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北极多毛纲动物中的新型抗菌肽为 BRICHOS 结构域的生物学功能提供了新的分子见解。

Novel Antimicrobial Peptides from the Arctic Polychaeta Provide New Molecular Insight into Biological Role of the BRICHOS Domain.

机构信息

M.M. Shemyakin & Yu.A. Ovchinnikov Institute of Bioorganic Chemistry, the Russian Academy of Sciences, Miklukho-Maklaya str. 16/10, 117997 Moscow, Russia.

出版信息

Mar Drugs. 2018 Oct 23;16(11):401. doi: 10.3390/md16110401.

DOI:10.3390/md16110401
PMID:30360541
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC6265681/
Abstract

Endogenous antimicrobial peptides (AMPs) are among the earliest molecular factors in the evolution of animal innate immunity. In this study, novel AMPs named nicomicins were identified in the small marine polychaeta in the Maldanidae family. Full-length mRNA sequences encoded 239-residue prepropeptides consisting of a putative signal sequence region, the BRICHOS domain within an acidic proregion, and 33-residue mature cationic peptides. Nicomicin-1 was expressed in the bacterial system, and its spatial structure was analyzed by circular dichroism and nuclear magnetic resonance spectroscopy. Nicomicins are unique among polychaeta AMPs scaffolds, combining an amphipathic -terminal α-helix and -terminal extended part with a six-residue loop stabilized by a disulfide bridge. This structural arrangement resembles the Rana-box motif observed in the α-helical host-defense peptides isolated from frog skin. Nicomicin-1 exhibited strong in vitro antimicrobial activity against Gram-positive bacteria at submicromolar concentrations. The main mechanism of nicomicin-1 action is based on membrane damage but not on the inhibition of bacterial translation. The peptide possessed cytotoxicity against cancer and normal adherent cells as well as toward human erythrocytes.

摘要

内源性抗菌肽（AMPs）是动物先天免疫进化过程中的最早的分子因素之一。在这项研究中，在小的海洋多毛纲环节动物Maldanidae 科中发现了新型 AMP，命名为nicomicin。全长 mRNA 序列编码 239 个残基的前原肽，包括一个假定的信号序列区域、酸性前区的 BRICHOS 结构域和 33 个残基的成熟阳离子肽。Nicomicin-1 在细菌系统中表达，并通过圆二色性和核磁共振波谱分析其空间结构。Nicomicin 在多毛纲 AMP 支架中是独特的，它结合了一个两亲性的 - 端 α-螺旋和 - 端扩展部分，带有一个由二硫键稳定的六个残基环。这种结构排列类似于从蛙皮中分离出的α-螺旋宿主防御肽中观察到的 Rana-box 基序。Nicomicin-1 在体外对革兰氏阳性菌具有很强的抗微生物活性，其浓度在亚微摩尔范围内。Nicomicin-1 的主要作用机制是基于膜损伤，而不是抑制细菌翻译。该肽对癌细胞和正常贴壁细胞以及人红细胞均具有细胞毒性。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/00e5de01c4f5/marinedrugs-16-00401-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/7086b4a328ef/marinedrugs-16-00401-g001.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/caa8fff56813/marinedrugs-16-00401-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/3d5ddcd262bc/marinedrugs-16-00401-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/753aee12b6e5/marinedrugs-16-00401-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/65b1e5aa4faa/marinedrugs-16-00401-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/486bb1a86d18/marinedrugs-16-00401-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/00e5de01c4f5/marinedrugs-16-00401-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/7086b4a328ef/marinedrugs-16-00401-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/ea2e919ae22a/marinedrugs-16-00401-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/fba05a0b63ec/marinedrugs-16-00401-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/caa8fff56813/marinedrugs-16-00401-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/3d5ddcd262bc/marinedrugs-16-00401-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/753aee12b6e5/marinedrugs-16-00401-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/65b1e5aa4faa/marinedrugs-16-00401-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/486bb1a86d18/marinedrugs-16-00401-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/481a/6265681/00e5de01c4f5/marinedrugs-16-00401-g009.jpg

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