ArticleProceedings of the National Academy of Sciences of the United States of America2011
Simple and elegant design of a virion egress structure in Archaea.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 55 citations in OpenAlex.
- CRISPR spacers reveal diverse and abundant Thermococcales viruses in hydrothermal vents.Research square · 2026Article
- Archaeal virus entry and egress.microLife · 2024Review
- Viruses of theFrontiers in microbiology · 2023Review
- The biology of thermoacidophilic archaea from the order Sulfolobales.FEMS microbiology reviews · 2021Article
- A filamentous archaeal virus is enveloped inside the cell and released through pyramidal portals.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- The intriguing world of archaeal viruses.PLoS pathogens · 2020Article
- Anti-CRISPR-Based and CRISPR-Based Genome Editing ofViruses · 2018Article
- Structure and assembly mechanism of virus-associated pyramids.Biophysical reviews · 2018Review
- Novel Sulfolobus Virus with an Exceptional Capsid Architecture.Journal of virology · 2018Article
- The enigmatic archaeal virosphere.Nature reviews. Microbiology · 2017Review
- Article
- A virus of hyperthermophilic archaea with a unique architecture among DNA viruses.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Archaeal viruses at the cell envelope: entry and egress.Frontiers in microbiology · 2015Review
- Self-assembly of the general membrane-remodeling protein PVAP into sevenfold virus-associated pyramids.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- First insights into the entry process of hyperthermophilic archaeal viruses.Journal of virology · 2013Article
- Massive activation of archaeal defense genes during viral infection.Journal of virology · 2013Article
- Functional interplay between a virus and the ESCRT machinery in archaea.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Novel insights into gene regulation of the rudivirus SIRV2 infecting Sulfolobus cells.RNA biology · 2013Article
- Genomics and genetics of Sulfolobus islandicus LAL14/1, a model hyperthermophilic archaeon.Open biology · 2013Article
- Insights into a viral lytic pathway from an archaeal virus-host system.Journal of virology · 2013Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Some viruses of Archaea use an unusual egress mechanism that involves the formation of virus-associated pyramids (VAPs) on the host cell surface. At the end of the infection cycle, these structures open outward and create apertures through which mature virions escape from the cell. Here we describe in detail the structure and composition of VAPs formed by the Sulfolobus islandicus rod-shaped virus 2 (SIRV2) in cells of its hyperthermophilic archaeal host. We show that the VAPs are stable and autonomous assemblies that can be isolated from membranes of infected cells and purified without affecting their structure. The purified VAPs are heterogeneous in size, reflecting the dynamics of VAP development in a population of infected cells; however, they have a uniform geometry, consisting of seven isosceles triangular faces forming a baseless pyramid. Biochemical and immunoelectron microscopy analyses revealed that the 10-kDa P98 protein encoded by the SIRV2 virus is the sole component of the VAPs. The VAPs were produced in Sulfolobus acidocaldarius and Escherichia coli by heterologous expression of the SIRV2-P98 gene. The results confirm that P98 is the only constituent of the VAPs and demonstrate that no other viral protein is involved in the assembly of pyramids. P98 was able to produce stable structures under conditions ranging from moderate to extremely high temperatures (80 °C) and from neutral to extremely acidic pH (pH 2), demonstrating another remarkable property of this exceptional viral protein.
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