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{{Short description|Genus of viruses}}
{{taxobox
{{Use dmy dates|date=April 2017}}
{{virusbox
| image = 2w0c_capsid.png
| image = 2w0c_capsid.png
| image_caption = The assembled [[capsid]] made of P2 and P3 proteins.<ref name="abrescia_2008">{{cite journal|last1=Abrescia|first1=Nicola G.A.|last2=Grimes|first2=Jonathan M.|last3=Kivelä|first3=Hanna M.|last4=Assenberg|first4=Rene|last5=Sutton|first5=Geoff C.|last6=Butcher|first6=Sarah J.|last7=Bamford|first7=Jaana K.H.|last8=Bamford|first8=Dennis H.|last9=Stuart|first9=David I.|title=Insights into Virus Evolution and Membrane Biogenesis from the Structure of the Marine Lipid-Containing Bacteriophage PM2|journal=Molecular Cell|date=September 2008|volume=31|issue=5|pages=749–761|doi=10.1016/j.molcel.2008.06.026}}</ref>
| image_caption = The assembled [[capsid]] made of P2 and P3 proteins.<ref name="abrescia_2008">{{cite journal|last1=Abrescia|first1=Nicola G.A.|last2=Grimes|first2=Jonathan M.|last3=Kivelä|first3=Hanna M.|last4=Assenberg|first4=Rene|last5=Sutton|first5=Geoff C.|last6=Butcher|first6=Sarah J.|last7=Bamford|first7=Jaana K.H.|last8=Bamford|first8=Dennis H.|last9=Stuart|first9=David I.|title=Insights into Virus Evolution and Membrane Biogenesis from the Structure of the Marine Lipid-Containing Bacteriophage PM2|journal=Molecular Cell|date=September 2008|volume=31|issue=5|pages=749–761|doi=10.1016/j.molcel.2008.06.026|pmid=18775333|doi-access=free}}</ref>
| taxon = Corticovirus
| virus_group = i
| familia = ''[[Corticoviridae]]''
| genus = '''''Corticovirus'''''
| subdivision_ranks = Type Species
| subdivision =
*''Pseudoalteromonas virus PM2''
}}
}}


'''''Corticovirus''''' is a genus of [[viruses]] in the family ''[[Corticoviridae]]''<ref name=ICTVReport>{{cite web|title=Corticoviridae|url=https://talk.ictvonline.org/ictv-reports/ictv_online_report/dsdna-viruses/w/corticoviridae|website=ICTV Online (10th) Report|language=en}}</ref>. Corticoviruses are [[bacteriophage]]s; that is, their natural [[host (biology)|hosts]] are [[bacteria]]. The genus contains only one species, the [[type species]] '''''Pseudoalteromonas virus PM2''''' (also known as '''Pseudoalteromonas phage PM2''' or '''bacteriophage PM2''').<ref name=ICTVReport/><ref name=ViralZone>{{cite web|title=Viral Zone|url=http://viralzone.expasy.org/all_by_species/533.html|publisher=ExPASy|accessdate=15 June 2015}}</ref> The name is derived from Latin ''cortex'', ''corticis'' (meaning 'crust' or 'bark'). However, [[prophage]]s closely related to PM2 are abundant in the genomes of aquatic bacteria, suggesting that the ecological importance of corticoviruses might be underestimated.<ref>{{cite journal|vauthors=Krupovic M, Bamford DH |title=Putative prophages related to lytic tailless marine dsDNA phage PM2 are widespread in the genomes of aquatic bacteria|journal=BMC Genomics|year=2007|volume=8|pages=236|doi=10.1186/1471-2164-8-236|pmid=17634101|url=http://www.biomedcentral.com/content/pdf/1471-2164-8-236.pdf|pmc=1950889}}</ref> Bacteriophage PM2 was first described in 1968 after isolation from [[seawater]] sampled from the coast of [[Chile]].<ref name="espejo_1968">{{cite journal|last1=Espejo|first1=Romilio T.|last2=Canelo|first2=Eliana S.|title=Properties of bacteriophage PM2: A lipid-containing bacterial virus|journal=Virology|date=April 1968|volume=34|issue=4|pages=738–747|doi=10.1016/0042-6822(68)90094-9}}</ref>
'''''Corticovirus''''' is a genus of [[viruses]] in the family ''[[Corticoviridae]]''.<ref name=ICTVReport>{{cite web|title=Corticoviridae|url=https://ictv.global/report/chapter/corticoviridae/corticoviridae|website=ICTV Online (10th) Report|language=en}}</ref> Corticoviruses are [[bacteriophage]]s; that is, their natural [[host (biology)|hosts]] are [[bacteria]]. The genus contains two species.<ref name=ICTVReport/><ref name=ViralZone>{{cite web|title=Viral Zone|url=http://viralzone.expasy.org/all_by_species/533.html|publisher=ExPASy|access-date=15 June 2015}}</ref> The name is derived from Latin ''cortex'', ''corticis'' (meaning 'crust' or 'bark'). However, [[prophage]]s closely related to PM2 are abundant in the genomes of aquatic bacteria, suggesting that the ecological importance of corticoviruses might be underestimated.<ref>{{cite journal|vauthors=Krupovic M, Bamford DH |title=Putative prophages related to lytic tailless marine dsDNA phage PM2 are widespread in the genomes of aquatic bacteria|journal=BMC Genomics|year=2007|volume=8|pages=236|doi=10.1186/1471-2164-8-236|pmid=17634101|url= |pmc=1950889 |doi-access=free }}</ref> Bacteriophage PM2 was first described in 1968 after isolation from [[seawater]] sampled from the coast of [[Chile]].<ref name="espejo_1968">{{cite journal|last1=Espejo|first1=Romilio T.|last2=Canelo|first2=Eliana S.|title=Properties of bacteriophage PM2: A lipid-containing bacterial virus|journal=Virology|date=April 1968|volume=34|issue=4|pages=738–747|doi=10.1016/0042-6822(68)90094-9|pmid=5655723 }}</ref>


