Difference between revisions of "Part:BBa K3286138"

Line 11: Line 11:
  
 
===Characterization by team 2021 UZurich===
 
===Characterization by team 2021 UZurich===
Seedling growth inhibition (SGI) assay was performed to characterize the immunogenicity of flg22 and elf18 peptide (by chemical synthesis).  
+
Seedling growth inhibition (SGI) assay was performed to characterize the immunogenicity of flg22 and elf18 peptides on <i>A. thaliana</i> Col-0 seedlings. flg22 and elf18 trigger similar levels of plant immune responses, which is consistent with previous research (Figure 2).
  
 
[[File:flg22vself18.png|500px]]
 
[[File:flg22vself18.png|500px]]
 +
 +
Figure 1. Results of SGI assay comparing the immunogenicity of flg22 and elf18
 +
  
 
[[File:flg22 vs elf18 from paper.png|700px]]
 
[[File:flg22 vs elf18 from paper.png|700px]]
 +
 +
Figure 2. Immunogenicity of flg22 and elf18 (modified from Li et al., 2009)
 +
 +
====Reference====
 +
Li, J., Zhao-Hui, C., Batoux, M., Nekrasov, V., Roux, M., Chinchilla, D., ... & Jones, J. D. (2009). Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR. Proceedings of the National Academy of Sciences, 106(37), 15973-15978.
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Revision as of 20:29, 20 October 2021


flg22

Flg22 is a peptide consisting of 22 conserved amino acids at the N-terminus flaggelin of Pseudomonas syringae [Felix et al., 1999]. Flg22 is a well described Microbe Associated Molecular Pattern (MAMPs). If recognised, MAMPS trigger PAMP Triggered Immunity in plants. They have been shown to trigger disease resistance in plants. [Zipfel et al., 2004]. flg22 can be used to active an immune response in plants.

It is very hard to purify this peptide if recombinantly expressed in E. coli, due to the small size and the folding of this peptide.

Felix, G., Duran, J. D., Volko, S., & Boller, T. (1999). Plants have a sensitive perception system for the most conserved domain of bacterial flagellin. The Plant Journal : For Cell and Molecular Biology, 18(3), 265–276. https://doi.org/10.1046/j.1365-313x.1999.00265.x Felix, G., Duran, J. D., Volko, S., & Boller, T. (1999). Plants have a sensitive perception system for the most conserved domain of bacterial flagellin. The Plant Journal : For Cell and Molecular Biology, 18(3), 265–276. https://doi.org/10.1046/j.1365-313x.1999.00265.x

Characterization by team 2021 UZurich

Seedling growth inhibition (SGI) assay was performed to characterize the immunogenicity of flg22 and elf18 peptides on A. thaliana Col-0 seedlings. flg22 and elf18 trigger similar levels of plant immune responses, which is consistent with previous research (Figure 2).

Flg22vself18.png

Figure 1. Results of SGI assay comparing the immunogenicity of flg22 and elf18


Flg22 vs elf18 from paper.png

Figure 2. Immunogenicity of flg22 and elf18 (modified from Li et al., 2009)

Reference

Li, J., Zhao-Hui, C., Batoux, M., Nekrasov, V., Roux, M., Chinchilla, D., ... & Jones, J. D. (2009). Specific ER quality control components required for biogenesis of the plant innate immune receptor EFR. Proceedings of the National Academy of Sciences, 106(37), 15973-15978.

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 58
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 58
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 58
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 58
    Illegal NgoMIV site found at 52
    Illegal AgeI site found at 16
  • 1000
    COMPATIBLE WITH RFC[1000]