Difference between revisions of "Part:BBa K2599001"
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<p style="padding-top:20px;font-size:20px"><b>Introduction</b></p> | <p style="padding-top:20px;font-size:20px"><b>Introduction</b></p> | ||
− | Bovicin HJ50 is isolated from <i> Streptococcus bovis </i> HJ50. It | + | Bovicin HJ50 is isolated from <i> Streptococcus bovis </i> HJ50. It shows similarity to type AII lantibiotics, the largest group of lantibiotics. It comprises a linear N-terminal region and a globular C-terminal region. Its disulfide bond is especially essential for antimicrobial activity. Like most of the bacteriocins produced by lactic acid bacteria, Bovicin HJ50 showed a narrow range of inhibiting activity. Its antimicrobial activity has been proved in reference. |
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The bactericidal activity of Bovicin HJ50 is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Its pore-forming activity is significantly different from other lantibiotics, suggesting a novel antimicrobial mechanism. | The bactericidal activity of Bovicin HJ50 is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Its pore-forming activity is significantly different from other lantibiotics, suggesting a novel antimicrobial mechanism. | ||
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<p style="padding-top:10px;font-size:20px;"><b>Features of Bovicin HJ50</b></p> | <p style="padding-top:10px;font-size:20px;"><b>Features of Bovicin HJ50</b></p> |
Revision as of 12:14, 1 October 2018
Antimicrobial peptide - Bovicin HJ50
This biobrick is the basic part of the Bovicin HJ50, more information please look for the composite part (BBa_K2599009).
Figure 1. Basic part of Bovicin HJ50
Introduction
Bovicin HJ50 is isolated from Streptococcus bovis HJ50. It shows similarity to type AII lantibiotics, the largest group of lantibiotics. It comprises a linear N-terminal region and a globular C-terminal region. Its disulfide bond is especially essential for antimicrobial activity. Like most of the bacteriocins produced by lactic acid bacteria, Bovicin HJ50 showed a narrow range of inhibiting activity. Its antimicrobial activity has been proved in reference.
Mechanism of Bovicin HJ50
The bacteriocins inhibit their target organisms through pore formation. Though the mechanism of each inhibition is vary from species to species, the general process is conserved. To see more details, please search for our project page.
The bactericidal activity of Bovicin HJ50 is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores. Its pore-forming activity is significantly different from other lantibiotics, suggesting a novel antimicrobial mechanism.
Features of Bovicin HJ50
1. Species Specific
Bacteriocins target strains or closely related species. The organisims that Bovicin HJ50 targets including Bacillus megaterium, Bacillus subtilis, Bacillus coagulans, etc.
Thus this bacteriocin is one of the peptide candidates for our project, that can solve the unbalance microbiota of agriculture in Taiwan.
More target organisms can be found on [http://bactibase.hammamilab.org/BAC156 bactibase].
2. Eco-friendly
Since Bovicin HJ50 is a polypeptide naturally produced by bacteria itself and can inhibit other bacteria without much environment impact. It don't pose threat to other organisms like farm animals or humans. Therefore, this toxin will not cause safety problem.
3. Biodegradable
Bovicin HJ50 is a short peptide that will degrade in a short time. After degradation, this antibacterial peptide is harmless to our environment.
Experiment Result
Cloning
We conbined our toxic gene to pSB1C3 backbone and conducted PCR to check the size of our part. The Bovicin HJ50 sequence length is around 171 b.p.
Figure 2 PCR
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 20
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
Reference