Difference between revisions of "Part:BBa K3606003"

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This part produces an antibiotic originated from Escherichia coli that targets a bacterial topoisomerase, DNA gyrase.
 
This part produces an antibiotic originated from Escherichia coli that targets a bacterial topoisomerase, DNA gyrase.
  
<h2>Design:</h2>
+
<h2>Background:</h2>
 +
Here, we tried to improve the former antimicrobial peptide(mccb17) expressing system of 2019 Fudan[[BBa_K3245010]]. By dividing into the peptide expressing parts and the immunity parts, we wanted to firstly test whether the polycistron could work properly and separately, then
 +
manipulate their expression level with more efficiency.
  
This part is an antibiotic coding gene cluster with leader peptide and proteins for maturation. We introduced it to our improved antibiotic expressing system to inhibit the growth of other bacteria in human intestine so as to enhance Nissle's competitiveness,as well as to reduce risk of illness caused by some opportunistic pathogens.  
+
<h2>Design:</h2>
 +
This part is an antibiotic coding gene cluster with leader peptide and proteins for its maturation.
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here
===Usage and Biology===
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<h2>Usage and Biology:</h2>
 +
We introduced it to our improved antibiotic expressing system to inhibit the growth of other bacteria in human intestine so as to enhance Nissle's competitiveness, as well as to reduce risk of illness caused by some opportunistic pathogens.
  
 
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<span class='h3bb'></span>
 
<span class='h3bb'></span>
 
<partinfo>BBa_K3606003 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K3606003 SequenceAndFeatures</partinfo>
 +
<h2>Results:</h2>
 +
We constructed the plasmid and successfully expressed the mcbABCD, here is the electrophoresis map.
 +
  
 +
<h2>Further Application:</h2>
 +
For futher application, this part is provided as an antimicrobial peptide(mccb17) expressing example and are effective for a wide range of microbes.
  
 
<!-- Uncomment this to enable Functional Parameter display  
 
<!-- Uncomment this to enable Functional Parameter display  

Revision as of 06:56, 25 October 2020


mcbABCD

This part produces an antibiotic originated from Escherichia coli that targets a bacterial topoisomerase, DNA gyrase.

Background:

Here, we tried to improve the former antimicrobial peptide(mccb17) expressing system of 2019 FudanBBa_K3245010. By dividing into the peptide expressing parts and the immunity parts, we wanted to firstly test whether the polycistron could work properly and separately, then manipulate their expression level with more efficiency.

Design:

This part is an antibiotic coding gene cluster with leader peptide and proteins for its maturation.


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal PstI site found at 2297
    Illegal PstI site found at 2330
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal PstI site found at 2297
    Illegal PstI site found at 2330
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal PstI site found at 2297
    Illegal PstI site found at 2330
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal PstI site found at 2297
    Illegal PstI site found at 2330
    Illegal NgoMIV site found at 1959
    Illegal AgeI site found at 2131
  • 1000
    COMPATIBLE WITH RFC[1000]

Results:

We constructed the plasmid and successfully expressed the mcbABCD, here is the electrophoresis map. 图

Further Application:

For futher application, this part is provided as an antimicrobial peptide(mccb17) expressing example and are effective for a wide range of microbes.

Reference

Collin F, Maxwell A. The Microbial Toxin Microcin B17: Prospects for the Development of New Antibacterial Agents. J Mol Biol. 2019;431(18):3400–3426. doi:10.1016/j.jmb.2019.05.050

S. Duquesne, D. Destoumieux-Garzón, J. Peduzzi, S. Rebuffat. Microcins, gene-encoded antibacterial peptides from enterobacteria

Sassone-Corsi M, Nuccio SP, Liu H, Hernandez D, Vu CT, Takahashi AA, Edwards RA, Raffatellu M. Microcins mediate competition among Enterobacteriaceae in the inflamed gut. Nature. 2016 Dec 8;540(7632):280-283.