Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm

• DOI: 10.1371/journal.pone.0258052
• Publication Date: 2021-10-11T17:45:02Z
• Authors: Jean-Louis Kouadio; Stephen Duff; Michael Aikins; Meiying Zheng; Timothy Rydel; Danqi Chen; Eric Bretsnyder; Chunsheng Xia; Jun Zhang; Jason Milligan; Artem Evdokimov; Jeffrey Nageotte; Yong Yin; William Moar; Kara Giddings; Yoonseong Park; Agoston Jerga; Jeffrey Haas
• Keywords: Western corn rootworm; Bacillus thuringiensis; Genetically modified maize; Alanine

The western corn rootworm (WCR), Diabrotica virgifera LeConte, is a major pest of significant economic importance in the United States. continuous need to control this maize and development field-evolved resistance toward all existing transgenic ( Zea mays L.) expressing Bacillus thuringiensis Bt ) insecticidal proteins against WCR has prompted new insect-protected crops distinct structural classes proteins. In current study, we describe crystal structure functional characterization Mpp75Aa1.1, which represents first (CRW) active protein member ETX_MTX2 sub-family beta-pore forming (β-PFPs), provides effective protection feeding. Mpp75Aa1.1 was solved at 1.94 Å resolution. processed its carboxyl-terminus by midgut proteases, forms an oligomer, specifically interacts with putative membrane-associated binding partners on apical microvilli cause cellular tissue damage resulting insect death. Alanine substitution surface-exposed amino acids W206, Y212, G217 within receptor domain I demonstrates that least these three are required for activity. distinctive spatial arrangement suggests they part epitope, may be unique not present other do have Overall, work establishes shares mode action consistent traditional WCR-active despite differences.