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检测抗菌肽-2 的抗菌机制。

Imaging the antimicrobial mechanism(s) of cathelicidin-2.

机构信息

Department of Infectious Diseases and Immunology, Division Molecular Host Defence, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.

Department of Cell Biology, Cell Microscopy Core, University Medical Centre Utrecht, Utrecht, The Netherlands.

出版信息

Sci Rep. 2016 Sep 14;6:32948. doi: 10.1038/srep32948.

DOI:10.1038/srep32948
PMID:27624595
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5021996/
Abstract

Host defence peptides (HDPs) have the potential to become alternatives to conventional antibiotics in human and veterinary medicine. The HDP chicken cathelicidin-2 (CATH-2) has immunomodulatory and direct killing activities at micromolar concentrations. In this study the mechanism of action of CATH-2 against Escherichia coli (E. coli) was investigated in great detail using a unique combination of imaging and biophysical techniques. Live-imaging with confocal fluorescence microscopy demonstrated that FITC-labelled CATH-2 mainly localized at the membrane of E. coli. Upon binding, the bacterial membrane was readily permeabilized as was shown by propidium iodide influx into the cell. Concentration- and time-dependent effects of the peptide on E. coli cells were examined by transmission electron microscopy (TEM). CATH-2 treatment was found to induce dose-dependent morphological changes in E. coli. At sub-minimal inhibitory concentrations (sub-MIC), intracellular granulation, enhanced vesicle release and wrinkled membranes were observed, while membrane breakage and cell lysis occurred at MIC values. These effects were visible within 1-5 minute of peptide exposure. Immuno-gold TEM showed CATH-2 binding to bacterial membranes. At sub-MIC values the peptide rapidly localized intracellularly without visible membrane permeabilization. It is concluded that CATH-2 has detrimental effects on E. coli at concentrations that do not immediately kill the bacteria.

摘要

宿主防御肽 (HDPs) 有可能成为人类和兽医医学中传统抗生素的替代品。HDP 鸡 cathelicidin-2 (CATH-2) 在微摩尔浓度下具有免疫调节和直接杀伤活性。在这项研究中，使用独特的成像和生物物理技术组合，详细研究了 CATH-2 对大肠杆菌 (E. coli) 的作用机制。用共聚焦荧光显微镜进行的实时成像表明，FITC 标记的 CATH-2 主要定位于大肠杆菌的膜上。结合后，细菌膜很容易被渗透，如碘化丙啶进入细胞所示。通过透射电子显微镜 (TEM) 检查了肽对大肠杆菌细胞的浓度和时间依赖性影响。发现 CATH-2 处理会诱导大肠杆菌的剂量依赖性形态变化。在亚最小抑菌浓度 (sub-MIC) 下，观察到细胞内颗粒形成、增强的囊泡释放和皱缩的膜，而在 MIC 值时则发生膜破裂和细胞裂解。这些影响在肽暴露后 1-5 分钟内可见。免疫金 TEM 显示 CATH-2 与细菌膜结合。在 sub-MIC 值下，肽迅速在细胞内定位，而没有明显的膜渗透。结论是，在不会立即杀死细菌的浓度下，CATH-2 对大肠杆菌有不良影响。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/1465f48924b1/srep32948-f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/417d5e2b13ed/srep32948-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/a29337fcb758/srep32948-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/92cca42d355b/srep32948-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/353791b101ad/srep32948-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/3863034bdaf0/srep32948-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/12f04ce9f63f/srep32948-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/1465f48924b1/srep32948-f7.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/417d5e2b13ed/srep32948-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/a29337fcb758/srep32948-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/92cca42d355b/srep32948-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/353791b101ad/srep32948-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/3863034bdaf0/srep32948-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/12f04ce9f63f/srep32948-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/55c2/5021996/1465f48924b1/srep32948-f7.jpg

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