scholarly journals Dynamics of Icosahedral Viruses: What Does Viral Tiling Theory Teach Us?

2008 ◽  
Vol 9 (3-4) ◽  
pp. 211-220 ◽  
Author(s):  
Kasper Peeters ◽  
Anne Taormina
Keyword(s):  
Vibrational Spectra ◽  
Coarse Graining ◽  
Point Mass ◽  
Inversion Symmetry ◽  
Top Down ◽  
Virus Capsid ◽  
Virus Capsids ◽  
Icosahedral Virus ◽  
Icosahedral Viruses

We present a top-down approach to the study of the dynamics of icosahedral virus capsids, in which each protein is approximated by a point mass. Although this represents a rather crude coarse-graining, we argue that it highlights several generic features of vibrational spectra which have been overlooked so far. We furthermore discuss the consequences of approximate inversion symmetry as well as the role played by viral tiling theory in the study of virus capsid vibrations.

A Dissection of the Protein–Protein Interfaces in Icosahedral Virus Capsids

2007 ◽  
Vol 367 (2) ◽  
pp. 574-590 ◽  
Author(s):  
Ranjit Prasad Bahadur ◽  
Francis Rodier ◽  
Joël Janin
Keyword(s):  
Protein Interfaces ◽  
Virus Capsids ◽  
Icosahedral Virus

scholarly journals The Closest Relatives of Icosahedral Viruses of Thermophilic Bacteria Are among Viruses and Plasmids of the Halophilic Archaea

2009 ◽  
Vol 83 (18) ◽  
pp. 9388-9397 ◽  
Author(s):  
Matti Jalasvuori ◽  
Silja T. Jaatinen ◽  
Simonas Laurinavičius ◽  
Elina Ahola-Iivarinen ◽  
Nisse Kalkkinen ◽  
...  
Keyword(s):  
Thermophilic Bacteria ◽  
Thermus Thermophilus ◽  
Halophilic Archaea ◽  
Structural Proteins ◽  
The Novel ◽  
Viral Membrane ◽  
Double Stranded Dna ◽  
Icosahedral Virus ◽  
Bacteriophage Genome ◽  
Icosahedral Viruses

ABSTRACT We have sequenced the genome and identified the structural proteins and lipids of the novel membrane-containing, icosahedral virus P23-77 of Thermus thermophilus. P23-77 has an ∼17-kb circular double-stranded DNA genome, which was annotated to contain 37 putative genes. Virions were subjected to dissociation analysis, and five protein species were shown to associate with the internal viral membrane, while three were constituents of the protein capsid. Analysis of the bacteriophage genome revealed it to be evolutionarily related to another Thermus phage (IN93), archaeal Halobacterium plasmid (pHH205), a genetic element integrated into Haloarcula genome (designated here as IHP for integrated Haloarcula provirus), and the Haloarcula virus SH1. These genetic elements share two major capsid proteins and a putative packaging ATPase. The ATPase is similar with the ATPases found in the PRD1-type viruses, thus providing an evolutionary link to these viruses and furthering our knowledge on the origin of viruses.

Deltahedral views of fullerene polymorphism

1993 ◽  
Vol 343 (1667) ◽  
pp. 133-144 ◽  
Keyword(s):  
Virus Particles ◽  
Lattice Symmetry ◽  
Surface Lattice ◽  
Lower Symmetry ◽  
Icosahedral Virus ◽  
Buckminster Fuller ◽  
Icosahedral Viruses ◽  
Underlying Geometry ◽  
Triangulation Number ◽  
Geodesic Dome

Fullerenes and icosahedral virus particles share the underlying geometry applied by Buckminster Fuller in his geodesic dome designs. The basic plan involves the construction of polyhedra from 12 pentagons together with some number of hexagons, or the symmetrically equivalent construction of triangular faceted surface lattices (deltahedra) with 12 five-fold vertices and some number of six-fold vertices. All the possible designs for icosahedral viruses built according to this plan were enumerated according to the triangulation number T = ( h 2 + hk + k 2 of icosadelta-hedra formed by folding equilateral triangular nets with lattice vectors of indices h, k connecting neighbouring five-fold vertices. Lower symmetry deltahedra can be constructed in which the vectors connecting five-fold vertices are not all identical. Applying the pentagon isolation rule, the possible designs for fullerenes with more than 20 hexagonal facets can be defined by the set of vectors in the surface lattice net of the corresponding deltahedra. Surface lattice symmetry and geometrical relations among fullerene isomers can be displayed more directly in unfolded deltahedral nets than in projected views of the deltahedra or their hexagonally and pentagonally facted dual polyhedra.

scholarly journals Asymmetrizing an icosahedral virus capsid by hierarchical assembly of subunits with designed asymmetry

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Zhongchao Zhao ◽  
Joseph Che-Yen Wang ◽  
Mi Zhang ◽  
Nicholas A. Lyktey ◽  
Martin F. Jarrold ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Medical Applications ◽  
Virus Capsid ◽  
Viral Capsids ◽  
Hierarchical Assembly ◽  
Assembly Pathway ◽  
B Virus ◽  
Icosahedral Virus ◽  
Surface Chemistries ◽  
Virus Capsid Protein

AbstractSymmetrical protein complexes are ubiquitous in biology. Many have been re-engineered for chemical and medical applications. Viral capsids and their assembly are frequent platforms for these investigations. A means to create asymmetric capsids may expand applications. Here, starting with homodimeric Hepatitis B Virus capsid protein, we develop a heterodimer, design a hierarchical assembly pathway, and produce asymmetric capsids. In the heterodimer, the two halves have different growth potentials and assemble into hexamers. These preformed hexamers can nucleate co-assembly with other dimers, leading to Janus-like capsids with a small discrete hexamer patch. We can remove the patch specifically and observe asymmetric holey capsids by cryo-EM reconstruction. The resulting hole in the surface can be refilled with fluorescently labeled dimers to regenerate an intact capsid. In this study, we show how an asymmetric subunit can be used to generate an asymmetric particle, creating the potential for a capsid with different surface chemistries.

Organization of dsDNA in icosahedral virus capsids

1992 ◽  
Vol 50 (1) ◽  
pp. 452-453 ◽  
Author(s):  
Frank P. Booy ◽  
Benes L. Trus ◽  
William W. Newcomb ◽  
Jay C. Brown ◽  
Philip Serwer ◽  
...  
Keyword(s):  
Structural Biology ◽  
Viral Capsids ◽  
Viral Genomes ◽  
Nucleic Acid Molecule ◽  
Cryo Electron Microscopy ◽  
Virus Capsids ◽  
Icosahedral Virus ◽  
Dna Strands ◽  
Simplex Virus

Condensation/decondensation reactions which effect the packaging of viral genomes into their capsids and their subsequent release constitute one of the basic phenomena which structural biology seeks to explain. The appropriate nucleic acid molecule(s) must be selected; then packaged at a high density to allow efficient utilization of the available space; the mutual electrostatic repulsion of DNA strands must somehow be overcome; and the arrangement of the DNA must allow for its ready release upon initiation of infection. Cryo-electron microscopy has emerged as an incisive tool for visualizing the internal organization of packaged DNA inside viral capsids. We illustrate its effectiveness with observations relating to bacteriophages T4, T7, and herpes simplex virus, type 1 (HSV-1).

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