期刊文献+

细菌毒力与β-内酰胺类抗生素耐药的相关性 被引量:6

Relativity Between Bacterial Virulence Factors and Beta-lactam Antibiotic Resistance
下载PDF
导出
摘要 抗生素的出现阻碍了致病菌的传播,但随着抗生素的广泛使用,细菌的耐药性问题越来越严重,给临床治疗带来巨大困难。细菌对β-内酰胺类抗生素的耐药问题已经引起广泛重视。致病菌能够在动物机体内定植、入侵并破坏机体的免疫系统,最终引起动物的发病,往往与其含有的毒力因子有关。近年来,随着研究的不断深入,人们发现细菌毒力的变化与其耐药性之间存在一定的关系。论文主要针对细菌的β-内酰胺类抗生素耐药和毒力之间的关系进行综述。 Antibiotics is essential in controlling infection caused by bacteria,unfortunately,the resistance of bacteria has emerged because of its extensive use,especially in beta-lactam antibiotics,which lead to a significant clinical problem worldwide in treating infections caused by bacteria.Virulence factors play a cru-cial role in its pathogenicity,particularly in permanent planting and invasion of the immune system in ani-mals.The recent studies indicated that there was a link between virulence factors and antibiotic resistance in bacteria.In this paper,the connection between virulence factors and beta-lactam antibiotic resistance were discussed.
出处 《动物医学进展》 CSCD 北大核心 2014年第9期106-109,共4页 Progress In Veterinary Medicine
基金 国家自然科学基金项目(31201954)
关键词 耐药性 毒力 Β-内酰胺类抗生素 细菌 resistance virulence β-lactam antibiotics bacteria
  • 相关文献

参考文献4

二级参考文献72

  • 1周坚芬,张永信.青霉素结合蛋白研究进展[J].国外医药(抗生素分册),1996,17(3):192-195. 被引量:5
  • 2Lim D, Strynadka N C J. Structural basis for the 13-1actam resis- tance of PBP2a from methicillin-resistant Staphylococcus aureus [J]. Nat Struct Biol, 2002, 9(11): 870-876.
  • 3Hakenbeck R, Coyette J. Resistant penicillin-binding proteins [J]. Cell Mol Life Sci, 1998, 54(4): 332-340.
  • 4Arbeloa A, Segal H, Hugonnet J E, et al. Role of class A peni- cillin-binding proteins in PBP5-mediated beta-lactam resistance in Enterococcus faecalis [J]. J Bacteriol, 2004, 186(5): 1221- 1228.
  • 5Henry X, Amoroso A, Coyette J, et al. Interaction of ceftobiprole with the low-affinity PBP 5 of Enterococcus faecium [J]. Anti- microb Agents Chemother, 2010, 54(2): 953-955.
  • 6Korsak D, Markiewicz Z, Gutkind G O, et al. Identification of the full set of Listeria mocytogenes penicillin-binding proteins and characterization of PBPD2 (Lmo2812) [J]. BMC Microbiol, 2010, 10: 239-245.
  • 7Philippe N, Pelosi L, Lenski R E, et al. Evolution of peni- cillin-binding protein 2 concentration and cell shape during a long-term experiment with Escherichia coli [J]. J Bacteriol, 2009, 191(3): 909-921.
  • 8Nicola G, Tomberg J, Pratt R F, et al. Crystal structures of covalent complexes of 13-1actam antibiotics with Escherichia coli penicillin-binding protein 5: toward an understanding of antibiotic specificity I-J]. Biochemistry, 2010, 49(37): 8094-8104.
  • 9Chowdhury C, Nayak T R, Young K D, et al. A weak DD-car- boxypeptidase activity explains the inability of PBP 6 to substi- tute for PBP 5 in maintaining normal cell shape in Escherichia coli [J]. FEMS Microbiol Lett, 2010, 303(1): 76-83.
  • 10Sauvage E, Kerff F, Fonze E, et al. The 2.4-A crystal structure of the penicillin-resistant penicillin-binding protein PBP5fm from Enterococcus faecium in complex with benzylpenicillin [J]. Cell Mol Life Sci, 2002, 59(7): 1223-1232.

共引文献46

同被引文献34

引证文献6

二级引证文献31

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