Difference between revisions of "Part:BBa K5311006"

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<partinfo>BBa_K5311006 short</partinfo>
 
<partinfo>BBa_K5311006 short</partinfo>
  
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The CAP 10-3 endolysin is an enzyme derived from a bacteriophage that specifically targets and lyses Cutibacterium acnes. Its inclusion in our project is essential, as it allows us to regulate the growth of Cutibacterium acnes, ensuring a balanced interaction between the patient’s original skin microbiota and the newly introduced microbiota from our product, thereby preventing dysbiosis.
 
  
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The primary function of this enzyme is to induce cell death in the transformed Cutibacterium acnes. It achieves this by degrading the peptidoglycan links in the bacterial cell wall, creating pores that destabilize the cell membrane. Ultimately, the exposed Cutibacterium acnes cells succumb to osmotic pressure, leading to their death.[1]
 
  
 
===Sequencing===
 
===Sequencing===
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===Biology===
 
===Biology===
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The CAP 10-3 endolysin is an enzyme derived from a bacteriophage that specifically targets and lyses Cutibacterium acnes. Its inclusion in our project is essential, as it allows us to regulate the growth of Cutibacterium acnes, ensuring a balanced interaction between the patient’s original skin microbiota and the newly introduced microbiota from our product, thereby preventing dysbiosis.
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In the case of the endolysin derived from the CAP 10-3 bacteriophage, its action specifically targets the degradation of the cell wall of Cutibacterium acnes, a Gram-positive bacterium with a cell wall rich in peptidoglycan, which is a crucial structural component. This endolysin is classified as an N-acetylmuramoyl-L-alanine amidase, which cleaves the bond between the N-acetylmuramic acid and the L-alanine residue in the peptidoglycan backbone.
  
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The primary function of this enzyme is to induce cell death in the transformed Cutibacterium acnes. It achieves this by degrading the peptidoglycan links in the bacterial cell wall, creating pores that destabilize the cell membrane. Ultimately, the exposed Cutibacterium acnes cells succumb to osmotic pressure, leading to their death.[1]
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By breaking down the peptidoglycan, the endolysin disrupts the rigid structure of the cell wall, leading to a loss of osmotic integrity. As a result, the bacterial cell can no longer withstand the internal pressure, causing rapid cell lysis. This mechanism is particularly effective against Gram-positive bacteria like C. acnes because they have a thick peptidoglycan layer that is more accessible to endolysins, unlike Gram-negative bacteria, which possess an additional outer membrane that restricts endolysin access.[1]

Revision as of 09:49, 29 September 2024

CAP 10-3 Endolysin


Sequencing

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 266
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 34
    Illegal NgoMIV site found at 445
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 193

Biology

In the case of the endolysin derived from the CAP 10-3 bacteriophage, its action specifically targets the degradation of the cell wall of Cutibacterium acnes, a Gram-positive bacterium with a cell wall rich in peptidoglycan, which is a crucial structural component. This endolysin is classified as an N-acetylmuramoyl-L-alanine amidase, which cleaves the bond between the N-acetylmuramic acid and the L-alanine residue in the peptidoglycan backbone.

By breaking down the peptidoglycan, the endolysin disrupts the rigid structure of the cell wall, leading to a loss of osmotic integrity. As a result, the bacterial cell can no longer withstand the internal pressure, causing rapid cell lysis. This mechanism is particularly effective against Gram-positive bacteria like C. acnes because they have a thick peptidoglycan layer that is more accessible to endolysins, unlike Gram-negative bacteria, which possess an additional outer membrane that restricts endolysin access.[1]