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A Novel Insecticidal Spider Peptide that Affects the Mammalian Voltage-Gated Ion Channel hKv1.5
- Source :
- Frontiers in Pharmacology, Frontiers in Pharmacology, Vol 11 (2021)
- Publication Year :
- 2021
- Publisher :
- Frontiers Media S.A., 2021.
-
Abstract
- Spider venoms include various peptide toxins that modify the ion currents, mainly of excitable insect cells. Consequently, scientific research on spider venoms has revealed a broad range of peptide toxins with different pharmacological properties, even for mammal species. In this work, thirty animal venoms were screened against hKv1.5, a potential target for atrial fibrillation therapy. The whole venom of the spider Oculicosa supermirabilis, which is also insecticidal to house crickets, caused voltage-gated potassium ion channel modulation in hKv1.5. Therefore, a peptide from the spider O. supermirabilis venom, named Osu1, was identified through HPLC reverse-phase fractionation. Osu1 displayed similar biological properties as the whole venom; so, the primary sequence of Osu1 was elucidated by both of N-terminal degradation and endoproteolytic cleavage. Based on its primary structure, a gene that codifies for Osu1 was constructed de novo from protein to DNA by reverse translation. A recombinant Osu1 was expressed using a pQE30 vector inside the E. coli SHuffle expression system. recombinant Osu1 had voltage-gated potassium ion channel modulation of human hKv1.5, and it was also as insecticidal as the native toxin. Due to its novel primary structure, and hypothesized disulfide pairing motif, Osu1 may represent a new family of spider toxins.
- Subjects :
- 0301 basic medicine
Spider Venoms
Venom
Peptide
recombinant expression
complex mixtures
law.invention
03 medical and health sciences
law
Pharmacology (medical)
atrial fibrillation
Original Research
chemistry.chemical_classification
Pharmacology
Spider
Kv1.5
030102 biochemistry & molecular biology
Voltage-gated ion channel
Chemistry
spider venom
lcsh:RM1-950
Protein primary structure
Spider toxin
030104 developmental biology
lcsh:Therapeutics. Pharmacology
Biochemistry
Recombinant DNA
Oculicosa supermirabilis
Subjects
Details
- Language :
- English
- ISSN :
- 16639812
- Volume :
- 11
- Database :
- OpenAIRE
- Journal :
- Frontiers in Pharmacology
- Accession number :
- edsair.doi.dedup.....95748ce74d03c3788294158184e38226