Recombinant expression of Intrepicalcin from the scorpion Vaejovis intrepidus and its effect on skeletal ryanodine receptors.

ABSTRACT:

Background

Scorpion venoms contain toxins that modulate ionic channels, among which are the calcins, a small group of short, basic peptides with an Inhibitor Cystine Knot (ICK) motif that target calcium release channels/ryanodine receptors (RyRs) with high affinity and selectivity. Here we describe the heterologous expression of Intrepicalcin, identified by transcriptomic analysis of venomous glands from Vaejovis intrepidus.

Methods

Recombinant Intrepicalcin was obtained in Escherichia coli BL21-DE3 (periplasm) by fusing the Intrepicalcin gene to sequences coding for signal-peptide, thioredoxin, His-tag and enterokinase cleavage site.

Results

[³H]Ryanodine binding, used as a functional index of RyR activity, revealed that recombinant Intrepicalcin activates

SUBMITTER: Vargas-Jaimes L 

PROVIDER: S-EPMC5329131 | biostudies-literature | 2017 Apr

REPOSITORIES: biostudies-literature