Difference between revisions of "Part:BBa K5066004"
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===Plasmid construct===
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<img src="https://static.igem.wiki/teams/5066/vip-basic-part.png" height="auto" width="50%"/>
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Fig 1. Plasmid design construct in pET-28a
  
 
===Sequence and Features===
 
===Sequence and Features===

Revision as of 09:18, 2 October 2024


Vip3Aa

Description

Vip3Aa is one of the Bacillus thuringiensis toxins, or Bt toxins, that derive from Bt bacteria and are commonly used as insecticides as they can target specific insects without causing harm to other species. There are a wide variety of strains derived from a selection of Bt bacteria and each has similar effects but targets different species of insects. There are three main categories of the Bt toxin, Cry, Cyt, and Vip, and the Xpp strains we renamed from Cry strains.[1]



Usage and Biology

Similar to all other Bt toxins, Vip3Aa toxin when bonded to the midgut epithelial cells of the insect, will induce pore formation. On a large scale, larvae midgut tissues lose their function and cause symptoms in the A. aegypti larvae including starvation, electrolyte imbalance and eventually death. resulting in cell death.[2]


Plasmid construct

Fig 1. Plasmid design construct in pET-28a

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal XhoI site found at 576
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 1447
    Illegal SapI.rc site found at 550


Reference

[1] Shilling, P. J., Mirzadeh, K., Cumming, A. J., Widesheim, M., Köck, Z., & Daley, D. O. (2020). Improved designs for pET expression plasmids increase protein production yield in Escherichia coli. Communications Biology, 3(1). https://doi.org/10.1038/s42003-020-0939-8

[2] Jiang, K., Chen, Z., Zang, Y., Shi, Y., Shang, C., Jiao, X., Cai, J., & Gao, X. (2023). Functional characterization of Vip3Aa from Bacillus thuringiensis reveals the contributions of specific domains to its insecticidal activity. Journal of Biological Chemistry, 299(3), 103000. https://doi.org/10.1016/j.jbc.2023.103000