dc.contributor.author | Peeters, E | |
dc.contributor.author | Boon, M | |
dc.contributor.author | Rollie, C | |
dc.contributor.author | Willaert, R | |
dc.contributor.author | Voet, M | |
dc.contributor.author | White, MF | |
dc.contributor.author | Prangishvili, D | |
dc.contributor.author | Lavigne, R | |
dc.contributor.author | Quax, TEF | |
dc.date.accessioned | 2018-05-14T10:55:13Z | |
dc.date.issued | 2017-07 | |
dc.description.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. | en_GB |
dc.description.sponsorship | This research was supported by the Geconcerteerde Onderzoeks Actie grant
‘Phage Biosystems’ from the KULeuven (http://www.kuleuven.be/onderzoek/kernprojecten/goa.htm). T.E.F.Q.
was supported by a FWO Pegasus Marie-Curie fellowship and a Marie-Curie Intra-European Fellowship.
The Belgian Federal Science Policy Office (Belspo) and the European Space Agency (ESA) PRODEX program
supported the work of RGW. E.P. was supported by start-up funds provided by the Vrije Universiteit Brussel (VUB). | en_GB |
dc.identifier.citation | Vol. 9, 190 | en_GB |
dc.identifier.doi | 10.3390/v9070190 | |
dc.identifier.uri | http://hdl.handle.net/10871/32828 | |
dc.language.iso | en | en_GB |
dc.publisher | MDPI | en_GB |
dc.relation.source | The following are available online at www.mdpi.com/1999-4915/9/7/190/s1,
Figure S1: Cleavage assay of SIRV1_Gp1 and SIRV2_Gp1; Figure S2: Cross-section analysis of a selection of large
complexes; Figure S3: Alignment of SIRV1_gp1 and SIRV2_gp1 on the base pair and amino acid level; Table S1:
Sequences of oligonucleotides used in this work. | en_GB |
dc.rights | © 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/) | en_GB |
dc.subject | archaea | en_GB |
dc.subject | archaeal virus | en_GB |
dc.subject | Rudiviridae | en_GB |
dc.subject | SIRV2 | en_GB |
dc.subject | Sulfolobus | en_GB |
dc.subject | DNA binding | en_GB |
dc.subject | helix-turn-helix domain | en_GB |
dc.title | DNA-interacting characteristics of the archaeal rudiviral protein SIRV2_Gp1 | en_GB |
dc.type | Article | en_GB |
dc.date.available | 2018-05-14T10:55:13Z | |
dc.identifier.issn | 1999-4915 | |
dc.description | This is the final version of the article. Available from the publisher via the DOI in this record. | en_GB |
dc.identifier.journal | Viruses | en_GB |