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Original article
Yu-Jing Zhu
Fujian Academy of Agricultural Sciences
Corresponding Author
ORCiD: https://orcid.org/0000-0002-0045-6708
License:
This work is licensed under a CC BY 4.0 License. Read Full License
As a pore-forming toxin, oligomerization and pore-formation were both required for the mode of action of Cry toxins. Previous studies revealed that Domain I helices α4-α5 were involved in oligomerization of Cry2Ab, while the active residues in charge of Cry2Ab aggregation remained ambiguous. In present studies, we built 20 Cry2Ab alanine mutants site directed in helices α4-α5 and demonstrated that mutants N151A, T152A, F157A, L183A, L185A and I188A blocked the assembly of 250 kDa oligomers, suggesting that those residues were key residues for Cry2Ab oligomerization. As expected, those variants severely reduced the insecticidal activity against P. xylostella which was similar to our previous reports. Furthermore, we found that the pore-forming activities of non-oligomerization mutants sharply decreased compared to wild-type Cry2Ab. Taken together, our data comprehensively identified key residues for Cry2Ab for the first time and emphasized that oligomerization was closely related to insecticidal activity and pore-forming activity in Cry2Ab.
Keywords
Cry2Ab, oligomerization, insecticidal activity, pore-forming activity.
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View the published article at AMB Express.
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Received 28 May, 2021
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On 16 May, 2021
Review #2 received
Received 16 May, 2021
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Received 14 May, 2021
Reviewers invited
Invitations sent on 14 May, 2021
Reviewer #1 agreed
On 13 May, 2021
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On 10 May, 2021
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A new preprint design is coming!
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See the published version of this preprint at AMB Express.
This is a preprint, a preliminary version of a manuscript that has not completed peer review at a journal. Research Square does not conduct peer review prior to posting preprints. The posting of a preprint on this server should not be interpreted as an endorsement of its validity or suitability for dissemination as established information or for guiding clinical practice.
Learn more about In Review
Original article
Yu-Jing Zhu
Fujian Academy of Agricultural Sciences
Corresponding Author
ORCiD: https://orcid.org/0000-0002-0045-6708
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
Peer Review Timeline
CURRENT STATUS: Published
View the published article at AMB Express.
Version 1
Posted 13 May, 2021
No community comments so far
Review #1 received
Received 28 May, 2021
Editorial decision: Major Revision
On 28 May, 2021
Reviewer #2 agreed
On 16 May, 2021
Review #2 received
Received 16 May, 2021
Reviews received
Received 14 May, 2021
Reviewers invited
Invitations sent on 14 May, 2021
Reviewer #1 agreed
On 13 May, 2021
Editor assigned
On 10 May, 2021
Submission checks complete
On 10 May, 2021
Editor invited
On 10 May, 2021
First submitted
On 09 May, 2021
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
View the published article at AMB Express.
As a pore-forming toxin, oligomerization and pore-formation were both required for the mode of action of Cry toxins. Previous studies revealed that Domain I helices α4-α5 were involved in oligomerization of Cry2Ab, while the active residues in charge of Cry2Ab aggregation remained ambiguous. In present studies, we built 20 Cry2Ab alanine mutants site directed in helices α4-α5 and demonstrated that mutants N151A, T152A, F157A, L183A, L185A and I188A blocked the assembly of 250 kDa oligomers, suggesting that those residues were key residues for Cry2Ab oligomerization. As expected, those variants severely reduced the insecticidal activity against P. xylostella which was similar to our previous reports. Furthermore, we found that the pore-forming activities of non-oligomerization mutants sharply decreased compared to wild-type Cry2Ab. Taken together, our data comprehensively identified key residues for Cry2Ab for the first time and emphasized that oligomerization was closely related to insecticidal activity and pore-forming activity in Cry2Ab.
Figure 1
Figure 2
Figure 3
Figure 4
Figure 5
This is a list of supplementary files associated with this preprint. Click to download.
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