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本文引用的文献

1
Resistance to antimicrobial peptides in Gram-negative bacteria.革兰氏阴性菌对抗菌肽的耐药性。
FEMS Microbiol Lett. 2012 May;330(2):81-9. doi: 10.1111/j.1574-6968.2012.02528.x. Epub 2012 Mar 12.
2
α-Defensins in human innate immunity.α-防御素在人体先天免疫中的作用。
Immunol Rev. 2012 Jan;245(1):84-112. doi: 10.1111/j.1600-065X.2011.01082.x.
3
OmpT outer membrane proteases of enterohemorrhagic and enteropathogenic Escherichia coli contribute differently to the degradation of human LL-37.肠出血性和肠致病性大肠杆菌的 OmpT 外膜蛋白酶对人 LL-37 的降解作用不同。
Infect Immun. 2012 Feb;80(2):483-92. doi: 10.1128/IAI.05674-11. Epub 2011 Dec 5.
4
Enteropathogenic and enterohaemorrhagic Escherichia coli: even more subversive elements.肠致病性和肠出血性大肠杆菌:更具颠覆性的因子。
Mol Microbiol. 2011 Jun;80(6):1420-38. doi: 10.1111/j.1365-2958.2011.07661.x. Epub 2011 May 5.
5
Paneth cells, antimicrobial peptides and maintenance of intestinal homeostasis.潘氏细胞、抗菌肽与肠道内稳态的维持。
Nat Rev Microbiol. 2011 May;9(5):356-68. doi: 10.1038/nrmicro2546. Epub 2011 Mar 22.
6
Gingipains produced by Porphyromonas gingivalis ATCC49417 degrade human-β-defensin 3 and affect peptide's antibacterial activity in vitro.牙龈卟啉单胞菌 ATCC49417 产生的gingipains 降解人β-防御素 3 并影响肽的体外抗菌活性。
Peptides. 2011 May;32(5):1073-7. doi: 10.1016/j.peptides.2011.02.003. Epub 2011 Feb 16.
7
Reduction of disulphide bonds unmasks potent antimicrobial activity of human β-defensin 1.二硫键的还原使人类β防御素 1 表现出强大的抗菌活性。
Nature. 2011 Jan 20;469(7330):419-23. doi: 10.1038/nature09674.
8
An outer membrane protease of the omptin family prevents activation of the Citrobacter rodentium PhoPQ two-component system by antimicrobial peptides.奥普汀家族的一种外膜蛋白酶可防止抗菌肽激活鼠柠檬酸杆菌PhoPQ双组分系统。
Mol Microbiol. 2009 Oct;74(1):98-111. doi: 10.1111/j.1365-2958.2009.06854.x. Epub 2009 Aug 24.
9
Burkholderia cenocepacia zinc metalloproteases influence resistance to antimicrobial peptides.洋葱伯克霍尔德菌锌金属蛋白酶影响对抗菌肽的抗性。
Microbiology (Reading). 2009 Sep;155(Pt 9):2818-2825. doi: 10.1099/mic.0.028969-0. Epub 2009 Jun 18.
10
VirB alleviates H-NS repression of the icsP promoter in Shigella flexneri from sites more than one kilobase upstream of the transcription start site.VirB可从转录起始位点上游超过1千碱基的位点缓解弗氏志贺氏菌中H-NS对icsP启动子的抑制作用。
J Bacteriol. 2009 Jun;191(12):4047-50. doi: 10.1128/JB.00313-09. Epub 2009 Apr 10.

肠出血性和肠致病性大肠杆菌进化出不同的策略来抵抗抗菌肽。

Enterohemorrhagic and enteropathogenic Escherichia coli evolved different strategies to resist antimicrobial peptides.

机构信息

Department of Microbiology and Immunology, McGill University, Montreal, QC, Canada.

出版信息

Gut Microbes. 2012 Nov-Dec;3(6):556-61. doi: 10.4161/gmic.21656. Epub 2012 Aug 16.

DOI:10.4161/gmic.21656
PMID:22895086
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3495793/
Abstract

Enterohemorrhagic and enteropathogenic Escherichia coli (EHEC and EPEC) are enteric human pathogens that colonize the large and small intestines, respectively. To establish infection EHEC and EPEC must overcome innate host defenses, such as antimicrobial peptides (AMPs) produced by the intestinal epithelium. Gram-negative pathogens have evolved different mechanisms to resist AMPs, including outer-membrane proteases that degrade AMPs. We showed that the protease OmpT degrades the human AMP LL-37 more rapidly in EHEC than in EPEC. Promoter-swap experiments showed that this is due to differences in the promoters of the two genes, leading to greater ompT expression and subsequently greater levels of OmpT in EHEC. Here, we propose that the different ompT expression in EHEC and EPEC reflects the varying levels of LL-37 throughout the human intestinal tract. These data suggest that EHEC and EPEC adapted to their specific niches by developing distinct AMP-specific resistance mechanisms.

摘要

肠出血性和肠致病性大肠杆菌(EHEC 和 EPEC)分别是定植于大肠和小肠的肠道人类病原体。为了建立感染,EHEC 和 EPEC 必须克服先天的宿主防御,例如由肠道上皮细胞产生的抗菌肽(AMPs)。革兰氏阴性病原体已经进化出不同的机制来抵抗 AMPs,包括降解 AMPs 的外膜蛋白酶。我们表明,蛋白酶 OmpT 在 EHEC 中比在 EPEC 中更快地降解人类 AMP LL-37。启动子交换实验表明,这是由于两个基因的启动子存在差异,导致 EHEC 中 ompT 的表达更高,随后 OmpT 的水平更高。在这里,我们提出 EHEC 和 EPEC 中不同的 ompT 表达反映了人类肠道中 LL-37 的不同水平。这些数据表明,EHEC 和 EPEC 通过开发独特的 AMP 特异性抗性机制来适应其特定的生态位。