Journal article
Structural and biophysical characterization of Bacillus thuringiensis insecticidal proteins Cry34Ab1 and Cry35Ab1
PLoS One, Vol.9(11)
2014
Abstract
Bacillus thuringiensis strains are well known for the production of insecticidal proteins upon sporulation and these proteins are deposited in parasporal crystalline inclusions. The majority of these insect-specific toxins exhibit three domains in the mature toxin sequence. However, other Cry toxins are structurally and evolutionarily unrelated to this three-domain family and little is known of their three dimensional structures, limiting our understanding of their mechanisms of action and our ability to engineer the proteins to enhance their function. Among the non-three domain Cry toxins, the Cry34Ab1 and Cry35Ab1 proteins from B. thuringiensis strain PS149B1 are required to act together to produce toxicity to the western corn rootworm (WCR) Diabrotica virgifera virgifera Le Conte via a pore forming mechanism of action. Cry34Ab1 is a protein of 14 kDa with features of the aegerolysin family (Pfam06355) of proteins that have known membrane disrupting activity, while Cry35Ab1 is a44 kDa member of the toxin-10 family (Pfam05431) that includes other insecticidal proteins such as the binary toxin BinA/BinB. The Cry34Ab1/Cry35Ab1 proteins represent an important seed trait technology having been developed as insect resistance traits in commercialized corn hybrids for control of WCR. The structures of Cry34Ab1 and Cry35Ab1 have been elucidated to 2.15 A° and 1.80 A° resolution, respectively. The solution structures of the toxins were further studied by small angle X-ray scattering and native electrospray ion mobility mass spectrometry. We present here the first published structure from the aegerolysin protein domain family and the structural comparisons of Cry34Ab1 and Cry35Ab1 with other pore forming toxins. © 2014 Kelker et al.
Details
- Title
- Structural and biophysical characterization of Bacillus thuringiensis insecticidal proteins Cry34Ab1 and Cry35Ab1
- Authors
- Matthew S Kelker (Author) - Dow AgroSciences, United StatesColin Berry (Author) - Cardiff University, United KingdomSteven L Evans (Author) - Dow AgroSciences, United StatesReetal Pai (Author) - Dow AgroSciences, United StatesDavid G McCaskill (Author) - Dow AgroSciences, United StatesNick X Wang (Author) - Dow AgroSciences, United StatesJoshua C Russell (Author) - University of Washington, United StatesMatthew D Baker (Author) - Cardiff UniversityCheng Yang (Author) - Rigaku Americas Corporation, United StatesJ W Pflugrath (Author) - Rigaku Americas Corporation, United StatesMatthew Wade (Author) - Cardiff University, United KingdomTim J Wess (Author) - Charles Sturt UniversityKenneth E Narva (Author) - Dow AgroSciences, United States
- Publication details
- PLoS One, Vol.9(11)
- Publisher
- Public Library of Science
- Date published
- 2014
- DOI
- 10.1371/journal.pone.0112555
- ISSN
- 1932-6203
- Copyright note
- Copyright © 2014 Kelker et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
- Organisation Unit
- Office of the Deputy Vice-Chancellor (Academic); University of the Sunshine Coast, Queensland
- Language
- English
- Record Identifier
- 99451248902621
- Output Type
- Journal article
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