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Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops
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| Zeitschriftentitel: | Bioscience Reports |
|---|---|
| Personen und Körperschaften: | , , , , , , , , , |
| In: | Bioscience Reports, 33, 2013, 1 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Portland Press Ltd.
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| Schlagwörter: |
| author_facet |
Fujii, Yuki Tanaka, Shiho Otsuki, Manami Hoshino, Yasushi Morimoto, Chinatsu Kotani, Takuya Harashima, Yuko Endo, Haruka Yoshizawa, Yasutaka Sato, Ryoichi Fujii, Yuki Tanaka, Shiho Otsuki, Manami Hoshino, Yasushi Morimoto, Chinatsu Kotani, Takuya Harashima, Yuko Endo, Haruka Yoshizawa, Yasutaka Sato, Ryoichi |
|---|---|
| author |
Fujii, Yuki Tanaka, Shiho Otsuki, Manami Hoshino, Yasushi Morimoto, Chinatsu Kotani, Takuya Harashima, Yuko Endo, Haruka Yoshizawa, Yasutaka Sato, Ryoichi |
| spellingShingle |
Fujii, Yuki Tanaka, Shiho Otsuki, Manami Hoshino, Yasushi Morimoto, Chinatsu Kotani, Takuya Harashima, Yuko Endo, Haruka Yoshizawa, Yasutaka Sato, Ryoichi Bioscience Reports Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops Cell Biology Molecular Biology Biochemistry Biophysics |
| author_sort |
fujii, yuki |
| spelling |
Fujii, Yuki Tanaka, Shiho Otsuki, Manami Hoshino, Yasushi Morimoto, Chinatsu Kotani, Takuya Harashima, Yuko Endo, Haruka Yoshizawa, Yasutaka Sato, Ryoichi 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20120113 <jats:p>Characterizing the binding mechanism of Bt (Bacillus thuringiensis) Cry toxin to the cadherin receptor is indispensable to understanding the specific insecticidal activity of this toxin. To this end, we constructed 30 loop mutants by randomly inserting four serial amino acids covering all four receptor binding loops (loops α8, 1, 2 and 3) and analysed their binding affinities for Bombyx mori cadherin receptors via Biacore. High binding affinities were confirmed for all 30 mutants containing loop sequences that differed from those of wild-type. Insecticidal activities were confirmed in at least one mutant from loops 1, 2 and 3, suggesting that there is no critical amino acid sequence for the binding of the four loops to BtR175. When two mutations at different loops were integrated into one molecule, no reduction in binding affinity was observed compared with wild-type sequences. Based on these results, we discussed the binding mechanism of Cry toxin to cadherin protein.</jats:p> Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops Bioscience Reports |
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10.1042/bsr20120113 |
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Portland Press Ltd., 2013 |
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Portland Press Ltd., 2013 |
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| title |
Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_unstemmed |
Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_full |
Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_fullStr |
Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_full_unstemmed |
Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_short |
Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_sort |
cry1aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain ii loops |
| topic |
Cell Biology Molecular Biology Biochemistry Biophysics |
| url |
http://dx.doi.org/10.1042/bsr20120113 |
| publishDate |
2013 |
| physical |
|
| description |
<jats:p>Characterizing the binding mechanism of Bt (Bacillus thuringiensis) Cry toxin to the cadherin receptor is indispensable to understanding the specific insecticidal activity of this toxin. To this end, we constructed 30 loop mutants by randomly inserting four serial amino acids covering all four receptor binding loops (loops α8, 1, 2 and 3) and analysed their binding affinities for Bombyx mori cadherin receptors via Biacore. High binding affinities were confirmed for all 30 mutants containing loop sequences that differed from those of wild-type. Insecticidal activities were confirmed in at least one mutant from loops 1, 2 and 3, suggesting that there is no critical amino acid sequence for the binding of the four loops to BtR175. When two mutations at different loops were integrated into one molecule, no reduction in binding affinity was observed compared with wild-type sequences. Based on these results, we discussed the binding mechanism of Cry toxin to cadherin protein.</jats:p> |
