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首页> 外文期刊>Biochemistry >Entry of a Six-Residue Antimicrobial Peptide Derived from Lactoferricin B into Single Vesicles and Escherichia coli Cells without Damaging their Membranes
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Entry of a Six-Residue Antimicrobial Peptide Derived from Lactoferricin B into Single Vesicles and Escherichia coli Cells without Damaging their Membranes

机译：将六残基抗微生物肽的进入衍生自Lactoferricin B的六核抗菌肽成单个囊泡和大肠杆菌细胞，而不会损坏它们的膜

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摘要

Lactoferricin B (LfcinB) and shorter versions of this peptide have antimicrobial activity. However, the elementary processes of interactions of these peptides with lipid membranes and bacteria are still not well understood. To elucidate the mechanism of their antimicrobial activity, we investigated the interactions of LfcinB (4-9) (its sequence of RRWQWR) with Escherichia coli cells and giant unilamellar vesicles (GUVs). LfcinB (4-9) and lissamine rhodamine B red-labeled LfcinB (4-9) (Rh-LfcinB (4-9)) did not induce an influx of a membrane-impermeant fluorescent probe, SYTOX green, from the outside of E. coli cells into their cytoplasm, indicating that no damage occurred in their plasma membrane. To examine the activity of LfcinB (4-9) to enter E. coli cytoplasm, we investigated the interaction of Rh-LfcinB (4-9) with single cells of E. coli containing calcein using confocal microscopy. We found that Rh-LfcinB (4-9) entered the cytoplasm without leakage of calcein. Next, we investigated the interactions of Rh-LfcinB (4-9) with single GUVs of dioleoylphosphatidylglycerol (DOPG) and dioleoylphosphatidylcholine (DOPC) mixtures containing a fluorescent probe, Alexa Fluor 647 hydrazide (AF647), using the single GUV method. The results indicate that Rh-LfcinB (4-9) outside the GUV translocated through the GUV membrane and entered its lumen without leakage of AF647. Interaction of Rh-LfcinB (4-9) with DNA increased its fluorescence intensity greatly. Therefore, we can conclude that Rh-LfcinB (4-9) can translocate across lipid membrane regions of the plasma membrane of E. coli cells to enter their cytoplasm without leakage of calcein and its antimicrobial activity is not due to damage of their plasma membranes.
机译：Lactoferricin B（LFCINB）和该肽的较短版本具有抗微生物活性。然而，这些肽与脂质膜和细菌相互作用的基本方法仍未得到很好的理解。为了阐明其抗微生物活性的机制，我们研究了LFCINB（4-9）（其RRWQWR）与大肠杆菌细胞和巨型Unilamellar囊泡（GUV）的相互作用。 LFCINB（4-9）和Lissamine Rhodamine B红色标记的LFCINB（4-9）（RH-LFCINB（4-9））没有诱导膜 - 缺乏荧光探针，Sytox Green的流入，从E外面。COLI细胞进入其细胞质，表明在其血浆膜中没有损伤。为了检查LFCINB（4-9）的活性进入大肠杆菌细胞质，我们使用共聚焦显微镜研究了rh-lfcinb（4-9）与含有Calcein的单细胞的单细胞的相互作用。我们发现RH-LFCINB（4-9）进入细胞质而不会泄漏Calcein。接下来，我们研究了用单一GUV法，用含有荧光探针，荧光探针（AF647）的二氧酰基磷脂酰甘油（DOPO）和二酰磷脂酰胆碱（DOPC）混合物的单射GUV的rH-LFCINB（4-9）的相互作用。结果表明，GUV外部的RH-LFCINB（4-9）通过GUV膜转移，并在没有AF647泄漏的情况下进入其腔。 RH-LFCINB（4-9）与DNA的相互作用大大增加了荧光强度。因此，我们可以得出结论，rh-lfcinb（4-9）可以穿过大肠杆菌细胞的质膜的脂质膜区域易转化，以进入它们的细胞质而不会泄漏唇肠，其抗微生物活性不是由于它们的血浆膜的损伤。

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  • 来源
    《Biochemistry》 |2017年第33期|共13页
  • 作者

    Moniruzzarnan Md.; Islam Md. Zahidul; Sharmin Sabrina; Dohra Hideo; Yamazaki Masahito;

  • 作者单位

    Shizuoka Univ Integrated Biosci Sect Grad Sch Sci &

    Technol Shizuoka 4228529 Japan;

    Shizuoka Univ Integrated Biosci Sect Grad Sch Sci &

    Technol Shizuoka 4228529 Japan;

    Shizuoka Univ Integrated Biosci Sect Grad Sch Sci &

    Technol Shizuoka 4228529 Japan;

    Shizuoka Univ Instrumental Res Support Off Res Inst Green Sci &

    Technol Shizuoka 4228529 Japan;

    Shizuoka Univ Integrated Biosci Sect Grad Sch Sci &

    Technol Shizuoka 4228529 Japan;

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  • 正文语种 eng
  • 中图分类 生物化学;
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