Part:BBa_K4607004

LysCSA13

Figure 1. Lys from the CSA13 bacteriophage diagram.

The endolysin Lys from the Staphylococcus aureus virulent bacteriophage CSA13 [1] is composed of two domains that make it capable to lysate the bacteria that are recognized by the enzyme. It keeps its stability in a range of 4 to 37°C and pH from 7 to 9.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  COMPATIBLE WITH RFC[12]
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  COMPATIBLE WITH RFC[25]
• 1000
  COMPATIBLE 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].

Results

Figure 2. 3D structure of the protein from the CSA13 bacteriophage, obtained with AlphaFold2.

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