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TitleVip3C proteins from spp. for controlling lepidopteran crop pests.
Journal, issue, pagesAppl Environ Microbiol, Page e0025325, Year 2025
Publish dateJun 20, 2025
AuthorsTodd Ciche / William Moar / Aqeel Ahmad / David Bowen / Catherine Chay / Arlene Howe / Uma Kesanapalli / Jennifer Lutke / Gregory Bean / Jason Milligan / Michael Pleau / Yong Yin / Waseem Akbar / Marty Heppler / Cara Griffith / Kimberly Morrell / Katherine Dunkmann / Heather Anderson / Jeffrey Ahrens / Pacifica Sommers / E Sethe Burgie / Fred Zinnel / Meiying Zheng / James Fitzpatrick / Michael Rau / Timothy Rydel / Tommi White / David Kerns / James Roberts /
PubMed AbstractNew proteins are needed to control insects not controlled with (Bt) crops, and those evolving resistance to Bt crops. These proteins are increasingly being reported from non-Bt organisms to control ...New proteins are needed to control insects not controlled with (Bt) crops, and those evolving resistance to Bt crops. These proteins are increasingly being reported from non-Bt organisms to control Bt-resistant insects. However, these proteins mostly control the corn rootworm, spp. (Coleoptera), whereas most Bt-resistant insects are lepidopteran. We hypothesized that diversifying our search for proteins into non-Bt organisms, such as those related to used to control Japanese beetle , could yield proteins with new insecticidal activities against Lepidoptera. Here, we identified Vip3Cb1 and Vip3Cc1 with broad lepidopteran activity, the first Vip3 proteins discovered from strains in the containing clade. Vip3Cb1 protected plants against cotton bollworm, and tobacco budworm and fall armyworm, , and Southwestern corn borer, , in cotton and maize, respectively, like commercial Vip3Aa. Distinct from Vip3Aa, Vip3Cb1 also protected maize against European corn borer, , the primary maize pest in the United States, with recent reports of resistance to Bt proteins. Consistent with previous reports, insects resistant to Vip3Aa were cross-resistant to Vip3Cb1. Cryo-electron microscopy demonstrated that Vip3Cb1 formed a pore-shaped tetramer upon proteolytic activation, in agreement with the pore-forming mechanism of action of Vip3Aa. Thus, diversifying the search beyond Bt has led to the discovery of the first Vip3 proteins from spp. with different activity spectra from Vip3Aa, providing additional tools to control pests, including those currently resistant to Bt Cry proteins.IMPORTANCENew insecticidal proteins are needed for controlling insect pests that can devastate crop yield if left uncontrolled. Diversifying our search for new insecticidal proteins in spp. resulted in the discovery of Vip3Cb1 and Vip3Cc1 insecticidal proteins active against lepidopteran crop pests. Structure and cross-resistance studies indicate overlap in the mechanism of action between Vip3Cb1 and commercial Vip3Aa. However, new activities, such as controlling European corn borer, make these proteins important new tools in the insect control toolbox.
External linksAppl Environ Microbiol / PubMed:40539778
MethodsEM (single particle)
Resolution2.61 - 3.04 Å
Structure data

47972

9efg

EMDB-47972, PDB-9efg:
VIP3Cb1 Toxin structure
Method: EM (single particle) / Resolution: 3.04 Å

47974

9efi

EMDB-47974, PDB-9efi:
VIP3Cb1 Protoxin Structure
Method: EM (single particle) / Resolution: 2.61 Å

Chemicals

ChemComp-MG:
Unknown entry

Source
  • paenibacillus popilliae (bacteria)
KeywordsTOXIN / Tetramer / Lepidopteran / Protoxin

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