==Taxonomy==
==Taxonomy==
The genus contains the following species:<ref>{{cite web |title=Virus Taxonomy: 2020 Release |url=https://ictv.global/taxonomy |publisher=International Committee on Taxonomy of Viruses (ICTV) |date=March 2021 |access-date=22 May 2021}}</ref>
<big>'''Group: dsDNA'''</big>
* ''[[Pseudoalteromonas virus Cr39582]]''
{{Collapsible list|title= <big>Order: Unassigned</big>
* ''[[Pseudoalteromonas virus PM2]]''
|1={{Collapsible list| framestyle=border:none; padding:1.0em;|title=Family: [[Corticoviridae]]

|1={{hidden begin|title=<small>Genus: Corticovirus</small>}}
Other unassigned phages:<ref>[https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?id=10659 Corticoviridae]. NCBI Taxonomy.</ref>
*<small>'''''Pseudoalteromonas virus PM2'''''</small>
* ''[[Pseudoalteromonas virus GXT1010]]''
{{hidden end}}
* ''[[Marinomonas virus YY]]''
}}
* ''[[Vibrio virus fNo16]]''
}}<ref name=ICTVReport />


==Virology==
==Virology==
The virons consist of a round, [[icosahedral]], non-enveloped [[capsid]] of a diameter of 60 [[nanometers|nm]] and an internal [[lipid]] [[cell membrane|membrane]] located between outer and inner [[protein]] shell.<ref>Kiveld, H.M., Kalkkinen, N. and Bamford, D.H. (2002). Bacteriophage PM2 has a protein capsid surrounding a spherical lipid-protein core" ''J. Virol'' 76, 8169-8178.</ref> The shells are composed of three layers whose surfaces reveals a pattern with distinctive features,<ref>Kiveld, H.M., Männistö, R.H., Kalkkinen, N. and Bamford, D.H. (1999). Purification and protein composition of PM2, the first lipid-containing bacterial virus to be isolated" ''Virology'' 262, 364-374.</ref> including bush-like spikes protruding from the twelve [[vertex (geometry)|vertices]].<ref>Harrison, S.C., Caspar, D.L., Camerini-Otero, R.D. and Franklin, R.M. (1971). Lipid and protein arrangement in bacteriophage PM2. Nat. New Biol., 229, 197-201.</ref>
The virons consist of a round, [[icosahedral]], non-enveloped [[capsid]] of a diameter of 60 [[nanometers|nm]] and an internal [[lipid]] [[cell membrane|membrane]] located between outer and inner [[protein]] shell.<ref>Kiveld, H.M., Kalkkinen, N. and Bamford, D.H. (2002). Bacteriophage PM2 has a protein capsid surrounding a spherical lipid-protein core" ''J. Virol.'' 76, 8169-8178.</ref> The shells are composed of three layers whose surfaces reveals a pattern with distinctive features,<ref>Kiveld, H.M., Männistö, R.H., Kalkkinen, N. and Bamford, D.H. (1999). Purification and protein composition of PM2, the first lipid-containing bacterial virus to be isolated" ''Virology'' 262, 364-374.</ref> including bush-like spikes protruding from the twelve [[vertex (geometry)|vertices]].<ref>Harrison, S.C., Caspar, D.L., Camerini-Otero, R.D. and Franklin, R.M. (1971). Lipid and protein arrangement in bacteriophage PM2. Nat. New Biol., 229, 197-201.</ref>