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| author | Fujii, Yuki, Tanaka, Shiho, Otsuki, Manami, Hoshino, Yasushi, Morimoto, Chinatsu, Kotani, Takuya, Harashima, Yuko, Endo, Haruka, Yoshizawa, Yasutaka, Sato, Ryoichi |
| author_facet | Fujii, Yuki, Tanaka, Shiho, Otsuki, Manami, Hoshino, Yasushi, Morimoto, Chinatsu, Kotani, Takuya, Harashima, Yuko, Endo, Haruka, Yoshizawa, Yasutaka, Sato, Ryoichi, Fujii, Yuki, Tanaka, Shiho, Otsuki, Manami, Hoshino, Yasushi, Morimoto, Chinatsu, Kotani, Takuya, Harashima, Yuko, Endo, Haruka, Yoshizawa, Yasutaka, Sato, Ryoichi |
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| description | <jats:p>Characterizing the binding mechanism of Bt (Bacillus thuringiensis) Cry toxin to the cadherin receptor is indispensable to understanding the specific insecticidal activity of this toxin. To this end, we constructed 30 loop mutants by randomly inserting four serial amino acids covering all four receptor binding loops (loops α8, 1, 2 and 3) and analysed their binding affinities for Bombyx mori cadherin receptors via Biacore. High binding affinities were confirmed for all 30 mutants containing loop sequences that differed from those of wild-type. Insecticidal activities were confirmed in at least one mutant from loops 1, 2 and 3, suggesting that there is no critical amino acid sequence for the binding of the four loops to BtR175. When two mutations at different loops were integrated into one molecule, no reduction in binding affinity was observed compared with wild-type sequences. Based on these results, we discussed the binding mechanism of Cry toxin to cadherin protein.</jats:p> |
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| imprint | Portland Press Ltd., 2013 |
| imprint_str_mv | Portland Press Ltd., 2013 |
| institution | DE-Ch1, DE-L229, DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14 |
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| spelling | Fujii, Yuki Tanaka, Shiho Otsuki, Manami Hoshino, Yasushi Morimoto, Chinatsu Kotani, Takuya Harashima, Yuko Endo, Haruka Yoshizawa, Yasutaka Sato, Ryoichi 0144-8463 1573-4935 Portland Press Ltd. Cell Biology Molecular Biology Biochemistry Biophysics http://dx.doi.org/10.1042/bsr20120113 <jats:p>Characterizing the binding mechanism of Bt (Bacillus thuringiensis) Cry toxin to the cadherin receptor is indispensable to understanding the specific insecticidal activity of this toxin. To this end, we constructed 30 loop mutants by randomly inserting four serial amino acids covering all four receptor binding loops (loops α8, 1, 2 and 3) and analysed their binding affinities for Bombyx mori cadherin receptors via Biacore. High binding affinities were confirmed for all 30 mutants containing loop sequences that differed from those of wild-type. Insecticidal activities were confirmed in at least one mutant from loops 1, 2 and 3, suggesting that there is no critical amino acid sequence for the binding of the four loops to BtR175. When two mutations at different loops were integrated into one molecule, no reduction in binding affinity was observed compared with wild-type sequences. Based on these results, we discussed the binding mechanism of Cry toxin to cadherin protein.</jats:p> Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops Bioscience Reports |
| spellingShingle | Fujii, Yuki, Tanaka, Shiho, Otsuki, Manami, Hoshino, Yasushi, Morimoto, Chinatsu, Kotani, Takuya, Harashima, Yuko, Endo, Haruka, Yoshizawa, Yasutaka, Sato, Ryoichi, Bioscience Reports, Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops, Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| title | Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_full | Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_fullStr | Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_full_unstemmed | Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_short | Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| title_sort | cry1aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain ii loops |
| title_unstemmed | Cry1Aa binding to the cadherin receptor does not require conserved amino acid sequences in the domain II loops |
| topic | Cell Biology, Molecular Biology, Biochemistry, Biophysics |
| url | http://dx.doi.org/10.1042/bsr20120113 |