The Sulfolobus rod-shaped virus 2 encodes a prominent structural component of the unique virion release system in Archaea

Tessa Quax; Mart Krupovic; Soizick Lucas; Patrick Forterre; David Prangishvili

doi:10.1016/j.virol.2010.04.020

The Sulfolobus rod-shaped virus 2 encodes a prominent structural component of the unique virion release system in Archaea

Tessa Quax, Mart Krupovic, Soizick Lucas, Patrick Forterre, David Prangishvili^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › Academic › peer-review

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Abstract

Recently a unique mechanism of virion release was discovered in Archaea, different from lysis and egress systems of bacterial and eukaryotic viruses. It involves formation of pyramidal structures on the host cell surface that rupture the S-layer and by opening outwards, create apertures through which mature virions escape the cell. Here we present results of a protein analysis of Sulfolobus islandicus cells infected with the rudivirus SIRV2, which enable us to postulate SIRV2-encoded protein P98 as the major constituent of these exceptional cellular ultrastructures.

Original language	English
Pages (from-to)	1-4
Number of pages	4
Journal	Virology
Volume	404
Issue number	1
DOIs	https://doi.org/10.1016/j.virol.2010.04.020
Publication status	Published - 15-Aug-2010
Externally published	Yes

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The Sulfolobus rod-shaped virus 2 encodes a prominent structural component of the unique virion release system in ArchaeaFinal publisher's version, 820 KBLicence: Elsevier

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abstract = "Recently a unique mechanism of virion release was discovered in Archaea, different from lysis and egress systems of bacterial and eukaryotic viruses. It involves formation of pyramidal structures on the host cell surface that rupture the S-layer and by opening outwards, create apertures through which mature virions escape the cell. Here we present results of a protein analysis of Sulfolobus islandicus cells infected with the rudivirus SIRV2, which enable us to postulate SIRV2-encoded protein P98 as the major constituent of these exceptional cellular ultrastructures.",

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AU - Quax, Tessa

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AU - Lucas, Soizick

AU - Forterre, Patrick

AU - Prangishvili, David

PY - 2010/8/15

Y1 - 2010/8/15

N2 - Recently a unique mechanism of virion release was discovered in Archaea, different from lysis and egress systems of bacterial and eukaryotic viruses. It involves formation of pyramidal structures on the host cell surface that rupture the S-layer and by opening outwards, create apertures through which mature virions escape the cell. Here we present results of a protein analysis of Sulfolobus islandicus cells infected with the rudivirus SIRV2, which enable us to postulate SIRV2-encoded protein P98 as the major constituent of these exceptional cellular ultrastructures.

AB - Recently a unique mechanism of virion release was discovered in Archaea, different from lysis and egress systems of bacterial and eukaryotic viruses. It involves formation of pyramidal structures on the host cell surface that rupture the S-layer and by opening outwards, create apertures through which mature virions escape the cell. Here we present results of a protein analysis of Sulfolobus islandicus cells infected with the rudivirus SIRV2, which enable us to postulate SIRV2-encoded protein P98 as the major constituent of these exceptional cellular ultrastructures.

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The Sulfolobus rod-shaped virus 2 encodes a prominent structural component of the unique virion release system in Archaea

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