Difference between revisions of "Part:BBa K4607004"

 
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<partinfo>BBa_K4607004 short</partinfo>
  
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<center><b>Figure 1.</b>  Lys from the CSA13 bacteriophage diagram.</center>
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<p align="justify">
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The endolysin Lys from the <i>Staphylococcus aureus virulent bacteriophage CSA13</i> [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.
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===<span class='h3bb'><b>Sequence and Features</b></span>===
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<partinfo>BBa_K4607004 SequenceAndFeatures</partinfo>
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===Usage and Biology===
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<div style="text-align:justify;">
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The endolysin Lys from the <i>Staphylococcus aureus virulent bacteriophage CSA1</i>, is composed of two domains. The bacteriophage CSA13 CHAP domain has excellent catalytic activity, up to 90%, degrading almost 15 strains of <i>Staphylococcus</i> 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].
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===Results===
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<center><b>Figure 2.</b> 3D structure of the protein from the CSA13 bacteriophage, obtained with AlphaFold2.</center>
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===References===
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[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

Revision as of 07:15, 21 July 2023

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