The Sulfolobus rod-shaped virus 2 encodes a prominent structural component of the unique virion release system in Archaea.
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.
Quax
Tessa E F
TE
Institut Pasteur, Molecular Biology of the Gene in Extremophiles Unit, 75724 Paris Cedex 15, France.
Krupovic
Mart
M
Lucas
Soizick
S
Forterre
Patrick
P
Prangishvili
David
D
D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D023642:Rudiviridae / Q000235:genetics / Q000254:growth & development*; D017385:Sequence Homology; D016944:Sulfolobus / Q000821:virology*; D014764:Viral Proteins / Q000235:genetics / Q000378:metabolism*; D057074:Virus Release
D014764:Viral Proteins