Molecular architecture and activation of the insecticidal protein Vip3Aa from Bacillus thuringiensis

Journal: Nature Communications

Published: 2020-08-07

DOI: 10.1038/s41467-020-17758-5

Affiliations: 5

Authors: 6

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Research Highlight

Shape-shifting insecticide

© Sandro Balbuena/EyeEm/Getty Images

© Sandro Balbuena/EyeEm/Getty Images

An analysis of the structure of an insect-killing protein produced by soil-dwelling microbes could lead new pest-control strategies for the agriculture industry.

The bacterium Bacillus thuringiensis secretes the insecticidal protein Vip3Aa, which is effective against many butterflies and moths. The protein is used as a pesticide to protect crops from pests. It gets converted into a toxic, insecticidal form when ingested by butterflies or moths but beyond that its mechanism is unknown.

Now, a team led by scientists from the Spanish National Research Council has used cryo-electron microscopy to detail the molecular architecture of Vip3Aa.

They found that the inactive ‘pre-toxin’ consists of four parts arranged in a pyramidal shape. Enzymes found in insect guts then cleave part of the protein, transforming it into its active structure.

The high-resolution structural information and insights into the activation mechanism of Vip3Aa should help biotechnology companies to engineer new insecticidal proteins that have greater stability and potency.

Supported content

  1. Nature Communications 11, 3974 (2020). doi: 10.1038/s41467-020-17758-5
Institutions Share
University of Valencia (UV), Spain 0.61
Centre for Biological Research (CIB), CSIC, Spain 0.33
Biomedical Research Networking Center on Rare Diseases (CIBERER), Spain 0.06

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