Difference between revisions of "Part:BBa K4607003"

 
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<partinfo>BBa_K4607003 short</partinfo>
  
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<center><b>Figure 1.</b> SH3 domain from the B30 bacteriophage diagram.</center>
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The Sh3 domain from the bacteriophage B30 is capable of recognizing and binding to the cell wall of <i>Streptococcus agalactiae, Streptococcus uberis, and Staphylococcus aureus</i>. It keeps its stability in a range of 4 to 37°C and pH from 7 to 8 [1].
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===<span class='h3bb'><b>Sequence and Features</b></span>===
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<partinfo>BBa_K46070003 SequenceAndFeatures</partinfo>
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===Usage and Biology===
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To increase the sensitivity of the enzyme for pathogenic bacteria, specifically <i>Streptococcus uberis, Staphylococcus aureus, and Streptococcus agalactiae</i>, the SH3 domain from the B30 bacteriophage was selected, which makes it completely safe for the host [3]. The use of enzybiotics represents an alternative to the misuse of antibiotics without loss of efficiency; it is a novel and environmentally friendly process. It supplies antibacterial protection to pathogenic bacteria but shows no toxic effects on mammalian cells.
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===Results===
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<center><b>Figure 2.</b> 3D structure of the SH3 domain from the B30 bacteriophage, obtained with AlphaFold2.</center>
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===References===
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[1] Jarábková, V., Tišáková, L., Benešík, M., & Godány, A. (2020). SH3 BINDING DOMAINS FROM PHAGE ENDOLYSINS: HOW TO USE THEM FOR DETECTION OF GRAMPOSITIVE PATHOGENS. Www.muni.cz, 9(6). https://www.muni.cz/vyzkum/publikace/1674660

Revision as of 06:58, 21 July 2023

SH3B30 Domain


Figure 1. SH3 domain from the B30 bacteriophage diagram.

The Sh3 domain from the bacteriophage B30 is capable of recognizing and binding to the cell wall of Streptococcus agalactiae, Streptococcus uberis, and Staphylococcus aureus. It keeps its stability in a range of 4 to 37°C and pH from 7 to 8 [1].

Sequence and Features

No part name specified with partinfo tag.

Usage and Biology

To increase the sensitivity of the enzyme for pathogenic bacteria, specifically Streptococcus uberis, Staphylococcus aureus, and Streptococcus agalactiae, the SH3 domain from the B30 bacteriophage was selected, which makes it completely safe for the host [3]. The use of enzybiotics represents an alternative to the misuse of antibiotics without loss of efficiency; it is a novel and environmentally friendly process. It supplies antibacterial protection to pathogenic bacteria but shows no toxic effects on mammalian cells.


Results

Figure 2. 3D structure of the SH3 domain from the B30 bacteriophage, obtained with AlphaFold2.

References

[1] Jarábková, V., Tišáková, L., Benešík, M., & Godány, A. (2020). SH3 BINDING DOMAINS FROM PHAGE ENDOLYSINS: HOW TO USE THEM FOR DETECTION OF GRAMPOSITIVE PATHOGENS. Www.muni.cz, 9(6). https://www.muni.cz/vyzkum/publikace/1674660