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Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain
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 Nicomache minor in the Maldanidae family. Full-length mRNA sequences encoded 239-res...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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MDPI
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6265681/ https://www.ncbi.nlm.nih.gov/pubmed/30360541 http://dx.doi.org/10.3390/md16110401 |
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author | Panteleev, Pavel V. Tsarev, Andrey V. Bolosov, Ilia A. Paramonov, Alexander S. Marggraf, Mariana B. Sychev, Sergey V. Shenkarev, Zakhar O. Ovchinnikova, Tatiana V. |
author_facet | Panteleev, Pavel V. Tsarev, Andrey V. Bolosov, Ilia A. Paramonov, Alexander S. Marggraf, Mariana B. Sychev, Sergey V. Shenkarev, Zakhar O. Ovchinnikova, Tatiana V. |
author_sort | Panteleev, Pavel V. |
collection | PubMed |
description | 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 Nicomache minor 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 N-terminal α-helix and C-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. |
format | Online Article Text |
id | pubmed-6265681 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-62656812018-12-06 Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain Panteleev, Pavel V. Tsarev, Andrey V. Bolosov, Ilia A. Paramonov, Alexander S. Marggraf, Mariana B. Sychev, Sergey V. Shenkarev, Zakhar O. Ovchinnikova, Tatiana V. Mar Drugs Article 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 Nicomache minor 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 N-terminal α-helix and C-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. MDPI 2018-10-23 /pmc/articles/PMC6265681/ /pubmed/30360541 http://dx.doi.org/10.3390/md16110401 Text en © 2018 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Panteleev, Pavel V. Tsarev, Andrey V. Bolosov, Ilia A. Paramonov, Alexander S. Marggraf, Mariana B. Sychev, Sergey V. Shenkarev, Zakhar O. Ovchinnikova, Tatiana V. Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain |
title | Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain |
title_full | Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain |
title_fullStr | Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain |
title_full_unstemmed | Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain |
title_short | Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain |
title_sort | novel antimicrobial peptides from the arctic polychaeta nicomache minor provide new molecular insight into biological role of the brichos domain |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6265681/ https://www.ncbi.nlm.nih.gov/pubmed/30360541 http://dx.doi.org/10.3390/md16110401 |
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