カプソメア
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/04/03 12:33:00」(JST)
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The capsomere is a subunit of the capsid, an outer covering of protein that protects the genetic material of a virus. Capsomeres self-assemble to form the capsid.
In this diagram of an Adenovirus, the capsid molecules are clearly visible.
Subunits called protomers aggregate to form capsomeres. Various arrangements of capsomeres are: 1) Icosahedral, 2) Helical, and 3) Complex.
1) Icosahedral- An icosahedron is a polygon with 12 vertices and 20 faces. Two types of capsomeres constitute the icosahedral capsid: pentagonal (pentons) at the vertices and hexagonal (hexons) at the faces. There are always twelve pentons, but the number of hexons varies among virus groups. In electron micrographs, capsomeres are recognized as regularly spaced rings with a central hole. Icosahedral symmetry is identical to cubic symmetry.
2) Helical- The protomers are not grouped in capsomeres, but are bound to each other so as to form a ribbon-like structure. This structure folds into a helix because the protomers are thicker at one end than at the other. The diameter of the helical capsid is determined by characteristics of its protomers, while its length is determined by the length of the nucleic acid it encloses.
3) Complex- e.g., that exhibited by poxvirus and rhabdovirus. This group comprises all those viruses which do not fit into either of the above two groups. When the viral particle has entered a host cell, the host cellular enzymes digest the capsid and its constituent capsomeres, thereby exposing the naked genetic material (DNA/RNA) of the virus, which subsequently enters the replication cycle.
Protect against physical, chemical, and enzymatic damage and are multiply redundant; having a few protein subunits that are repeated. This is because the viral genome is being as economic as possible by only needing a few protein codons to make a large structure. One of the major functions of a capsid is to introduce the enclosed viral genome into host cells by adsorbing readily to host cell surfaces. /,;
English Journal
- The asymmetric structure of an icosahedral virus bound to its receptor suggests a mechanism for genome release.
- Dent KC, Thompson R, Barker AM, Hiscox JA, Barr JN, Stockley PG, Ranson NA.SourceAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
- Structure (London, England : 1993).Structure.2013 Jul 2;21(7):1225-34.
- Simple, spherical RNA viruses have well-understood, symmetric protein capsids, but little structural information is available for their asymmetric components, such as minor proteins and their genomes, which are vital for infection. Here, we report an asymmetric structure of bacteriophage MS2, attach
- PMID 23810697
- Molecular energetics in the capsomere of virus-like particle revealed by molecular dynamics simulations.
- Zhang L, Tang R, Bai S, Connors NK, Lua LH, Chuan YP, Middelberg AP, Sun Y.SourceDepartment of Biochemical Engineering and Key Laboratory of Systems Bioengineering of the Ministry of Education, School of Chemical Engineering and Technology, Tianjin University, Tianjin, China.
- The journal of physical chemistry. B.J Phys Chem B.2013 May 9;117(18):5411-21. doi: 10.1021/jp311170w. Epub 2013 Apr 26.
- Virus-like particles (VLPs) are highly organized nanoparticles that have great potential in vaccinology, gene therapy, drug delivery, and materials science. However, the application of VLPs is hindered by obstacles in their design and production due to low efficiency of self-assembly. In the present
- PMID 23586433
- Sequence-specific, RNA-protein interactions overcome electrostatic barriers preventing assembly of satellite tobacco necrosis virus coat protein.
- Ford RJ, Barker AM, Bakker SE, Coutts RH, Ranson NA, Phillips SE, Pearson AR, Stockley PG.SourceAstbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, UK.
- Journal of molecular biology.J Mol Biol.2013 Mar 25;425(6):1050-64. doi: 10.1016/j.jmb.2013.01.004. Epub 2013 Jan 11.
- We have examined the roles of RNA-coat protein (CP) interactions in the assembly of satellite tobacco necrosis virus (STNV). The viral genomic RNA encodes only the CP, which comprises a β-barrel domain connected to a positively charged N-terminal extension. In the previous crystal structures of thi
- PMID 23318955
Japanese Journal
- 21aPSA-28 ウイルスカプシド形成の粗視化モデルシミュレーション(2)(21aPSA 領域12ポスターセッション,領域12(ソフトマター物理,化学物理,生物物理))
- 26pPSB-38 粗視化モデルによるウイルスキャプシド形成シミュレーション(26pPSB 領域12ポスターセッション,領域12(ソフトマター物理,化学物理,生物物理))
- CHARACTERISTICS OF CORYNEBACTERIUM RENALE PHAGE
- YANAGAWA Ryo,SHINAGAWA Morikazu
- Japanese Journal of Veterinary Research 16(4), 137-144_3, 1968-12-00
- … The tail is exhibiting a capsomere structure. …
- NAID 110001073982
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- The capsomere is a basic subunit of the capsid, an outer covering of protein that protects the genetic material of a virus. Capsomeres self-assemble to form the capsid. In this diagram of an Adenovirus, the capsid molecules are clearly visible.
- cap·so·mere (k p s -mîr ) or cap·so·mer (-m r). n. A subunit of a viral capsid. capsomere. [kap′səmir]. one of the building blocks of a viral capsid. It consists of groups of identical protein molecules and is visible in an electron microscope.
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