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

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 thr...

Ausführliche Beschreibung

Gespeichert in:

Bibliographische Detailangaben
Veröffentlicht in:	Virology (New York, N.Y.) N.Y.), 2010-08, Vol.404 (1), p.1-4
Hauptverfasser:	Quax, Tessa E.F, Krupovič, Mart, Lucas, Soizick, Forterre, Patrick, Prangishvili, David
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Archaea Biochemistry, Molecular Biology Hyperthermophile Infectious Disease Life Sciences Lysis Microbiology and Parasitology Molecular Sequence Data Rudiviridae Rudiviridae - genetics Rudiviridae - growth & development Sequence Homology SIRV2 Sulfolobus Sulfolobus - virology Sulfolobus islandicus Viral Proteins Viral Proteins - genetics Viral Proteins - metabolism Virus Release Virus–host interaction
Online-Zugang:	Volltext
Tags:	Tag hinzufügen Keine Tags, Fügen Sie den ersten Tag hinzu!

Beschreibung
Zusammenfassung:	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.
ISSN:	0042-6822 1096-0341
DOI:	10.1016/j.virol.2010.04.020