Tectivirus

Tectiviridae
CryoEM model of Enterobacteria phage PRD1 capsid. PDB entry 1gw7[1]
Virus classification
Group: Group I (dsDNA)
Family: Tectiviridae
Genus: Tectivirus
Type species
Enterobacteria phage PRD1

Tectivirus is a genus of viruses, and is currently the only genus in the family Tectiviridae. Gram-negative bacteria serve as natural hosts. There are currently four species in this genus including the type species Enterobacteria phage PRD1.[2][3] Tectiviruses have no head-tail structure, but are capable of producing tail-like tubes of ~ 60×10 nm upon adsorption or after chloroform treatment. The name is derived from Latin tectus (meaning 'covered').

Virology

The virions of Tectiviridae species are non-enveloped, icosahedral and display a pseudo T=25 symmetry.[2] The capsid has two layers. The outer layer is a protein structure of 240 capsid proteins trimers, and the inner one is a proteinaceous lipid membrane which envelopes the virus genome. Apical spikes extending about 20 nanometers (nm) protrude from the icosahedrons vertices.

The genome is a single molecule of linear double-stranded DNA of 15 kilobases in length, and has 30 open reading frames.[2] It forms a tightly packed coil and encodes several structural proteins. It encodes about 30 proteins that are transcribed in operons. At least 9 structural proteins are present in the viron. The genome is about 66 megaDaltons in weight and constitutes 14–15% of the virion by weight. Lipids constitute a further 15% by weight. Carbohydrates are not present.

Genus Structure Symmetry Capsid Genomic Arrangement Genomic Segmentation
TectivirusIcosahedralT=25Non-EnvelopedLinearMonopartite

Life cycle

Viral replication is cytoplasmic. Entry into the host cell is achieved by adsorption into the host cell.[2] After adsorption to the host cell surface the virion extrudes a tail-tube structure through a vertex for genome delivery into the host. Replication follows the DNA strand displacement model. DNA-templated transcription is the method of transcription.[2] Capsid proteins polymerize around a lipoprotein vesicle translocated in the cytoplasm by virion assembly factors.

Mature virons are released by lysis, which, in the case of PRD1, is achieved with the aid of virus-encoded lysis machinery consisting of four proteins: P15 (endolysin),[4] P35 (holin),[5] P36 and P37 (homologues of the Rz/Rz1 proteins of phage lambda).[6]

Genus Host Details Tissue Tropism Entry Details Release Details Replication Site Assembly Site Transmission
TectivirusGram-negative bacteriaNoneInjectionLysisCytoplasmCytoplasmPassive diffusion

Taxonomy

Group: dsDNA

[3]

References

  1. ↑ San Martín, C; Huiskonen, JT; Bamford, JK; Butcher, SJ; Fuller, SD; Bamford, DH; Burnett, RM (2002). "Minor proteins, mobile arms and membrane-capsid interactions in the bacteriophage PRD1 capsid". Nature Structural Biology. 9 (10): 756–63. doi:10.1038/nsb837. PMID 12219080.
  2. 1 2 3 4 5 "Viral Zone". ExPASy. Retrieved 15 June 2015.
  3. 1 2 ICTV. "Virus Taxonomy: 2014 Release". Retrieved 15 June 2015.
  4. ↑ Caldentey J, Hänninen AL, Bamford DH (1994). "Gene XV of bacteriophage PRD1 encodes a lytic enzyme with muramidase activity". Eur J Biochem. 225 (1): 341–346. doi:10.1111/j.1432-1033.1994.00341.x. PMID 7925454.
  5. ↑ Rydman PS, Bamford DH (2003). "Identification and mutational analysis of bacteriophage PRD1 holin protein P35". J Bacteriol. 185 (13): 3795–3803. doi:10.1128/JB.185.13.3795-3803.2003. PMC 161566Freely accessible. PMID 12813073.
  6. ↑ Krupovic M, Cvirkaite-Krupovic V, Bamford DH (2008). "Identification and functional analysis of the Rz/Rz1-like accessory lysis genes in the membrane-containing bacteriophage PRD1". Mol Microbiol. 68 (2): 492–503. doi:10.1111/j.1365-2958.2008.06165.x. PMID 18366440.

Further reading

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