Successful refolding and NMR structure of rMagi3: A disulfide‐rich insecticidal spider toxin

• Published in: Protein science 2018-03, Vol.27 (3), p.692-701
• Main Authors: Titaux‐Delgado, Gustavo, Carrillo, Elisa, Mendoza, Angeles, Mayorga‐Flores, Marlen, Escobedo‐González, Fátima C., Cano‐Sánchez, Patricia, López‐Vera, Estuardo, Corzo, Gerardo, del Rio‐Portilla, Federico
• Format: Article
• Language: English
• Subjects: Amino acid sequence; Animals; Biological activity; Biological effects; Chromatography; Disulfides - chemistry; insecticidal; Insecticides - chemistry; Insecticides - isolation & purification; Insects; Macrothele gigas; Magnetic Resonance Spectroscopy; Mice; Models, Molecular; Molecular biology; NMR; NMR solution structure; Nuclear magnetic resonance; Predators; Protein Conformation; Purification; refolding disulfide‐bonded toxins; spider toxin; Spider Venoms - chemistry; Spider Venoms - isolation & purification; Spiders; Spiders - metabolism; Toxins
• ISSN: 0961-8368; 1469-896X
• DOI: 10.1002/pro.3363

The need for molecules with high specificity against noxious insects leads the search towards spider venoms that have evolved highly selective toxins for insect preys. In this respect, spiders as a highly diversified group of almost exclusive insect predators appear to possess infinite potential for the discovery of novel insect‐selective toxins. In 2003, a group of toxins was isolated from the spider Macrothele gigas and the amino acid sequence was reported. We obtained, by molecular biology techniques in a heterologous system, one of these toxins. Purification process was optimized by chromatographic methods to determine the three‐dimensional structure by nuclear magnetic resonance in solution, and, finally, their biological activity was tested. rMagi3 resulted to be a specific insect toxin with no effect on mice. PDB Code(s): 6AX2