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抗菌肽乳铁传递蛋白B和蛙皮素2穿过细菌细胞质膜并存在于细胞质中。

The antimicrobial peptides lactoferricin B and magainin 2 cross over the bacterial cytoplasmic membrane and reside in the cytoplasm.

作者信息

Haukland H H, Ulvatne H, Sandvik K, Vorland L H

机构信息

Department of Medical Microbiology, University Hospital Tromsø, Norway.

出版信息

FEBS Lett. 2001 Nov 23;508(3):389-93. doi: 10.1016/s0014-5793(01)03100-3.

DOI:10.1016/s0014-5793(01)03100-3
PMID:11728458
Abstract

The localization of immunolabelled antimicrobial peptides was studied using transmission electron microscopy. Staphylococcus aureus and Escherichia coli were exposed to lactoferricin B (17-41), lactoferricin B (17-31) and D-lactoferricin B (17-31). E. coli was also exposed to cecropin P1 and magainin 2. The lactoferricins were found in the cytoplasm of both bacteria. In S. aureus the amount of cytoplasmic lactoferricin B (17-41) was time- and concentration-dependent, reaching a maximum within 30 min. Cecropin P1 was confined to the cell wall, while magainin 2 was found in the cytoplasm of E. coli. The finding of intracellularly localized magainin is not reported previously.

摘要

使用透射电子显微镜研究了免疫标记抗菌肽的定位。金黄色葡萄球菌和大肠杆菌分别暴露于乳铁蛋白B(17 - 41)、乳铁蛋白B(17 - 31)和D - 乳铁蛋白B(17 - 31)。大肠杆菌还暴露于天蚕素P1和蛙皮素2。在两种细菌的细胞质中均发现了乳铁蛋白。在金黄色葡萄球菌中,细胞质中乳铁蛋白B(17 - 41)的量呈时间和浓度依赖性,在30分钟内达到最大值。天蚕素P1局限于细胞壁,而蛙皮素2则存在于大肠杆菌的细胞质中。细胞内定位的蛙皮素这一发现此前未见报道。

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