Difference between revisions of "Part:BBa K1919000"

(→‎Usage and Biology)
(→‎Usage and Biology)
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Cecropins, a group of small AMPs mainly found in the hemolymph of insects, consist of 31 39 amino acid residues and have a broad spectrum, high heat stability and potent bacteriostatic activity [3-5]. CecropinXJ (Part BBa_K1919000) is a member of the Cecropin family, which was first cloned from the larvae of the Xinjiang silkworm (Bombyx mori). Previous researches have determined the complete amino acid sequence of this molecule [6]. It has been demonstrated that CecropinXJ could be expressed in eukaryotic expression system such as Pichia pastoris [7] or prokaryotic expression system such as E.coli [8]. What’s more, CecropinXJ exhibited to have various activities such as antibacterial activity against both Gram‑positive and Gram-negative bacteria, as well as antifungal activity [8]. These characteristics indicate that CecropinXJ is an ideal antimicrobial substance to be used to treat foot diseases caused by microbes.
 
Cecropins, a group of small AMPs mainly found in the hemolymph of insects, consist of 31 39 amino acid residues and have a broad spectrum, high heat stability and potent bacteriostatic activity [3-5]. CecropinXJ (Part BBa_K1919000) is a member of the Cecropin family, which was first cloned from the larvae of the Xinjiang silkworm (Bombyx mori). Previous researches have determined the complete amino acid sequence of this molecule [6]. It has been demonstrated that CecropinXJ could be expressed in eukaryotic expression system such as Pichia pastoris [7] or prokaryotic expression system such as E.coli [8]. What’s more, CecropinXJ exhibited to have various activities such as antibacterial activity against both Gram‑positive and Gram-negative bacteria, as well as antifungal activity [8]. These characteristics indicate that CecropinXJ is an ideal antimicrobial substance to be used to treat foot diseases caused by microbes.
  
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In recent years, studies concerning the expression of anti¬microbial peptides have mainly focused on the use of fusion partners [9]. For example, Thioredoxin, a heat-stable and low molecular weight soluble protein in the prokaryotic cytoplasm, has been shown to display chaperone like activity [10]. Fusion proteins of antimicrobial peptides generated in E. coli reduce the toxic effect of antimicrobial peptides to the host cells and protect the small antimicrobial peptides from proteolytic degradation.
 
  
 
[1] Boman HG: Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 13: 61-92, 1995.
 
[1] Boman HG: Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 13: 61-92, 1995.
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[6] Li JY, Zhang FC and Ma ZH: Prokaryotic expression of cecropin gene isolated from the silk worm Bombyx mori Xinjiang race and antibacterial activity of fusion cecropin. Acta Entomol Sin 47: 407-411, 2004 (In Chinese).
 
[6] Li JY, Zhang FC and Ma ZH: Prokaryotic expression of cecropin gene isolated from the silk worm Bombyx mori Xinjiang race and antibacterial activity of fusion cecropin. Acta Entomol Sin 47: 407-411, 2004 (In Chinese).
 +
 
[7] Tang X, Wang H, Kelaimu R, Mao XF and Liu ZY: Molecular cloning, expression of cecropin-XJ gene from silkworm and antibacterial activity in Pichia pastoris. Biotechnology 21: 26-31, 2011 (In Chinese).
 
[7] Tang X, Wang H, Kelaimu R, Mao XF and Liu ZY: Molecular cloning, expression of cecropin-XJ gene from silkworm and antibacterial activity in Pichia pastoris. Biotechnology 21: 26-31, 2011 (In Chinese).
 +
 
[8] Xia L, Zhang F, Liu Z, Ma J and Yang J: Expression and characterization of cecropinXJ, a bioactive antimicrobial peptide from Bombyx mori (Bombycidae, Lepidoptera) in Escherichia coli. Experimental and Therapeutic Medicine 5: 1745-1751, 2013.
 
