期刊文献+

细胞型朊蛋白抑菌活性的初步探索 被引量:1

Tentative Exploring of Antibacterial Activity of Cellular Prion Protein
在线阅读 下载PDF
导出
摘要 目的:研究细胞型朊蛋白(PrP^c)有无抑菌活性。方法:把Pr Pc分别与金黄色葡萄球菌、枯草芽孢杆菌、巨大芽孢杆菌、苏云金芽孢杆菌、大肠杆菌等5种菌孵育一定时间,然后用碘化丙锭对上述5种样品染色后采用流式细胞仪检测各样品的荧光信号。结果:通过对流式细胞仪的荧光信号进行分析,发现PrP^c对金黄色葡萄球菌和枯草芽孢杆菌具有明显的抑制活性,而另外3种菌的样品没有检测到荧光信号的增强,亦即PrP^c对这3种菌无抑菌活性。结论:细胞型朊蛋白有一定的抑菌活性,有望成为一种新型的抗菌肽。 Objective: To study the antibacterial activity of cellular prion protein(Pr Pc). Methods: Incubated Pr Pc with the five randomly selected bacteria, Staphylococcus aureus, Bacillus subtilis, B.megaterium, B.thuringiensis and Escherichia coli BL-21 respectively for a period, then dyed the five sample with propidium iodide respectively fora certain time and detected the fluorescence signal of the five sample with flow cytometer ultimately. Results:The fluorescence signals of the five sample indicated that Pr Pchave visible antibacterial effect on S.aureus and B.subtilis, but enhanced fluorescence signals of the other three bacteria were not detected, so Pr Pchave no distinctantibacterial activity towards the other three bacteria. Conclusion: Cellular prion protein have a certain degree ofantibacterial activity, and it is expected to become a new type of antibacterial peptide.
出处 《生物技术通讯》 CAS 2016年第2期257-259,共3页 Letters in Biotechnology
关键词 细胞型朊蛋白 抑菌活性 抗菌肽 荧光信号 cellular prion protein antibacterial activity antimicrobial peptides fluorescence signal
作者简介 王立娟(1981-),女,讲师,硕士,通信作者:王立娟,(E-mail)wlj.wang@163.com
  • 相关文献

参考文献20

  • 1Williams K J, Bax R P. Challenges in developing new anti bacterial drugs[J]. Curr Opin Invest Drugs, 2009,10(2):157- 163.
  • 2Boman H G. Antibacterial peptides:key components needed in hnmunity[J]. Cell, 1991,65(2):205-207.
  • 3Nguyen L T, Haney E F, Vogel H J. The expanding scope of antimicrobial peptide structures and their modes of action [J]. Trends Biotechnol, 2011,29(9):464-472.
  • 4Jenssen H, Hamill P, Hancock R E W. Peptide agents[J]. Clin Microbiol Rev, 2006,19(3):491-511.
  • 5许若丹,钟理,张伟,柳伟强,牛建章.阳离子抗菌肽结构与抗菌活性的关系[J].中国公共卫生,2005,21(9):1141-1143. 被引量:9
  • 6Haneoek R E W, Sahl H G. Antimierobial and host-defense peptides as new anti-infective therapeutic strategies[J]. Nat Bioteehnol, 2006,24(12):1551-1557.
  • 7张杰,路伟,刘永生.细胞型朊蛋白(PrP^c)研究进展[J].中国人兽共患病学报,2008,24(1):83-86. 被引量:5
  • 8Simone A D, Dodson G G, Fraternali F, et al. Water mole- cules as structural determinants among prions of low se- quence identity[J]. FEBS Lett, 2006,580(10):2488-2494.
  • 9Martins V R, Linden R, Prado M A M, et al. Cellular prion pvtein:on the road for functions[J]. FEBS Lett, 2002,512(1): 25-28.
  • 10Westergard L, Christensen H M, Harris D A. The cellular pri- ori protein(PrP':): its physiological function and role in disease [J]. Biochim Biophys Acta, 2007,1772(6):629-644.

二级参考文献66

  • 1Qian S,Wang W,Yang L,et al.Structure of transmembrane pore induced by Bax-derived peptide:evidence for lipidic pores.Proc Natl Acad Sci USA,2008,105:17379-17383.
  • 2Sugawara M,Resende JM,Moraes CM,et al.Membrane structure and interactions of human catestatin by multidimensional solution and solid-state NMR spectroscopy.Faseb J,2010,24:1737-1746.
  • 3Palffy R,Gardlik R,Behuliak M,et al.On the physiology and pathophysiology of antimicrobial peptides.Mol Med,2009,15:51-59.
  • 4Resende JM,Moraes CM,Munhoz VH,et al.Membrane structure and conformational changes of the antibiotic heterodimeric peptide distinctin by solid-state NMR spectroscopy.Proc Natl Acad Sci USA,2009,106:16639-16644.
  • 5Bolintineanu D,Hazrati E,Davis HT,et al.Antimicrobial mechanism of pore-forming protegrin peptides:100 pores to kill E.coli.Peptides,2009,31:1-8.
  • 6Giuliani A,Pirri G,Bozzi A,et al.Antimicrobial peptides:natural templates for synthetic membrane-active compounds.Cell Mol Life Sci,2008,65:2450-2460.
  • 7Brogden KA.Antimicrobial peptides:pore formers or metabolic inhibitors in bacteria? Nat Rev Microbiol,2005,3:238-250.
  • 8Uyterhoeven ET,Butler CH,Ko D,et al.Investigating the nucleic acid interactions and antimicrobial mechanism of buforin II.FEBS Lett,2008,582:1715-1718.
  • 9Porcelli F,Verardi R,Shi L,et al.NMR structure of the cathelicidin-derived human antimicrobial peptide LL-37 in dodecylphosphocholine micelles.Biochemistry,2008,47:5565-5572.
  • 10Anbanandam A,Albarado DC,Tirziu DC,et al.Molecular basis for proline-and arginine-rich peptide inhibition of proteasome.J Mol Biol,2008,384:219-227.

共引文献33

同被引文献13

引证文献1

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部