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Viruses 2017, 9(7), 190; doi:10.3390/v9070190

DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1

1
Research Group of Microbiology, Department of Bio-Engineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium
2
Laboratory of Gene Technology, Department of Biosystems, KU Leuven, Kasteelpark Arenberg 21 box 2462, Heverlee, 3001 Leuven, Belgium
3
Biomedical Sciences Research Complex, University of St Andrews, Fife, North Haugh, St. Andrews KY16 9AJ, UK
4
Alliance Research Group VUB-UGhent NanoMicrobiology, IJRG VUB-EPFL, BioNanotechnology & NanoMedicine, Research Group Structural Biology Brussels, Department of Bio-Engineering Sciences, Vrije Universiteit Brussel, Pleinlaan 2, B-1050 Brussels, Belgium
5
Department of Microbiology, Institut Pasteur, 75015 Paris, France
*
Author to whom correspondence should be addressed.
Received: 4 May 2017 / Revised: 6 July 2017 / Accepted: 10 July 2017 / Published: 18 July 2017
(This article belongs to the Special Issue Viruses of Microbes)
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Abstract

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. View Full-Text
Keywords: archaea; archaeal virus; Rudiviridae; SIRV2; Sulfolobus; DNA binding; helix-turn-helix domain archaea; archaeal virus; Rudiviridae; SIRV2; Sulfolobus; DNA binding; helix-turn-helix domain
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MDPI and ACS Style

Peeters, E.; Boon, M.; Rollie, C.; Willaert, R.G.; Voet, M.; White, M.F.; Prangishvili, D.; Lavigne, R.; Quax, T.E. DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1. Viruses 2017, 9, 190.

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