Difference between revisions of "Part:BBa K4147002"
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<partinfo>BBa_K4147002 short</partinfo> | <partinfo>BBa_K4147002 short</partinfo> | ||
− | This part contains the linear construct BBa_K4147001 for (CBD)2-DrsB1 with | + | This part contains the linear construct BBa_K4147001 for (CBD)2-DrsB1 which already counts with a PelB signal peptide on the N- terminal as well as a 6X-His tag at the end of the dermaseptin CDS (C- terminal) for later protein purification. This composite construct includes a LacI regulated promoter. Additionally, it contains an RBS under the part name BBa_B0032. Finally, it has a double terminator (BBa_B0015) to ensure correct termination. As a linear 1075 bp construct, it contains the RFC10 prefix and suffix, making the part compatible with other iGEM parts. |
+ | |||
Among a wide range of AMPs, polycationic dermaseptin peptides are produced by the skin glands of the frog <i>Phyllomedusa bicolor</i> [1]. It supplies both antibacterial and antifungal protection to a broad range of plant pathogens but shows no toxic effects on plant and mammalian cells [2]. This peptide of molecular weight of 22.1 kDa contains a tandem repeat of a chitin binding domain (CBD) as an improvement of dermaseptin-b1 gene (AKA MsrA2)(BBa_K2577001) which binds to chitin fungal cell wall, thereby increasing the lytic activity of the catalytic dom | Among a wide range of AMPs, polycationic dermaseptin peptides are produced by the skin glands of the frog <i>Phyllomedusa bicolor</i> [1]. It supplies both antibacterial and antifungal protection to a broad range of plant pathogens but shows no toxic effects on plant and mammalian cells [2]. This peptide of molecular weight of 22.1 kDa contains a tandem repeat of a chitin binding domain (CBD) as an improvement of dermaseptin-b1 gene (AKA MsrA2)(BBa_K2577001) which binds to chitin fungal cell wall, thereby increasing the lytic activity of the catalytic dom | ||
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===Functional Parameters=== | ===Functional Parameters=== | ||
<partinfo>BBa_K4147002 parameters</partinfo> | <partinfo>BBa_K4147002 parameters</partinfo> | ||
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+ | ===REFERENCES=== | ||
+ | [1] Shams, M. V., Nazarian-Firouzabadi, F., Ismaili, A., & Shirzadian-Khorramabad, R. (2019). Production of a Recombinant Dermaseptin Peptide in Nicotiana tabacum Hairy Roots with Enhanced Antimicrobial Activity. Molecular Biotechnology. doi:10.1007/s12033-019-00153-x | ||
+ | [2] Khademi, M., Varasteh-Shams, M., Nazarian-Firouzabadi, F., & Ismaili, A. (2020). New Recombinant Antimicrobial Peptides Confer Resistance to Fungal Pathogens in Tobacco Plants. Frontiers in Plant Science, 11. doi:10.3389/fpls.2020.01236 |
Revision as of 23:16, 7 October 2022
Expression construct for (CBD)2-DrsB1: Dermaseptin AMP from Phyllomedusa bicolor
This part contains the linear construct BBa_K4147001 for (CBD)2-DrsB1 which already counts with a PelB signal peptide on the N- terminal as well as a 6X-His tag at the end of the dermaseptin CDS (C- terminal) for later protein purification. This composite construct includes a LacI regulated promoter. Additionally, it contains an RBS under the part name BBa_B0032. Finally, it has a double terminator (BBa_B0015) to ensure correct termination. As a linear 1075 bp construct, it contains the RFC10 prefix and suffix, making the part compatible with other iGEM parts.
Among a wide range of AMPs, polycationic dermaseptin peptides are produced by the skin glands of the frog Phyllomedusa bicolor [1]. It supplies both antibacterial and antifungal protection to a broad range of plant pathogens but shows no toxic effects on plant and mammalian cells [2]. This peptide of molecular weight of 22.1 kDa contains a tandem repeat of a chitin binding domain (CBD) as an improvement of dermaseptin-b1 gene (AKA MsrA2)(BBa_K2577001) which binds to chitin fungal cell wall, thereby increasing the lytic activity of the catalytic dom
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal AgeI site found at 392
Illegal AgeI site found at 671 - 1000COMPATIBLE WITH RFC[1000]
REFERENCES
[1] Shams, M. V., Nazarian-Firouzabadi, F., Ismaili, A., & Shirzadian-Khorramabad, R. (2019). Production of a Recombinant Dermaseptin Peptide in Nicotiana tabacum Hairy Roots with Enhanced Antimicrobial Activity. Molecular Biotechnology. doi:10.1007/s12033-019-00153-x [2] Khademi, M., Varasteh-Shams, M., Nazarian-Firouzabadi, F., & Ismaili, A. (2020). New Recombinant Antimicrobial Peptides Confer Resistance to Fungal Pathogens in Tobacco Plants. Frontiers in Plant Science, 11. doi:10.3389/fpls.2020.01236