The icosahedral capsid (T = 21) is 56 [[nanometer]]s (nm) in diameter and is composed of 1200 P1 (spike) and 60 P2 (capsid) proteins. The pentameric receptor-binding spikes protrude from the 12 fivefold axes. The capsid encloses an internal lipid core containing the structural proteins P3 to P10.
The icosahedral capsid (T = 21) is 56 [[nanometer]]s (nm) in diameter and is composed of 1200 P1 (spike) and 60 P2 (capsid) proteins. The pentameric receptor-binding spikes protrude from the 12 fivefold axes. The capsid encloses an internal lipid core containing the structural proteins P3 to P10.{{cn|date=October 2022}}


== Genome ==
== Genome ==
Line 32: Line 29:
Transcription is organised into three operons.
Transcription is organised into three operons.


Replication of the genome is via a rolling-circle mechanism, initiated by the virus encoded endonuclease P12.
Replication of the genome is via a rolling-circle mechanism, initiated by the virus encoded endonuclease P12.{{cn|date=October 2022}}
{| class="wikitable sortable" style="text-align:center"
{| class="wikitable sortable" style="text-align:center"
|-
|-
! Genus !! Structure || Symmetry !! Capsid !! Genomic arrangement !! Genomic segmentation
! Genus !! Structure || Symmetry !! Capsid !! Genomic arrangement !! Genomic segmentation
|-
|-
|Corticovirus||Polyhedral||T=21||Non-enveloped||Circular||Monopartite
|''Corticovirus''||Polyhedral||T=21||Non-enveloped||Circular||Monopartite
|}
|}


==Life cycle==
==Life cycle==
[[File:Viruses.11.-2019-76-Fig-1c.png|thumb|Entry mechanism of Pseudoalteromonas phage PM2]]
Viral replication is cytoplasmic. Entry into the host cell is achieved by adsorption to the host cell surface followed by fusion of the viral membrane with the outer membrane of the host cell and subsequent genome delivery into the cell interior.<ref>{{cite journal|vauthors=Cvirkaite-Krupovic V, Krupovic M, Daugelavicius R, Bamford DH |title=Calcium ion-dependent entry of the membrane-containing bacteriophage PM2 into its Pseudoalteromonas host|journal=Virology|date=2010|volume=405|issue=1|pages=120–128|doi=10.1016/j.virol.2010.05.021|pmid=20646729|url=http://www.sciencedirect.com/science/article/pii/S0042682210003521}}</ref> DNA-templated transcription is the method of transcription. Bacteria of the genus ''[[Pseudoalteromonas]]'' serve as the natural host. Corticovirus PM2 is a lytic virus and at the end of the infection cycle disrupts the host cell using a unique lysis system consisting of phage-encoded proteins P17 and P18 as well as an unidentified host autolysin.<ref>{{cite journal|vauthors=Krupovic M, Daugelavicius R, Bamford DH |title=A novel lysis system in PM2, a lipid-containing marine double-stranded DNA bacteriophage|journal=Mol Microbiol|date=2007|volume=64|issue=6|pages=1635–48|doi=10.1111/j.1365-2958.2007.05769.x|pmid=17555443|url=http://onlinelibrary.wiley.com/doi/10.1111/j.1365-2958.2007.05769.x/full}}</ref> However, identification of PM2-like proviruses in bacterial genomes indicates that other members of this family might be temperate viruses. Transmission routes are passive diffusion.<ref name=ViralZone />
Viral replication is cytoplasmic. Entry into the host cell is achieved by adsorption to the host cell surface followed by fusion of the viral membrane with the outer membrane of the host cell and subsequent genome delivery into the cell interior.<ref>{{cite journal|vauthors=Cvirkaite-Krupovic V, Krupovic M, Daugelavicius R, Bamford DH |title=Calcium ion-dependent entry of the membrane-containing bacteriophage PM2 into its Pseudoalteromonas host|journal=Virology|date=2010|volume=405|issue=1|pages=120–128|doi=10.1016/j.virol.2010.05.021|pmid=20646729|doi-access=free}}</ref> DNA-templated transcription is the method of transcription. Bacteria of the genera ''[[Pseudoalteromonas]]'', ''[[Marinomonas]]'' and ''[[Vibrio]]'' serve as the natural host. Corticovirus PM2 is a lytic virus and at the end of the infection cycle disrupts the host cell using a unique lysis system consisting of phage-encoded proteins P17 and P18 as well as an unidentified host autolysin.<ref>{{cite journal|vauthors=Krupovic M, Daugelavicius R, Bamford DH |title=A novel lysis system in PM2, a lipid-containing marine double-stranded DNA bacteriophage|journal=Mol Microbiol|date=2007|volume=64|issue=6|pages=1635–48|doi=10.1111/j.1365-2958.2007.05769.x|pmid=17555443|doi-access=free}}</ref> However, identification of PM2-like proviruses in bacterial genomes indicates that other members of this family might be temperate viruses. Transmission routes are passive diffusion.<ref name=ViralZone />