[8] Xia L, Zhang F, Liu Z, Ma J and Yang J: Expression and characterization of cecropinXJ, a bioactive antimicrobial peptide from Bombyx mori (Bombycidae, Lepidoptera) in Escherichia coli. Experimental and Therapeutic Medicine 5: 1745-1751, 2013.
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[9] Zorko M and Jerala R: Production of recombinant antimicrobial peptides in bacteria. Methods Mol Biol 618: 61-76, 2010.
 
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[10] LaVallie ER, Diblasio EA, Kovacic S, Grant KL, Schendel PF and McCoy JM: A thioredoxin gene fusion expression system that circumvents inclusion body formation in E. coli cytoplasm. Biotechnology (NY) 11: 187-193, 1993.
 

Revision as of 15:34, 11 October 2016


The coding sequence of antimicrobial peptide CecropinXJ

Antimicrobial peptide CecropinXJ belongs to AMP family Cecropin, a group of small basic polypeptides mainly found in the hemolymph of insects, consist of 31-39 amino acid residues and have a broad spectrum, high heat stability and potent bacteriostatic activity.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Usage and Biology

Antimicrobial peptides (AMPs) are a group of peptides that play roles in the innate immune system to protect the host from invading pathogens [1]. AMPs have minimal toxicity and low sensitivity effects to the host [2], which means antimicrobial peptides have the potential to be used to replace antibiotics in the future. Thus, the detrimental effects of antibiotics overuse will be released.

Cecropins, a group of small AMPs mainly found in the hemolymph of insects, consist of 31 39 amino acid residues and have a broad spectrum, high heat stability and potent bacteriostatic activity [3-5]. CecropinXJ (Part BBa_K1919000) is a member of the Cecropin family, which was first cloned from the larvae of the Xinjiang silkworm (Bombyx mori). Previous researches have determined the complete amino acid sequence of this molecule [6]. It has been demonstrated that CecropinXJ could be expressed in eukaryotic expression system such as Pichia pastoris [7] or prokaryotic expression system such as E.coli [8]. What’s more, CecropinXJ exhibited to have various activities such as antibacterial activity against both Gram‑positive and Gram-negative bacteria, as well as antifungal activity [8]. These characteristics indicate that CecropinXJ is an ideal antimicrobial substance to be used to treat foot diseases caused by microbes.


[1] Boman HG: Peptide antibiotics and their role in innate immunity. Annu Rev Immunol 13: 61-92, 1995.

[2] Devine DA and Hancock RE: Cationic peptides: distribution and mechanisms of resistance. Curr Pharm Des 8: 703-714, 2002.

[3] Boman HG, Wade D, Boman IA, Wåhlin B and Merrifield RB: Antibacterial and antimalarial properties of peptides that are cecropin-melittin hybrids. FEBS Lett 259: 103-106, 1989.

[4] Moore AJ, Devine DA and Bibby MC: Preliminary experimental anticancer activity of cecropins. Pept Res 7: 265-269, 1994.

[5] Hancock RE and Lehrer R: Cationic peptides: a new source of antibiotics. Trends Biotechnol 16: 82-88, 1998.

[6] Li JY, Zhang FC and Ma ZH: Prokaryotic expression of cecropin gene isolated from the silk worm Bombyx mori Xinjiang race and antibacterial activity of fusion cecropin. Acta Entomol Sin 47: 407-411, 2004 (In Chinese).

[7] Tang X, Wang H, Kelaimu R, Mao XF and Liu ZY: Molecular cloning, expression of cecropin-XJ gene from silkworm and antibacterial activity in Pichia pastoris. Biotechnology 21: 26-31, 2011 (In Chinese).

[8] Xia L, Zhang F, Liu Z, Ma J and Yang J: Expression and characterization of cecropinXJ, a bioactive antimicrobial peptide from Bombyx mori (Bombycidae, Lepidoptera) in Escherichia coli. Experimental and Therapeutic Medicine 5: 1745-1751, 2013.