Key residues of Bacillus thuringiensis Cry2Ab for oligomerization and pore-formation activity
© 2021. The Author(s)..
As a pore-forming toxin, activation, oligomerization and pore-formation were both required for the mode of action of Cry toxins. Previous results revealed that the helices α4-α5 of Domain I were involved in the oligomerization of Cry2Ab, however, the key residues for Cry2Ab aggregation remained ambiguous. In present studies, we built 20 Cry2Ab alanine mutants site-directed in the helices α4-α5 of Domain I and demonstrated that mutants N151A, T152A, F157A, L183A, L185A and I188A could reduce the assembly of the 250 kDa oligomers, suggesting that these mutation residues might be essential for Cry2Ab oligomerization. As expected, all of these variants showed lower insecticidal activity against P. xylostella. Furthermore, we found that the pore-forming activities of these mutants also decreased when compared to wild-type Cry2Ab. Taken together, our data identified key residues for Cry2Ab oligomerization and emphasized that oligomerization was closely related to the insecticidal activity and pore-forming activity of Cry2Ab.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:11 |
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| Enthalten in: |
AMB Express - 11(2021), 1 vom: 31. Juli, Seite 112 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Pan, Zhi-Zhen [VerfasserIn] |
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| Links: |
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| Themen: |
Cry2Ab |
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| Anmerkungen: |
Date Revised 03.08.2021 published: Electronic Citation Status PubMed-not-MEDLINE |
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| doi: |
10.1186/s13568-021-01270-0 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM328761990 |
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| 245 | 1 | 0 | |a Key residues of Bacillus thuringiensis Cry2Ab for oligomerization and pore-formation activity |
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| 500 | |a Date Revised 03.08.2021 | ||
| 500 | |a published: Electronic | ||
| 500 | |a Citation Status PubMed-not-MEDLINE | ||
| 520 | |a © 2021. The Author(s). | ||
| 520 | |a As a pore-forming toxin, activation, oligomerization and pore-formation were both required for the mode of action of Cry toxins. Previous results revealed that the helices α4-α5 of Domain I were involved in the oligomerization of Cry2Ab, however, the key residues for Cry2Ab aggregation remained ambiguous. In present studies, we built 20 Cry2Ab alanine mutants site-directed in the helices α4-α5 of Domain I and demonstrated that mutants N151A, T152A, F157A, L183A, L185A and I188A could reduce the assembly of the 250 kDa oligomers, suggesting that these mutation residues might be essential for Cry2Ab oligomerization. As expected, all of these variants showed lower insecticidal activity against P. xylostella. Furthermore, we found that the pore-forming activities of these mutants also decreased when compared to wild-type Cry2Ab. Taken together, our data identified key residues for Cry2Ab oligomerization and emphasized that oligomerization was closely related to the insecticidal activity and pore-forming activity of Cry2Ab | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Cry2Ab | |
| 650 | 4 | |a Insecticidal activity | |
| 650 | 4 | |a Oligomerization | |
| 650 | 4 | |a Pore-forming activity | |
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| 700 | 1 | |a Liu, Bo |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Qing-Xi |e verfasserin |4 aut | |
| 700 | 1 | |a Zhu, Yu-Jing |e verfasserin |4 aut | |
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