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DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1
Whereas the infection cycles of many bacterial and eukaryotic viruses have been characterized in detail, those of archaeal viruses remain largely unexplored. Recently, studies on a few model archaeal viruses such as SIRV2 (Sulfolobus islandicus rod-shaped virus) have revealed an unusual lysis mechan...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5537682/ https://www.ncbi.nlm.nih.gov/pubmed/28718834 http://dx.doi.org/10.3390/v9070190 |
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author | Peeters, Eveline Boon, Maarten Rollie, Clare Willaert, Ronnie G. Voet, Marleen White, Malcolm F. Prangishvili, David Lavigne, Rob Quax, Tessa E. F. |
author_facet | Peeters, Eveline Boon, Maarten Rollie, Clare Willaert, Ronnie G. Voet, Marleen White, Malcolm F. Prangishvili, David Lavigne, Rob Quax, Tessa E. F. |
author_sort | Peeters, Eveline |
collection | PubMed |
description | Whereas the infection cycles of many bacterial and eukaryotic viruses have been characterized in detail, those of archaeal viruses remain largely unexplored. Recently, studies on a few model archaeal viruses such as SIRV2 (Sulfolobus islandicus rod-shaped virus) have revealed an unusual lysis mechanism that involves the formation of pyramidal egress structures on the host cell surface. To expand understanding of the infection cycle of SIRV2, we aimed to functionally characterize gp1, which is a SIRV2 gene with unknown function. The SIRV2_Gp1 protein is highly expressed during early stages of infection and it is the only protein that is encoded twice on the viral genome. It harbours a helix-turn-helix motif and was therefore hypothesized to bind DNA. The DNA-binding behavior of SIRV2_Gp1 was characterized with electrophoretic mobility shift assays and atomic force microscopy. We provide evidence that the protein interacts with DNA and that it forms large aggregates, thereby causing extreme condensation of the DNA. Furthermore, the N-terminal domain of the protein mediates toxicity to the viral host Sulfolobus. Our findings may lead to biotechnological applications, such as the development of a toxic peptide for the containment of pathogenic bacteria, and add to our understanding of the Rudiviral infection cycle. |
format | Online Article Text |
id | pubmed-5537682 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-55376822017-08-04 DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1 Peeters, Eveline Boon, Maarten Rollie, Clare Willaert, Ronnie G. Voet, Marleen White, Malcolm F. Prangishvili, David Lavigne, Rob Quax, Tessa E. F. Viruses Article Whereas the infection cycles of many bacterial and eukaryotic viruses have been characterized in detail, those of archaeal viruses remain largely unexplored. Recently, studies on a few model archaeal viruses such as SIRV2 (Sulfolobus islandicus rod-shaped virus) have revealed an unusual lysis mechanism that involves the formation of pyramidal egress structures on the host cell surface. To expand understanding of the infection cycle of SIRV2, we aimed to functionally characterize gp1, which is a SIRV2 gene with unknown function. The SIRV2_Gp1 protein is highly expressed during early stages of infection and it is the only protein that is encoded twice on the viral genome. It harbours a helix-turn-helix motif and was therefore hypothesized to bind DNA. The DNA-binding behavior of SIRV2_Gp1 was characterized with electrophoretic mobility shift assays and atomic force microscopy. We provide evidence that the protein interacts with DNA and that it forms large aggregates, thereby causing extreme condensation of the DNA. Furthermore, the N-terminal domain of the protein mediates toxicity to the viral host Sulfolobus. Our findings may lead to biotechnological applications, such as the development of a toxic peptide for the containment of pathogenic bacteria, and add to our understanding of the Rudiviral infection cycle. MDPI 2017-07-18 /pmc/articles/PMC5537682/ /pubmed/28718834 http://dx.doi.org/10.3390/v9070190 Text en © 2017 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 Peeters, Eveline Boon, Maarten Rollie, Clare Willaert, Ronnie G. Voet, Marleen White, Malcolm F. Prangishvili, David Lavigne, Rob Quax, Tessa E. F. DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1 |
title | DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1 |
title_full | DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1 |
title_fullStr | DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1 |
title_full_unstemmed | DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1 |
title_short | DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1 |
title_sort | dna-interacting characteristics of the archaeal rudiviral protein sirv2_gp1 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5537682/ https://www.ncbi.nlm.nih.gov/pubmed/28718834 http://dx.doi.org/10.3390/v9070190 |
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