Part:BBa_K2834000
6x His-Tag
Apidaecin is mostly lethal to Gram-negative bacteria, nevertheless, in the previous investigation by Khilnani, J. in 2015 [1] apidaecin by itself showed antimicrobial activity against P. larvae and worked in synergy with defensin 2 effectively inhibiting this pathogen. Apidaecin appears to have no effect toward eukaryotic cells, and there is little to no bacterial resistance. The mechanism by which apidaecin kills bacteria starts with a non-specific binding of the peptide to an outer membrane component, which is a substantial lipopolysaccharide (LPS) component. Apidaecin later invades the periplasmic space thanks to a specific receptor/docking molecule, which is a component of the transport system on the inner membrane. The peptide is then translocated into the interior of the cell.[2] It is transported through into the cytosol by SbmA.[3] Once the peptide is inside of the cell it has two possible targets: DnaK and the 70s ribosome. Apidaecin leads the protein synthesis inhibition by targeting the ribosome. However, it appears that the ultimate target is the DnaK, this is the major bacterial Hsp70 (70 kDa heat shock proteins). DnaK has several functions that end up inhibited by the peptide; the ATPase activity, which is involved in the initiation of DNA synthesis, and the refolding of misfolded proteins.[2] DnaK is also indispensable for the viability of the cell in stress conditions like heat shock at 42ºC.[4]
[1] Khilnani, Jasmin Camille. (2015). The Effects of Honeybee (Apis mellifera) Antimicrobial Peptides on Paenibacillus larvae. UNLV Theses, Dissertations, Professional Papers, and Capstones. 2486. https://digitalscholarship.unlv.edu/thesesdissertations/2486 [2] Li, W. F., Ma, G. X., & Zhou, X. X. (2006). Apidaecin-type peptides: biodiversity, structure–function relationships and mode of action. Peptides, 27(9), 2350-2359. [3] Krizsan, A., Volke, D., Weinert, S., Sträter, N., Knappe, D., & Hoffmann, R. (2014). Insect-Derived Proline-Rich Antimicrobial Peptides Kill Bacteria by Inhibiting Bacterial Protein Translation at the 70 S Ribosome.Angewandte Chemie International Edition, 53(45), 12236–12239. [4] Calloni, G., Chen, T., Schermann, S. M., Chang, H., Genevaux, P., Agostini, F., et al. (2012). DnaK Functions as a Central Hub in the E. coli Chaperone Network. Cell Reports, 1(3), 251–264.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
| None |