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Prokaryotic Expression of Reindeer β-defensin-1(reBD-1) Gene and Bioactivity Evaluation

Author: SuLiNa
Tutor: YangYinFeng
School: Inner Mongolia Agricultural University
Course: Basic Veterinary Science
Keywords: Reindeer Defensin Clone Protein expression Antibacterial activity
CLC: Q78
Type: Master's thesis
Year: 2011
Downloads: 28
Quote: 0
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Abstract


Defensins (defensin) are a class of short peptides organisms innate immune system is a family of endogenous antimicrobial peptides . Defensin having a broad spectrum of antibacterial activity , both in intracellular or extracellular can directly kill the bacteria, fungi , viruses and other pathogenic microorganisms , and to maintain the stability of the environment of the machine body , while the cytotoxicity of certain malignant cells . beta - defensin is one of the important members of the defensin family , reindeer β- defensin expression, purification and antibacterial activity has begun a preliminary study . This test is designed to build reindeer β-defensin -1 ( reindeerβ -defensin -1 , reBD -1 ) gene prokaryotic expression vector pET - 32a ( ) / reBD -1 induced reBD-1 fusion protein expressed in E. coli and its expression product of biological activity evaluation . RT-PCR amplified genes coding reBD-1 before the original peptide . Was amplified from recombinant cloning vector pMD-19T/reBD-1 , reBD-1 mature peptide coding sequences , and cloned into pET-32a () in the IPTG induction in the E. coli BL21 (DE3) using reBD-1 fusion protein . The expression of the fusion protein to expand cultivation , further purified in vitro antibacterial experiments . The results showed that the coding reBD - 1 prepro peptide and the mature peptide gene sequence size of 225bp and 138bp, and the desired gene sequence with reBD-1 mRNA is 100% sequence homology . The prepro peptide and the mature peptide fusion protein molecular weight respectively for 28KDa and 24KDa . Agarose diffusion method showed that 0.08 mg / ml of purified mature peptide protein activity of Staphylococcus aureus and Escherichia coli resistant . The results show that the the reBD - prepro peptide and mature peptide fusion protein was highly expressed in E. coli . The activity of the mature peptide fusion protein the Bai Duige Gram-positive and Gram-negative bacteria resistance , before the original peptide fusion protein without antibacterial activity .

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CLC: > Biological Sciences > Molecular Biology > Genetic engineering (genetic engineering)
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