Structure of Small Viruses

Crick, Francis; Watson, James D.

doi:10.1038/177473a0

Cited by 681 publications

(344 citation statements)

References 15 publications

Supporting

Mentioning

336

Contrasting

Unclassified

Order By: Relevance

“…[8][9][10][11][12][13][14][15][16][17]) and insightful theoretical works (e.g. [18][19][20][21][22][23][24][25][26][27][28][29][30][31]). The in vivo replication of many viruses, however, involves simultaneous assembly and encapsidation of the viral genome [32].…”

Section: Introductionmentioning

confidence: 99%

Controlling viral capsid assembly with templating

Hagan

2008

Phys. Rev. E

104

View full text Add to dashboard Cite

We develop coarse-grained models that describe the dynamic encapsidation of functionalized nanoparticles by viral capsid proteins. We find that some forms of cooperative interactions between protein subunits and nanoparticles can dramatically enhance rates and robustness of assembly, as compared to the spontaneous assembly of subunits into empty capsids. For large core-subunit interactions, subunits adsorb onto core surfaces en masse in a disordered manner, and then undergo a cooperative rearrangement into an ordered capsid structure. These assembly pathways are unlike any identified for empty capsid formation. Our models can be directly applied to recent experiments in which viral capsid proteins assemble around the functionalized inorganic nanoparticles [Sun et al., Proc. Natl. Acad. Sci (2007) 104, 1354. In addition, we discuss broader implications for understanding the dynamic encapsidation of single-stranded genomic molecules during viral replication and for developing multicomponent nanostructured materials.

show abstract

Section: Introductionmentioning

confidence: 99%

Controlling viral capsid assembly with templating

Hagan

2008

Phys. Rev. E

104

View full text Add to dashboard Cite

show abstract

“…Spherical virus capsids, for example, enclose space by using the geometry of the icosahedron, thus exploiting the economy of this form in terms of both surface area-to-volume ratio and genetic efficiency of subunit-based symmetric assembly (1). These capsids have 6 fivefold rotation axes, 10 threefold axes, and 15 twofold axes, providing equivalent environments for 60 identical subunits.…”

mentioning

confidence: 99%

Chemical mimicry of viral capsid self-assembly

Olson

Keinan

2007

Proc. Natl. Acad. Sci. U.S.A.

102

View full text Add to dashboard Cite

Stable structures of icosahedral symmetry can serve numerous functional roles, including chemical microencapsulation and delivery of drugs and biomolecules, epitope presentation to allow for an efficient immunization process, synthesis of nanoparticles of uniform size, observation of encapsulated reactive intermediates, formation of structural elements for supramolecular constructs, and molecular computing. By examining physical models of spherical virus assembly we have arrived at a general synthetic strategy for producing chemical capsids at size scales between fullerenes and spherical viruses. Such capsids can be formed by self-assembly from a class of molecules developed from a symmetric pentagonal core. By designing chemical complementarity into the five interface edges of the molecule, we can produce self-assembling stable structures of icosahedral symmetry. We considered three different binding mechanisms: hydrogen bonding, metal binding, and formation of disulfide bonds. These structures can be designed to assemble and disassemble under controlled environmental conditions. We have conducted molecular dynamics simulation on a class of corannulene-based molecules to demonstrate the characteristics of self-assembly and to aid in the design of the molecular subunits. The edge complementarities can be of diverse structure, and they need not reflect the fivefold symmetry of the molecular core. Thus, self-assembling capsids formed from coded subunits can serve as addressable nanocontainers or custom-made structural elements.corannulene ͉ icosahedral capsids ͉ molecular containers ͉ physical modeling ͉ nanotechnology

show abstract

“…Crick & Watson (1956) presented a powerful hypothesis, based on genetic economy and protein interactions, to suggest that in simple viruses the coats would be made from multiple copies of a coat protein, symmetrically arranged. For rod-shaped viruses, this would imply helical symmetry, whereas for spherical or isometric viruses the symmetry would be cubic.…”

Section: Specimen Preparationmentioning

confidence: 99%

The Leeuwenhoek lecture 2006. Microscopy goes cold: frozen viruses reveal their structural secrets

Crowther

2007

Phil. Trans. R. Soc. B

View full text Add to dashboard Cite

The electron microscope provides a powerful tool for investigating the structure of biological complexes such as viruses. A modern instrument is fully capable of atomic resolution on suitable non-biological specimens, but biological materials are difficult to preserve, owing to their fragility, and to image, owing to their radiation, sensitivity. The act of imaging the specimen severely damages it. Originally, samples were prepared by staining with a heavy metal salt, which provides a stable specimen but limits the amount of details that can be retrieved. Now particulate specimens, such as viruses, are prepared by rapid freezing of unstained material and observed in a frozen state with low doses of electrons. The resulting images require extensive computer processing to extract fully detailed three-dimensional information about the specimen. The whole process is referred to as single-particle electron cryomicroscopy. Using this approach, the structure of the human hepatitis B virus core was solved at the level of the protein fold. By comparing maps of RNA-and DNAcontaining cores, it was possible to propose a model for the maturation and control of the envelopment of the virus during assembly. These examples show that cryomicroscopy offers great potential for understanding the structure and function of complex biological assemblies.

show abstract

Structure of Small Viruses

Cited by 681 publications

References 15 publications

Controlling viral capsid assembly with templating

Controlling viral capsid assembly with templating

Chemical mimicry of viral capsid self-assembly

The Leeuwenhoek lecture 2006. Microscopy goes cold: frozen viruses reveal their structural secrets

Contact Info

Product

Resources

About