Pseudomonas virus phi6
This article needs additional citations for verification. (May 2012) |
Pseudomonas virus phi6 | |
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The RNA-packaged procapsid (protein shell) of Pseudomonas virus phi6 | |
Genome of pseudomonas virus phi6 | |
Virus classification | |
(unranked): | Virus |
Realm: | Riboviria |
Kingdom: | Orthornavirae |
Phylum: | Duplornaviricota |
Class: | Vidaverviricetes |
Order: | Mindivirales |
Family: | Cystoviridae |
Genus: | Cystovirus |
Species: | Pseudomonas virus phi6
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Synonyms | |
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Proteins[edit]
The genome of
Life cycle[edit]
A copy of the sense strand of the large genome segment (6374 bases) is then synthesized (transcription) on the vertices of the capsid, with the RNA-dependent RNA polymerase, P2, and released into the host cell cytosol. The four proteins translated from the large segment spontaneously assemble into procapsids, which then package a large segment sense strand, polymerizing its complement during entry through the P2 polymerase-containing vertices. While the large segment is being translated (expressed) and synthesized (replicated), the parental phage releases copies of the sense strands of the medium segment (4061 bases) and small segment (2948 bases) into the cytosol. They are translated, and packaged into the procapsids in order: medium then small. The filled capsids are then coated with the nucleocapsid protein P8, and then outer membrane proteins somehow attract bacterial inner membrane, which then envelopes the nucleocapsid.
The lytic protein, P5, is contained between the P8 nucleocapsid shell and the viral envelope. The completed phage progeny remain in the cytosol until sufficient levels of the lytic protein P5 degrade the host cell wall. The cytosol then bursts forth, disrupting the outer membrane, releasing the phage. The bacterium is killed by this lysis.
RNA-dependent RNA polymerase[edit]
RNA-dependent RNA polymerases (RdRPs) are critical components in the life cycle of double-stranded RNA (dsRNA) viruses. However, it is not fully understood how these important enzymes function during viral replication. Expression and characterization of the purified recombinant RdRP of
Research[edit]
See also[edit]
References[edit]
- ^ Murphy FA, Fauquet CM, Bishop DH, Ghabrial SA, Jarvis AW, Martelli GP, Mayo MA, Summers MD (1995). "Virus taxonomy: sixth report of the International Committee on Taxonomy of Viruses" (PDF). Archives of Virology. 10: 350–4.
- ^ Krupovic M, Kuhn M, Adriaenssens JH, Yamada E, Wittmann T, Vogensen J, metal (May 2015). "To rename all (522)existing bacterial virus and 2 archaeal virus species" (PDF). International Committee on Taxonomy of Viruses. Retrieved 29 August 2019.
- ^ a b Poranen MM, Mäntynen S (October 2017). "ICTV Virus Taxonomy Profile: Cystoviridae". The Journal of General Virology. 98 (10): 2423–2424. doi:10.1099/jgv.0.000928. PMC 5725992. PMID 28933690.
- ^ Lyytinen OL, Starkova D, Poranen MM (February 2019). "Microbial production of lipid-protein vesicles using enveloped bacteriophage phi6". Microbial Cell Factories. 18 (1): 29. doi:10.1186/s12934-019-1079-z. PMC 6366064. PMID 30732607.
- ^ Koivunen MR, Sarin LP, Bamford DH (2008). "Structure-Function Insights Into the RNA-Dependent RNA Polymerase of the dsRNA Bacteriophage
Φ 6". Segmented Double-stranded RNA Viruses: Structure and Molecular Biology. Caister Academic Press. ISBN 978-1-904455-21-9.
External links[edit]
- Detailed molecular description
- Descriptions of tests of evolutionary theory by the Turner Lab
- Descriptions of tests of evolutionary theory by the Burch Lab
- The Universal Virus Database of the International Committee on the Taxonomy of Viruses
- The origin of phospholipids of the enveloped bacteriophage phi6