The Sulfolobus rod-shaped virus 2 encodes a prominent structural component of the unique virion release system in Archaea
Autor: | Mart Krupovic, Tessa E. F. Quax, Soizick Lucas, Patrick Forterre, David Prangishvili |
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Přispěvatelé: | Biologie Moléculaire du Gène chez les Extrêmophiles (BMGE), Institut Pasteur [Paris], Institut Pasteur [Paris] (IP) |
Jazyk: | angličtina |
Rok vydání: | 2010 |
Předmět: |
viruses
Molecular Sequence Data Sequence Homology MESH: Amino Acid Sequence SIRV2 Virus Microbiology Sulfolobus 03 medical and health sciences Viral Proteins Virology [SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology Amino Acid Sequence MESH: Sequence Homology Virus Release 030304 developmental biology Host cell surface 0303 health sciences Virus–host interaction MESH: Molecular Sequence Data biology 030306 microbiology MESH: Virus Release Archaeal Viruses biology.organism_classification Archaea MESH: Viral Proteins Hyperthermophile 3. Good health Cell biology Rudiviridae Lysis [SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitology MESH: Sulfolobus MESH: Rudiviridae Rudivirus |
Zdroj: | Virology Virology, Elsevier, 2010, 404 (1), pp.1-4. ⟨10.1016/j.virol.2010.04.020⟩ Virology, 2010, 404 (1), pp.1-4. ⟨10.1016/j.virol.2010.04.020⟩ |
ISSN: | 0042-6822 1096-0341 |
DOI: | 10.1016/j.virol.2010.04.020⟩ |
Popis: | International audience; 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. |
Databáze: | OpenAIRE |
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