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...
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ftdoajarticles:oai:doaj.org/article:e3a4b196616f4f168594bc7a74ab3c5c 2023-05-15T15:07:10+02:00 Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain Pavel V. Panteleev Andrey V. Tsarev Ilia A. Bolosov Alexander S. Paramonov Mariana B. Marggraf Sergey V. Sychev Zakhar O. Shenkarev Tatiana V. Ovchinnikova 2018-10-01T00:00:00Z https://doi.org/10.3390/md16110401 https://doaj.org/article/e3a4b196616f4f168594bc7a74ab3c5c EN eng MDPI AG https://www.mdpi.com/1660-3397/16/11/401 https://doaj.org/toc/1660-3397 1660-3397 doi:10.3390/md16110401 https://doaj.org/article/e3a4b196616f4f168594bc7a74ab3c5c Marine Drugs, Vol 16, Iss 11, p 401 (2018) antimicrobial peptide polychaeta innate immunity BRICHOS domain recombinant peptide α-helix Rana-box nuclear magnetic resonance (NMR) Biology (General) QH301-705.5 article 2018 ftdoajarticles https://doi.org/10.3390/md16110401 2022-12-30T23:59:34Z 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. Article in Journal/Newspaper Arctic Directory of Open Access Journals: DOAJ Articles Arctic Marine Drugs 16 11 401 |
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Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
antimicrobial peptide polychaeta innate immunity BRICHOS domain recombinant peptide α-helix Rana-box nuclear magnetic resonance (NMR) Biology (General) QH301-705.5 |
spellingShingle |
antimicrobial peptide polychaeta innate immunity BRICHOS domain recombinant peptide α-helix Rana-box nuclear magnetic resonance (NMR) Biology (General) QH301-705.5 Pavel V. Panteleev Andrey V. Tsarev Ilia A. Bolosov Alexander S. Paramonov Mariana B. Marggraf Sergey V. Sychev Zakhar O. Shenkarev Tatiana V. Ovchinnikova Novel Antimicrobial Peptides from the Arctic Polychaeta Nicomache minor Provide New Molecular Insight into Biological Role of the BRICHOS Domain |
topic_facet |
antimicrobial peptide polychaeta innate immunity BRICHOS domain recombinant peptide α-helix Rana-box nuclear magnetic resonance (NMR) Biology (General) QH301-705.5 |
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 |
Article in Journal/Newspaper |
author |
Pavel V. Panteleev Andrey V. Tsarev Ilia A. Bolosov Alexander S. Paramonov Mariana B. Marggraf Sergey V. Sychev Zakhar O. Shenkarev Tatiana V. Ovchinnikova |
author_facet |
Pavel V. Panteleev Andrey V. Tsarev Ilia A. Bolosov Alexander S. Paramonov Mariana B. Marggraf Sergey V. Sychev Zakhar O. Shenkarev Tatiana V. Ovchinnikova |
author_sort |
Pavel V. Panteleev |
title |
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_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_sort |
novel antimicrobial peptides from the arctic polychaeta nicomache minor provide new molecular insight into biological role of the brichos domain |
publisher |
MDPI AG |
publishDate |
2018 |
url |
https://doi.org/10.3390/md16110401 https://doaj.org/article/e3a4b196616f4f168594bc7a74ab3c5c |
geographic |
Arctic |
geographic_facet |
Arctic |
genre |
Arctic |
genre_facet |
Arctic |
op_source |
Marine Drugs, Vol 16, Iss 11, p 401 (2018) |
op_relation |
https://www.mdpi.com/1660-3397/16/11/401 https://doaj.org/toc/1660-3397 1660-3397 doi:10.3390/md16110401 https://doaj.org/article/e3a4b196616f4f168594bc7a74ab3c5c |
op_doi |
https://doi.org/10.3390/md16110401 |
container_title |
Marine Drugs |
container_volume |
16 |
container_issue |
11 |
container_start_page |
401 |
_version_ |
1766338731754651648 |