Difference between revisions of "Part:BBa K3409000"

 
 
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<partinfo>BBa_K3409000 short</partinfo>
 
<partinfo>BBa_K3409000 short</partinfo>
  
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Bacteriophages are viruses that can infect bacteria. Bacteriophages from Myoviridae family possesse Long Tail Fibers (LTF) which bind to specific motifs of the outer membrane of the target bacteria. T4 bacteriophages belong to Myoviridae family and are able to specifically recognize Escherichia coli thanks to specific recpetor binding proteins of the distal region of their LTF. These recpetor binding proteins recognize Lipopolysaccharide (LPS) or Outer membrane protein C which are present on the outer membrane of the target bacteria. To be more precise, the T4 uses the tip of its LTF to bind specifically to E. coli. The LTF is encoded by different proteins, on the tip is the gene product (gp) 37 and it is the gp37 that confers the T4 bacteriohage LTF binding specificity.  
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This part codes for the receptor binding protein, gene product 37 (gp37) of the T4 Myoviridae phage.
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===Usage===
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Bacteriophages have already been identified to target pathogenic bacteria like Salmonella, Listeria, M. tuberculosis, Pseudomonas or E. coli. Phage therapy uses bacteriophages, natural bacterial enemies to kill pathogenic bacteria. It originated in Paris, in the early 20th century. The use of these viruses to treat patients infected by bacteria was a safe option at the time but it was soon forgotten when antibiotics were discovered. Nowadays, when the available antibiotics are starting to show weaknesses, bacteriophages are gaining interest to fight against antimicrobial resistance. The concept relies on the use of these bacterial viruses to specifically attach and inject their genetic material into their host, leading to their lysis. Using phage therapy to fight against these infections has already proved beneficial in a number of cases.
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===Biology===
 +
Bacteriophages are viruses that can infect bacteria. Bacteriophages from Myoviridae family possess Long Tail Fibers (LTF) which bind to specific motifs of the outer membrane of the target bacteria. T4 bacteriophages belong to Myoviridae family and are able to specifically recognize Escherichia coli thanks to specific receptor binding proteins of the distal region of their LTF. These recpetor binding proteins recognize Lipopolysaccharide (LPS) or Outer membrane protein C which are present on the outer membrane of the target bacteria. To be more precise, the T4 uses the tip of its LTF to bind specifically to E. coli. These LTFs are attached to the phages base plate and play a role in phage adsorption to the target thanks to adhesins. In fact, they are responsible for the specific and reversible interaction with the receptors on the host membrane and once bound, they induce a conformational change. This brings the tail spikes near the target with which they irreversibly interact. Next is the puncture of the target’s membrane as the tail sheath injects the phages genetic material for infection. 
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[[File: T4.png|border|500px]]
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Figure 1 : Annotated structure of the T4 bacteriophage
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The LTF is encoded by different proteins, on the tip is the gene product (gp) 37 and it is the gp37 that confers the T4 bacteriophage LTF binding specificity.  
 +
 
 
For the proper folding of gp37, two chaperone proteins are required and have to be co-expressed, i.e., the gp 57a, encoded by the  gene 57A and gp38, encoded by the gene 38. They both participate in the proper folding of the distal part of the long fibers.
 
For the proper folding of gp37, two chaperone proteins are required and have to be co-expressed, i.e., the gp 57a, encoded by the  gene 57A and gp38, encoded by the gene 38. They both participate in the proper folding of the distal part of the long fibers.
  
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<!-- Add more about the biology of this part here
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===Usage and Biology===
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===Bibliography===
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Trojet, S. N., Caumont-Sarcos, A., Perrody, E., Comeau, A. M., & Krisch, H. M. (2011). The gp38 adhesins of the T4 superfamily: A complex modular determinant of the Phage’s host specificity. Genome Biology and Evolution, 3(1), 674–686. https://doi.org/10.1093/gbe/evr059
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Islam, M. Z., Fokine, A., Mahalingam, M., Zhang, Z., Garcia-Doval, C., Van Raaij, M. J., Rossmann, M. G., & Rao, V. B. (2019). Molecular Anatomy of the Receptor Binding Module of a Bacteriophage Long Tail Fiber. PLoS Pathogens, 15(12), 1–21. https://doi.org/10.1371/journal.ppat.1008193
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Latest revision as of 08:19, 26 October 2020


Gene Product (gp) 37

This part codes for the receptor binding protein, gene product 37 (gp37) of the T4 Myoviridae phage.

Usage

Bacteriophages have already been identified to target pathogenic bacteria like Salmonella, Listeria, M. tuberculosis, Pseudomonas or E. coli. Phage therapy uses bacteriophages, natural bacterial enemies to kill pathogenic bacteria. It originated in Paris, in the early 20th century. The use of these viruses to treat patients infected by bacteria was a safe option at the time but it was soon forgotten when antibiotics were discovered. Nowadays, when the available antibiotics are starting to show weaknesses, bacteriophages are gaining interest to fight against antimicrobial resistance. The concept relies on the use of these bacterial viruses to specifically attach and inject their genetic material into their host, leading to their lysis. Using phage therapy to fight against these infections has already proved beneficial in a number of cases.

Biology

Bacteriophages are viruses that can infect bacteria. Bacteriophages from Myoviridae family possess Long Tail Fibers (LTF) which bind to specific motifs of the outer membrane of the target bacteria. T4 bacteriophages belong to Myoviridae family and are able to specifically recognize Escherichia coli thanks to specific receptor binding proteins of the distal region of their LTF. These recpetor binding proteins recognize Lipopolysaccharide (LPS) or Outer membrane protein C which are present on the outer membrane of the target bacteria. To be more precise, the T4 uses the tip of its LTF to bind specifically to E. coli. These LTFs are attached to the phages base plate and play a role in phage adsorption to the target thanks to adhesins. In fact, they are responsible for the specific and reversible interaction with the receptors on the host membrane and once bound, they induce a conformational change. This brings the tail spikes near the target with which they irreversibly interact. Next is the puncture of the target’s membrane as the tail sheath injects the phages genetic material for infection.

T4.png Figure 1 : Annotated structure of the T4 bacteriophage

The LTF is encoded by different proteins, on the tip is the gene product (gp) 37 and it is the gp37 that confers the T4 bacteriophage LTF binding specificity.

For the proper folding of gp37, two chaperone proteins are required and have to be co-expressed, i.e., the gp 57a, encoded by the gene 57A and gp38, encoded by the gene 38. They both participate in the proper folding of the distal part of the long fibers.


Bibliography

Trojet, S. N., Caumont-Sarcos, A., Perrody, E., Comeau, A. M., & Krisch, H. M. (2011). The gp38 adhesins of the T4 superfamily: A complex modular determinant of the Phage’s host specificity. Genome Biology and Evolution, 3(1), 674–686. https://doi.org/10.1093/gbe/evr059

Islam, M. Z., Fokine, A., Mahalingam, M., Zhang, Z., Garcia-Doval, C., Van Raaij, M. J., Rossmann, M. G., & Rao, V. B. (2019). Molecular Anatomy of the Receptor Binding Module of a Bacteriophage Long Tail Fiber. PLoS Pathogens, 15(12), 1–21. https://doi.org/10.1371/journal.ppat.1008193


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 292
    Illegal BglII site found at 1486
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 1666
    Illegal AgeI site found at 634
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 1869