Part:BBa_K4248001
LL-37
LL-37
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
contribution
The innate immune system is a functional and physiological barrier for the body to resist microbial infection, and antimicrobial peptides are important effector molecules of the innate immune system. At present, about 1500 kinds of antimicrobial peptides have been discovered. Such antimicrobial peptides are widely used in cancer cells, Gram-negative and positive bacteria, fungi, viruses, protozoa and so on. The human body mainly produces two types of antimicrobial peptides: defensin family peptides and cathelicidin family peptides. Although there are many members of the defensin family of peptides, cathelicidin has only one antimicrobial peptide product, LL-37. LL-37 is the C-terminal cleavage product of cathelicidin peptide Hcap-18, which directly kills bacteria, fungi and viruses. LL-37 is expressed widely in human body cells, such as epithelial skin cell，bone marrow cells, and neutrophils. It is responsible for immune defense against bacterial invasion, with study showing its effect of significant reduction in attachment of bacteria and biofilm production We deliberately searched the IGEM biological element library and found that LL-37 was first submitted by the BBa_K1162006 team. On this basis, we carried out further molecular cloning construction and corresponding functional experiments, which can provide further information for other IGEM.
Contribution
The innate immune system is a functional and physiological barrier for the body to resist microbial infection, and antimicrobial peptides are important effector molecules of the innate immune system. At present, about 1500 kinds of antimicrobial peptides have been discovered. Such antimicrobial peptides are widely used in cancer cells, Gram-negative and positive bacteria, fungi, viruses, protozoa and so on. The human body mainly produces two types of antimicrobial peptides: defensin family peptides and cathelicidin family peptides. Although there are many members of the defensin family of peptides, cathelicidin has only one antimicrobial peptide product, LL-37. LL-37 is the C-terminal cleavage product of cathelicidin peptide Hcap-18, which directly kills bacteria, fungi and viruses. LL-37 is expressed widely in human body cells, such as epithelial skin cell，bone marrow cells, and neutrophils. It is responsible for immune defense against bacterial invasion, with study showing its effect of significant reduction in attachment of bacteria and biofilm production We deliberately searched the IGEM biological element library and found that LL-37 was first submitted by the BBa_K1162006 team. On this basis, we carried out further molecular cloning construction and corresponding functional experiments, which can provide further information for other IGEM.
1. Construction of the antimicrobial peptide expression plasmids
We send the constructed recombinant plasmid to a sequencing company for sequencing. The returned sequencing comparison results showed that there were no mutations in the ORF region (Figure 1.), and the plasmid was successfully constructed. So far, we have successfully obtained five recombinant plasmids, which were respectively on the pET28a(+) vector, which can be used to express antimicrobial peptide proteins.
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