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Synergistic activity between Bacillus thuringiensis Cry6Aa and Cry55Aa toxins against Meloidogyne incognita.

Peng D, Chai L, Wang F, Zhang F, Ruan L, Sun M - Microb Biotechnol (2011)

Bottom Line: Plant-parasitic nematodes are the most destructive group of plant pathogens worldwide and are extremely challenging to control.Furthermore, ligand blot analyses of the interaction between total proteins of M. incognita and the three toxins showed many different signal bands, indicating that there is a range of host proteins with which the toxins can interact.Our discovery provides an effective strategy for controlling M. incognita by using a combination of Cry6Aa and Cry55Aa.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.

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Related in: MedlinePlus

Analysis of the interaction between total proteins of M. incognita and nematicidal toxins Cry5Ba (lane 1), Cry6Aa (lane 2) and Cry55Aa (lane 3). The ability of Cry toxins to bind to M. incognita is shown on a nitrocellulose membrane and detected by antibodies against the respective toxin.
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f1: Analysis of the interaction between total proteins of M. incognita and nematicidal toxins Cry5Ba (lane 1), Cry6Aa (lane 2) and Cry55Aa (lane 3). The ability of Cry toxins to bind to M. incognita is shown on a nitrocellulose membrane and detected by antibodies against the respective toxin.

Mentions: Protein structure analysis was used to predict the mode of action of Cry5Ba, Cry6Aa and Cry55Aa. A phylogeny of the Cry toxins that have been documented to be toxic to nematodes is shown in Fig. S1. Cry6Aa, Cry5Ba and Cry55Aa belong to three different subfamilies (Fig. S1). Of the five blocks in the N‐terminal region of crystal proteins that are conserved between most of the family, Cry1A and Cry5Ba share three blocks and Cry6Aa and Cry55Aa share none (Fig. S2). In addition, the interaction between toxins and M. incognita were analysed by ligand blotting to understand the range of host proteins with which Cry5Ba, Cry6Aa and Cry55Aa can interact. This revealed positive signal bands for all three crystal proteins, indicating that all three could bind to host proteins. However, the binding protein signal profiles were very different between Cry5Ba, Cry6Aa and Cry55Aa (Fig. 1). The different protein structures and binding patterns of the three proteins with M. incognita proteins indicates that the modes of action of Cry6Aa, Cry5Ba and Cry55Aa in targeting M. incognita may be different.


Synergistic activity between Bacillus thuringiensis Cry6Aa and Cry55Aa toxins against Meloidogyne incognita.

Peng D, Chai L, Wang F, Zhang F, Ruan L, Sun M - Microb Biotechnol (2011)

Analysis of the interaction between total proteins of M. incognita and nematicidal toxins Cry5Ba (lane 1), Cry6Aa (lane 2) and Cry55Aa (lane 3). The ability of Cry toxins to bind to M. incognita is shown on a nitrocellulose membrane and detected by antibodies against the respective toxin.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3815414&req=5

f1: Analysis of the interaction between total proteins of M. incognita and nematicidal toxins Cry5Ba (lane 1), Cry6Aa (lane 2) and Cry55Aa (lane 3). The ability of Cry toxins to bind to M. incognita is shown on a nitrocellulose membrane and detected by antibodies against the respective toxin.
Mentions: Protein structure analysis was used to predict the mode of action of Cry5Ba, Cry6Aa and Cry55Aa. A phylogeny of the Cry toxins that have been documented to be toxic to nematodes is shown in Fig. S1. Cry6Aa, Cry5Ba and Cry55Aa belong to three different subfamilies (Fig. S1). Of the five blocks in the N‐terminal region of crystal proteins that are conserved between most of the family, Cry1A and Cry5Ba share three blocks and Cry6Aa and Cry55Aa share none (Fig. S2). In addition, the interaction between toxins and M. incognita were analysed by ligand blotting to understand the range of host proteins with which Cry5Ba, Cry6Aa and Cry55Aa can interact. This revealed positive signal bands for all three crystal proteins, indicating that all three could bind to host proteins. However, the binding protein signal profiles were very different between Cry5Ba, Cry6Aa and Cry55Aa (Fig. 1). The different protein structures and binding patterns of the three proteins with M. incognita proteins indicates that the modes of action of Cry6Aa, Cry5Ba and Cry55Aa in targeting M. incognita may be different.

Bottom Line: Plant-parasitic nematodes are the most destructive group of plant pathogens worldwide and are extremely challenging to control.Furthermore, ligand blot analyses of the interaction between total proteins of M. incognita and the three toxins showed many different signal bands, indicating that there is a range of host proteins with which the toxins can interact.Our discovery provides an effective strategy for controlling M. incognita by using a combination of Cry6Aa and Cry55Aa.

View Article: PubMed Central - PubMed

Affiliation: State Key Laboratory of Agricultural Microbiology, College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.

Show MeSH
Related in: MedlinePlus