کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1933803 | 1050625 | 2009 | 6 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: AdDLP, a bacterial defensin-like peptide, exhibits anti-Plasmodium activity AdDLP, a bacterial defensin-like peptide, exhibits anti-Plasmodium activity](/preview/png/1933803.png)
Antimicrobial defensins with the cysteine-stabilized α-helical and β-sheet (CSαβ) motif are widely distributed in three eukaryotic kingdoms. However, recent work suggests that bacteria could possess defensin-like peptides (DLPs). Here, we report recombinant expression, in vitro folding, structural and functional characterization of a DLP from the myxobacterium Anaeromyxobacter dehalogenans (AdDLP). Circular dichroism analysis indicates that recombinant AdDLP adopts a typical structural feature of eukaryotic defensins, which is also consistent with an ab initio structure model predicted using I-TASSER algorithm. We found that AdDLP is an antimalarial peptide that led to more than 50% growth inhibition on sexual stages of Plasmodium berghei at micromolar concentrations and killed 100% intraerythrocytic Plasmodium falciparum at 10 μM in a time-dependent manner. These results provide functional evidence for myxobacterial origin of eukaryotic defensins. High-level production of the pure anti-Plasmodium peptide without harming mammalian red blood cells in Escherichia coli makes AdDLP an interesting candidate for antimalarial drug design.
Journal: Biochemical and Biophysical Research Communications - Volume 387, Issue 2, 18 September 2009, Pages 393–398