{| class="wikitable sortable" style="text-align:center"
{| class="wikitable sortable" style="text-align:center"
Line 47: Line 45:
! Genus !! Host details !! Tissue tropism !! Entry details !! Release details !! Replication site !! Assembly site !! Transmission
! Genus !! Host details !! Tissue tropism !! Entry details !! Release details !! Replication site !! Assembly site !! Transmission
|-
|-
|Corticovirus||Bacteria||None||Injection||Lysis||Cytoplasm||Cytoplasm||Passive diffusion
|''Corticovirus''||Bacteria||None||Injection||Lysis||Cytoplasm||Cytoplasm||Passive diffusion
|}
|}


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==External links==
==External links==
* [https://talk.ictvonline.org/ictv-reports/ictv_online_report/dsdna-viruses/w/corticoviridae '''ICTV Online(10th) Report: Corticoviridae]
* [https://ictv.global/report/chapter/corticoviridae/corticoviridae '''ICTV Online(10th) Report: Corticoviridae''']
* [http://viralzone.expasy.org/all_by_species/533.html '''Viralzone''': Corticovirus]
* [http://viralzone.expasy.org/all_by_species/533.html '''Viralzone''': Corticovirus]
{{Baltimore classification}}
{{Baltimore classification}}
{{Taxonbar|from=Q1135608}}
{{Use dmy dates|date=April 2017}}


[[Category:Corticoviridae]]
[[Category:Corticoviridae| ]]
[[Category:Bacteriophages]]
[[Category:Bacteriophages]]
[[Category:Virus genera]]

Latest revision as of 21:56, 28 November 2023

Corticovirus
The assembled capsid made of P2 and P3 proteins.[1]
Virus classification Edit this classification
(unranked): Virus
Realm: Varidnaviria
Kingdom: Bamfordvirae
Phylum: Preplasmiviricota
Class: Tectiliviricetes
Order: Vinavirales
Family: Corticoviridae
Genus: Corticovirus

Corticovirus is a genus of viruses in the family Corticoviridae.[2] Corticoviruses are bacteriophages; that is, their natural hosts are bacteria. The genus contains two species.[2][3] The name is derived from Latin cortex, corticis (meaning 'crust' or 'bark'). However, prophages closely related to PM2 are abundant in the genomes of aquatic bacteria, suggesting that the ecological importance of corticoviruses might be underestimated.[4] Bacteriophage PM2 was first described in 1968 after isolation from seawater sampled from the coast of Chile.[5]

Taxonomy[edit]

The genus contains the following species:[6]

Other unassigned phages:[7]

Virology[edit]

The virons consist of a round, icosahedral, non-enveloped capsid of a diameter of 60 nm and an internal lipid membrane located between outer and inner protein shell.[8] The shells are composed of three layers whose surfaces reveals a pattern with distinctive features,[9] including bush-like spikes protruding from the twelve vertices.[10]

The icosahedral capsid (T = 21) is 56 nanometers (nm) in diameter and is composed of 1200 P1 (spike) and 60 P2 (capsid) proteins. The pentameric receptor-binding spikes protrude from the 12 fivefold axes. The capsid encloses an internal lipid core containing the structural proteins P3 to P10.[citation needed]

Genome[edit]

The genome is not segmented, constitutes 13% of the virus's weight and contains a single molecule of circular, supercoiled, double-stranded DNA of 10 kilobases in length. The genome has a g + c content of 43%.[11] It encodes ~21 proteins.

