Structural journey of an insecticidal protein against western corn rootworm

Guendalina Marini, Brad Poland, Chris Leininger, Natalya Lukoyanova, Dan Spielbauer, Jennifer K. Barry, Dan Altier, Amy Lum, Eric Scolaro, Claudia Pérez Ortega, Nasser Yalpani, Gary Sandahl, Tim Mabry, Jeffrey Klever, Timothy Nowatzki, Jian-Zhou Zhao, Amit Sethi, Adane Kassa, Virginia Crane, Albert L. Lu, Mark E. Nelson (), Narayanan Eswar (), Maya Topf () and Helen R. Saibil ()
Additional contact information
Guendalina Marini: University of London
Brad Poland: Corteva Agriscience
Chris Leininger: Corteva Agriscience
Natalya Lukoyanova: University of London
Dan Spielbauer: Corteva Agriscience
Jennifer K. Barry: Corteva Agriscience
Dan Altier: Corteva Agriscience
Amy Lum: Corteva Agriscience
Eric Scolaro: Corteva Agriscience
Claudia Pérez Ortega: Corteva Agriscience
Nasser Yalpani: Corteva Agriscience
Gary Sandahl: Corteva Agriscience
Tim Mabry: Corteva Agriscience
Jeffrey Klever: Corteva Agriscience
Timothy Nowatzki: Corteva Agriscience
Jian-Zhou Zhao: Corteva Agriscience
Amit Sethi: Corteva Agriscience
Adane Kassa: Corteva Agriscience
Virginia Crane: Corteva Agriscience
Albert L. Lu: Corteva Agriscience
Mark E. Nelson: Corteva Agriscience
Narayanan Eswar: Corteva Agriscience
Maya Topf: University of London
Helen R. Saibil: University of London

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract The broad adoption of transgenic crops has revolutionized agriculture. However, resistance to insecticidal proteins by agricultural pests poses a continuous challenge to maintaining crop productivity and new proteins are urgently needed to replace those utilized for existing transgenic traits. We identified an insecticidal membrane attack complex/perforin (MACPF) protein, Mpf2Ba1, with strong activity against the devastating coleopteran pest western corn rootworm (WCR) and a novel site of action. Using an integrative structural biology approach, we determined monomeric, pre-pore and pore structures, revealing changes between structural states at high resolution. We discovered an assembly inhibition mechanism, a molecular switch that activates pre-pore oligomerization upon gut fluid incubation and solved the highest resolution MACPF pore structure to-date. Our findings demonstrate not only the utility of Mpf2Ba1 in the development of biotechnology solutions for protecting maize from WCR to promote food security, but also uncover previously unknown mechanistic principles of bacterial MACPF assembly.

Date: 2023
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DOI: 10.1038/s41467-023-39891-7

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