Part:BBa_K4607004
LysCSA13
This biobrick consist of the endolysin Lys from the Staphylococcus aureus virulent bacteriophage CSA13, it is composed of two domains: The CHAP domain, with an excellent catalytic activity, up to 90%, degrading almost 15 strains of Staphylococcus including methicillin-resistant strains (MRSA) [1], and the SH3 domain, which recognizes and binds to the highly specific glycine of the pentaglycine cross-bridge glycosidic bond in the heteropolymer of the S. aureus peptidoglycan, activating the catalytic domain [2]. The enzyme has a length of 249 amino acids and a molecular weight of 28.36 kDa. It keeps its stability in a range of 4 to 37 °C and a pH of 7 to 9, the average endolysin lifetime is about 20 minutes[3]. The part is adapted to the Golden Gate cloning method.
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]
Usage and Biology
The endolysin Lys from the Staphylococcus aureus virulent bacteriophage CSA1, is composed of two domains. The bacteriophage CSA13 CHAP domain has excellent catalytic activity, up to 90%, degrading almost 15 strains of Staphylococcus including methicillin-resistant strains (MRSA). As with many of the endolysins, it cleaves to the cell wall by disrupting the peptidoglycan that composes the bacterial cell; for this to be possible, the bacteriophage CSA13 SH3 domain recognizes and binds to the glycine of the pentaglycine cross-bridge glycosidic bond in the heteropolymer of the peptidoglycan, which makes it completely safe for the host [1].
References
[1] Cha, Y., Son, B., & Ryu, S. (2019). Effective removal of staphylococcal biofilms on various food contact surfaces by Staphylococcus aureus phage endolysin LysCSA13. Food Microbiology, 84, 103245. https://doi.org/10.1016/j.fm.2019.103245| None |