Transcription is organised into three operons.

Replication of the genome is via a rolling-circle mechanism, initiated by the virus encoded endonuclease P12.[citation needed]

Genus Structure Symmetry Capsid Genomic arrangement Genomic segmentation
Corticovirus Polyhedral T=21 Non-enveloped Circular Monopartite

Life cycle[edit]

Entry mechanism of Pseudoalteromonas phage PM2

Viral replication is cytoplasmic. Entry into the host cell is achieved by adsorption to the host cell surface followed by fusion of the viral membrane with the outer membrane of the host cell and subsequent genome delivery into the cell interior.[12] DNA-templated transcription is the method of transcription. Bacteria of the genera Pseudoalteromonas, Marinomonas and Vibrio serve as the natural host. Corticovirus PM2 is a lytic virus and at the end of the infection cycle disrupts the host cell using a unique lysis system consisting of phage-encoded proteins P17 and P18 as well as an unidentified host autolysin.[13] However, identification of PM2-like proviruses in bacterial genomes indicates that other members of this family might be temperate viruses. Transmission routes are passive diffusion.[3]

Genus Host details Tissue tropism Entry details Release details Replication site Assembly site Transmission
Corticovirus Bacteria None Injection Lysis Cytoplasm Cytoplasm Passive diffusion

References[edit]

  1. ^ Abrescia, Nicola G.A.; Grimes, Jonathan M.; Kivelä, Hanna M.; Assenberg, Rene; Sutton, Geoff C.; Butcher, Sarah J.; Bamford, Jaana K.H.; Bamford, Dennis H.; Stuart, David I. (September 2008). "Insights into Virus Evolution and Membrane Biogenesis from the Structure of the Marine Lipid-Containing Bacteriophage PM2". Molecular Cell. 31 (5): 749–761. doi:10.1016/j.molcel.2008.06.026. PMID 18775333.
  2. ^ a b "Corticoviridae". ICTV Online (10th) Report.
  3. ^ a b "Viral Zone". ExPASy. Retrieved 15 June 2015.
  4. ^ Krupovic M, Bamford DH (2007). "Putative prophages related to lytic tailless marine dsDNA phage PM2 are widespread in the genomes of aquatic bacteria". BMC Genomics. 8: 236. doi:10.1186/1471-2164-8-236. PMC 1950889. PMID 17634101.
  5. ^ Espejo, Romilio T.; Canelo, Eliana S. (April 1968). "Properties of bacteriophage PM2: A lipid-containing bacterial virus". Virology. 34 (4): 738–747. doi:10.1016/0042-6822(68)90094-9. PMID 5655723.
  6. ^ "Virus Taxonomy: 2020 Release". International Committee on Taxonomy of Viruses (ICTV). March 2021. Retrieved 22 May 2021.
  7. ^ Corticoviridae. NCBI Taxonomy.
  8. ^ Kiveld, H.M., Kalkkinen, N. and Bamford, D.H. (2002). Bacteriophage PM2 has a protein capsid surrounding a spherical lipid-protein core" J. Virol. 76, 8169-8178.
  9. ^ Kiveld, H.M., Männistö, R.H., Kalkkinen, N. and Bamford, D.H. (1999). Purification and protein composition of PM2, the first lipid-containing bacterial virus to be isolated" Virology 262, 364-374.
  10. ^ Harrison, S.C., Caspar, D.L., Camerini-Otero, R.D. and Franklin, R.M. (1971). Lipid and protein arrangement in bacteriophage PM2. Nat. New Biol., 229, 197-201.
  11. ^ Männistö, R.H., Kivelä, H.M., Paulin, L., Bamford, D.H. and Bamford, J.K.H. (1999). The complete genome sequence of PM2, the first lipid-containing bacterial virus to be isolated" Virology 262, 355-363.
  12. ^ Cvirkaite-Krupovic V, Krupovic M, Daugelavicius R, Bamford DH (2010). "Calcium ion-dependent entry of the membrane-containing bacteriophage PM2 into its Pseudoalteromonas host". Virology. 405 (1): 120–128. doi:10.1016/j.virol.2010.05.021. PMID 20646729.
  13. ^ Krupovic M, Daugelavicius R, Bamford DH (2007). "A novel lysis system in PM2, a lipid-containing marine double-stranded DNA bacteriophage". Mol Microbiol. 64 (6): 1635–48. doi:10.1111/j.1365-2958.2007.05769.x. PMID 17555443.

External links[edit]