| 技术与方法 |
|
|
|
|
| 5’非翻译区序列改建提高抗菌肽PR39表达 |
| 明飞平1,2, 杨军1, 朱进美1, 邝哲师3, 李华周4, 夏枫耿2, 叶明强3, 王候光4, 赵祥杰3, 黄志丰1, 蔡海明1, 施巨清1, 马苗鹏1, 张玲华1 |
1. 华南农业大学生命科学学院 广东省农业生物蛋白质功能与调控重点实验室 广州 510642;
2. 广州市微生物研究所 广州 510663;
3. 广东省农科院农业生物技术研究所 广州 510642;
4. 广州市良种猪场 广州 510540 |
|
| Modification of 5’UTR Sequences of pPIC9K Increases Expression of Antimicrobial Peptide PR39 |
| MING Fei-ping1,2, YANG Jun1, ZHU Jin-mei1, KUANG Zhe-shi3, LI Hua-zhou4, XIA Feng-geng2, YE Ming-qiang3, WANG Hou-guang4, ZHAO Xiang-jie3, HUANG Zhi-feng1, MA Miao-peng1, SHI Ju-qing1, CAI Hai-ming1, ZHANG Ling-hua1 |
1. College of Life Science, South China Agricultural University, Guangdong Provincial Key Laboratory of Protein Function and Regulation in Agricultural Organisms, Guangzhou 510642, China;
2. Guangzhou Institute of Microbiology, Guangzhou 510663, China;
3. Bio-Tech Research Institute, Guangdong Academy of Agricultural Sciences, Guangzhou 510640, China;
4. Guangzhou Fine Breed Swine Farm, Guangzhou 510540, China |
引用本文:
明飞平, 杨军, 朱进美, 邝哲师, 李华周, 夏枫耿, 叶明强, 王候光, 赵祥杰, 黄志丰, 蔡海明, 施巨清, 马苗鹏, 张玲华. 5’非翻译区序列改建提高抗菌肽PR39表达[J]. 中国生物工程杂志, 2013, 33(12): 86-91.
MING Fei-ping, YANG Jun, ZHU Jin-mei, KUANG Zhe-shi, LI Hua-zhou, XIA Feng-geng, YE Ming-qiang, WANG Hou-guang, ZHAO Xiang-jie, HUANG Zhi-feng, MA Miao-peng, SHI Ju-qing, CAI Hai-ming, ZHANG Ling-hua. Modification of 5’UTR Sequences of pPIC9K Increases Expression of Antimicrobial Peptide PR39. China Biotechnology, 2013, 33(12): 86-91.
链接本文:
https://manu60.magtech.com.cn/biotech/CN/
或
https://manu60.magtech.com.cn/biotech/CN/Y2013/V33/I12/86
|
[1] Daly R, Hearn M T, et al.Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. Journal of Molecular Recognition, 2004, 18(2):119-138.
[2] LU Jian rong, WANG Hui min, WU Ping, et al.Modificaion of 5'UTR sequences of pPIC9 increases expression of antimicrobial peptide LL-37. Academic Journal of Second Military, 2007, 28(12):1329-1334.
[3] Sreekrishna K, Brankamp R G, Kropp K E, et al. Strategies for optimal synthesis and secretion of heterologous proteins in the methyotrophic yeast Pichia pastoris.Gene, 1997, 190:55-62.
[4] Ren Hai qing. Expression of porcine β-Defensin-1 gene in Pichia pastoris.Harbin: Northeast Agricultural University, 2009.
[5] Liu De hui, He jun, Lin yun xiong, et al. Expression of antimicrobial peptide LL-37 in Pichia pastoris SMD1168 and activity identification. Chinese Journal of Preventive Veterinary Medicine, 2010, 32(2): 98-101.
[6] Agerberth B, Lee J Y, Bergman T, et al.Amino acid sequence of PR-39: Isolation from pig intestine of a new member of the family of proline-arginine-rich antibacterial peptides. Eur J Biochem, 1991, 202:849-850.
[7] Hoekema A, Kastelein R A, Vasser M, et al. Codon replacement in the PGK1 gene of Saccharomyces cerevisiae: experimental approach to study the role of biased codon usage in gene expression. Mol Cell Biol, 1987, 7(8):2914-2924.
[8] Herbert S, Bera A, Nerz C, et al. Molecular basis of resistance to muramidase and cationic antimicrobial peptide activity of lysozyme in staphylococci. PLoS Pathog, 2007, 3(7): 0981-0994.
[9] Hilpert K, Hancock R E. Use of luminescent bacteria for rapid screening and characterization of short cationic antimicrobial peptides synthesized on cellulose using peptide array technology. Nat Protoc, 2007, 2(7):1652-1660.
[10] Boman H G, Agerberth B, Boman A, et al. Mechanisms of action on Escherichia coli of cecropin-P1 and PR-39, two antibacterial peptides from pig intestine.Infect Immun, 1993, 61(7):2978-2984.
[11] Vunnam S, Juvvadi P, Memifield R B, et al. Synthesis and antibacterial action of cecropin and proline-arginine-rich peptides from pig intestine. J Pept Res, 1997, 49(1):59-66.
[12] Linde C M, Hoffner S E, Refai E, et al. In vitro activity of PR-39, a proline-arginine-rich peptide, against susceptible and multi-drug-resistant Mycobacterium tuberculosis. J Antimicrob Chemother, 2001, 47(5):575-580.
[13] Yasuhiko. PR-39, a proline/argine-rich antimicrobial peptide, exerts cardioprotective effects in myocardial is chemia-reperfusion. Cardiovascular Research, 2001, (49): 69-77.
[14] Hocquellet A, Odaert B, Cabanne C, et al. Structure-activity relationship of human liver-expressed antimicrobial peptide 2. Peptides, 2010, 31(1):58-66.
[15] Howard A, Townes C, Milona P, et al. Expression and functional analyses of liver expressed antimicrobial peptide-2 (LEAP-2) variant forms in human tissues.Cell Immunol, 2010, 261(2):128-133. |
|
Viewed |
|
|
|
Full text
|
|
|
|
|
Abstract
|
|
|
|
|
Cited |
|
|
|
|
| |
Shared |
|
|
|
|
| |
Discussed |
|
|
|
|
