A novel insecticidal spider peptide that affects the mammalian voltage-gated ion channel hkv1.5
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, thi...
- Autores:
-
Corrales García, Ligia Luz
Clement Carretero, Herlinda
Corzo Burguete, Gerardo
Alvarado, Diana
Cardoso Arenas, Samuel
Arenas, Iván
Montero Domínguez, Pavel Andrei
Olamendi Portugal, Timoteo
Zamudio, Fernando
Csoti, Agota
Borrego, Jesús
Panyi, Gyorgy
Papp, Ferenc
- Tipo de recurso:
- Article of investigation
- Fecha de publicación:
- 2021
- Institución:
- Universidad de Antioquia
- Repositorio:
- Repositorio UdeA
- Idioma:
- eng
- OAI Identifier:
- oai:bibliotecadigital.udea.edu.co:10495/38819
- Acceso en línea:
- https://hdl.handle.net/10495/38819
- Palabra clave:
- Fibrilación Atrial
Atrial Fibrillation
Canal de Potasio Kv1.5
Kv1.5 Potassium Channel
Venenos de Araña
Spider Venoms
Oculicosa supermirabilis
Recombinant expression
https://id.nlm.nih.gov/mesh/D001281
https://id.nlm.nih.gov/mesh/D051666
https://id.nlm.nih.gov/mesh/D013111
- Rights
- openAccess
- License
- http://creativecommons.org/licenses/by/2.5/co/
| Summary: | 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. |
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