica Quintero-Hern{\'a}ndez and Georgina B. Gurrola and Lourival Domingos Possani},

Interacting sites of scorpion toxin ErgTx1 with hERG1 K+ channels.

Positive selection-guided mutational analysis revealing two key functional sites of scorpion ERG K(+) channel toxins.

Antivenom Derived from the Ct1a and Ct17 Recombinant Toxins of the Scorpion Centruroides tecomanus

This communication reveals the possibility of producing a specific and regional antivenom with polyclonal antibodies that neutralize the complete venom of Centruroides tecomanus and remarkably, the recombinant toxins were excellent immunogens.

Toxin modulators and blockers of hERG K(+) channels.

Microbial production of toxins from the scorpion venom: properties and applications

The most used microbial system in the heterologous expression of scorpion venom components is Escherichia coli (85%), and among all the recombinant venom components produced, 69% were neurotoxins.

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

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.

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

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.

Scorpion and spider venom peptides: gene cloning and peptide expression.



Mapping the Binding Site of a Humanether-a-go-go-related Gene-specific Peptide Toxin (ErgTx) to the Channel's Outer Vestibule*

This study proposes that the long S5-P linker of the HERG channel forms an amphipathic α-helix that, together with the P-S6 linker, forms a hydrophobic ErgTx binding site, which paves the way for future mutant cycle analysis of interacting residues in the Ergtx·HERG complex, which will yield information about the topology of HERG's outer vestibule.

A toxin to nervous, cardiac, and endocrine ERG K+ channels isolated from Centruroides noxius scorpion venom

  • G. GurrolaB. Rosati E. Wanke
  • Biology
    FASEB journal : official publication of the Federation of American Societies for Experimental Biology
  • 1999
This work isolated a peptide from the scorpion Centruroides noxius Hoffmann that has no sequence homologies with other toxins, and demonstrates that it specifically inhibits (IC50 = 16±1 nM) only ERG channels of different species and distinct histogenesis.

Structural and functional features of noxiustoxin: a K+ channel blocker.

Binding of [125I]-Noxiustoxin to rat brain synaptosome membranes and displacement with synthetic peptides corresponding to the amino acid sequence of Noxiustoxin, show that the N-terminal segment of

Structural and Functional Role of the Extracellular S5-P Linker in the HERG Potassium Channel

A structural model for the outer vestibule of the HERG channel is proposed, in which the 583–597 segment forms an α-helix, that may make important contribution to the unique C-type inactivation phenotype.

Scorpion toxins specific for Na+-channels.

A classification containing 10 different groups of toxins is proposed in this review, based on functional and structural features of the known toxins, and the limited success obtained in the search for the site through which these peptides bind to the channels.

Oxidation of Methionine Residues in Antithrombin

Structural studies indicate that highly oxidized AT is less able to undergo the complete conformational change induced by heparin, most probably due to oxidation of Met17, and oxidation does not appear to be a means of controlling AT activity.

Mutant potassium channels with altered binding of charybdotoxin, a pore-blocking peptide inhibitor.

The inhibition by charybdotoxin of A-type potassium channels expressed in Xenopus oocytes was studied for several splicing variants of the Drosophila Shaker gene and for several site-directed mutants

Nonessential role for methionines in the productive association between calmodulin and the plasma membrane Ca-ATPase.

Calculation of the binding affinities of individual CaM domains associated with activation of the PM-Ca-ATPase suggests that mutations of methionines located in either domain of CaM can decrease the initial high-affinity association between CaM and the PM, but have little effect upon the subsequent binding of the opposing globular domain.

In Vitro Methionine Oxidation of Recombinant Human Leptin

Investigation of the role and importance of the four methionines in recombinant human leptin, and the effect of methionine oxidation in leptin structural stability and biological activity found that Met69, but not Met1, plays a critical role in the protein stability and activity.