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Fusion expression of the PGLa-AM1 with native structure and evaluation of its anti-<Emphasis Type="Italic">Helicobacter pylori</Emphasis> activity
Authors:Email author" target="_blank">Xiaolin?ZhangEmail author  Anmin?Jiang  Guisheng?Wang  Hao?Yu  Banghua?Qi  Youyi?Xiong  Guoliang?Zhou  Meisong?Qin  Jinfeng?Dou  Email author" target="_blank">Jianfei?WangEmail author
Institution:1.The Department of Pharmacy, Food and Drug School,Anhui Science and Technology University,Fengyang,China;2.The School of Life Science,University of Science and Technology of China,Hefei,China;3.Biology and Food Engineering School,Fuyang Normal University,Fuyang,China;4.The Ministry of Agriculture Key Laboratory of Microbial Organic Fertilizer,Bengbu,China
Abstract:Helicobacter pylori (H. pylori) shows increasingly enhanced resistance to various antibiotics, and its eradication has become a major problem in medicine. The antimicrobial peptide PGLa-AM1 is a short peptide with 22 amino acids and exhibits strong antibacterial activity. In this study, we investigated whether it has anti-H. pylori activity for the further development of anti-H. pylori drugs to replace existing antibiotics. However, the natural antimicrobial peptide PGLa-AM1 shows a low yield and is difficult to separate, limiting its application. A good strategy to solve this problem is to express the antimicrobial peptide PGLa-AM1 using gene engineering at a high level and low cost. For getting PGLa-AM1 with native structure, in this study, a specific protease cleavage site of tobacco etch virus (TEV) was designed before the PGLa-AM1 peptide. For convenience to purify and identify high-efficiency expression PGLa-AM1, the PGLa-AM1 gene was fused with the polyhedrin gene of Bombyx mori (B. mori), and a 6 × His tag was designed to insert before the amino terminus of the fusion protein. The fusion antibacterial peptide PGLa-AM1 (FAMP) gene codon was optimized, and the gene was synthesized and cloned into the Escherichia coli (E. coli) pET-30a (+) expression vector. The results showed that the FAMP was successfully expressed in E. coli. Its molecular weight was approximately 34 kDa, and its expression level was approximately 30 mg/L. After the FAMP was purified, it was further digested with TEV protease. The acquired recombinant antimicrobial peptide PGLa-AM1 exerted strong anti-H. pylori activity and therapeutic effect in vitro and in vivo.
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