Structure–function characterization of an insecticidal protein GNIP1Aa, a member of an MACPF and β-tripod families
Author(s) -
Jelena Zaitseva,
Daniel Vaknin,
Christian F. Krebs,
James R. Doroghazi,
Sara L. Milam,
Deepa Balasubramanian,
Nicholas B. Duck,
Joerg Freigang
Publication year - 2019
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.1815547116
Subject(s) - biology , protein family , protein domain , peptide sequence , protein structure , sequence alignment , genetics , biochemistry , gene
Significance GNIP1Aa is a protein fromChromobacterium piscinae that demonstrates specific toxicity toward Western corn rootworm, one of the most devastating corn pests in the United States. Our studies provide insight into the GNIP1Aa structure and place this protein into an insecticidal protein class, membrane attack complex/PerForin–β-tripod, different from all insect-control products of modern agricultural technology available on the market. Protein activity and uniqueness make GNIP1Aa an excellent commercial candidate for development into a transgenic product. Such a product might have a high potential to combat crop damage in corn and to delay development of resistance in insects. Our work also contributes to the general understanding of the mechanism of action of pore-forming proteins and their target specificity.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom