Self-assembly approaches to nanomaterial encapsulation in viral protein cages

Aniagyei, Stella E.; DuFort, Christopher C.; Kao, C. Cheng; Dragnea, Bogdan

doi:10.1039/b805874c

Cited by 105 publications

(103 citation statements)

References 92 publications

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“…They can subsequently be assembled efficiently in vitro to VLPs and encapsidate under specific conditions cargo materials such as ssRNA (Aniagyei et al, 2008). Cowpea chlorotic mottle virus (CCMV; Bromoviridae) VLPs, for instance, have been shown to incorporate heterologous ssRNAs of different sizes (Cadena-Nava et al, 2012).…”

Section: Virus-like Particlesmentioning

confidence: 99%

Viral Delivery of dsRNA for Control of Insect Agricultural Pests and Vectors of Human Disease: Prospects and Challenges

et al. 2017

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RNAi is applied as a new and safe method for pest control in agriculture but efficiency and specificity of delivery of dsRNA trigger remains a critical issue. Various agents have been proposed to augment dsRNA delivery, such as engineered micro-organisms and synthetic nanoparticles, but the use of viruses has received relatively little attention. Here we present a critical view of the potential of the use of recombinant viruses for efficient and specific delivery of dsRNA. First of all, it requires the availability of plasmid-based reverse genetics systems for virus production, of which an overview is presented. For RNA viruses, their application seems to be straightforward since dsRNA is produced as an intermediate molecule during viral replication, but DNA viruses also have potential through the production of RNA hairpins after transcription. However, application of recombinant virus for dsRNA delivery may not be straightforward in many cases, since viruses can encode RNAi suppressors, and virus-induced silencing effects can be determined by the properties of the encoded RNAi suppressor. An alternative is virus-like particles that retain the efficiency and specificity determinants of natural virions but have encapsidated non-replicating RNA. Finally, the use of viruses raises important safety issues which need to be addressed before application can proceed.

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Section: Virus-like Particlesmentioning

confidence: 99%

Viral Delivery of dsRNA for Control of Insect Agricultural Pests and Vectors of Human Disease: Prospects and Challenges

et al. 2017

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“…[5] In many cases, the synthesis and structuration of hybrid nano-objects is achieved under equilibrium or non-equilibrium conditions through a range of strategies involving integrative, higher-order, or transformative self-assembly. [6,7] Often these approaches involve the confinement and templating of reactions on or within supramolecular assemblies such as dendrimers, [8] organogel nanofilaments, [9] peptide fibers, [10] helical micelles, [11] virus capsids, [12] and protein cages. [13] Recently, cross-linked lysozyme crystals, approximately 200 mm in size, have been used to prepare nanoplasmonic arrays by intracrystalline metallization, [14] suggesting that the high mesoporosity of protein crystals might be exploited in general for the template-directed assembly of organized inorganic nanostructures across a range of length scales.…”

mentioning

confidence: 99%

Microemulsion‐Mediated Self‐Assembly and Silicification of Mesostructured Ferritin Nanocrystals

Lambert

Viravaidya

et al. 2010

Angew Chem Int Ed

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Nanoscale objects with advanced structure and function are of considerable interest in areas such as sensing, drug delivery and bioelectronics, [1,2] and have important implications for biotoxicity [3,4] and the emergence of life. [5] In many cases, the synthesis and structuration of hybrid nano-objects is achieved under equilibrium or non-equilibrium conditions through a range of strategies involving integrative, higher-order, or transformative self-assembly. [6,7] Often these approaches involve the confinement and templating of reactions on or within supramolecular assemblies such as dendrimers, [8] organogel nanofilaments, [9] peptide fibers, [10] helical micelles, [11] virus capsids, [12] and protein cages. [13] Recently, cross-linked lysozyme crystals, approximately 200 mm in size, have been used to prepare nanoplasmonic arrays by intracrystalline metallization, [14] suggesting that the high mesoporosity of protein crystals might be exploited in general for the template-directed assembly of organized inorganic nanostructures across a range of length scales. Whilst many common proteins readily form crystals with macroscopic dimensions, it is generally difficult to produce nanoscale counterparts that would be effective as templates for the preparation of discrete hybrid nanomaterials. In this regard, the iron storage protein, ferritin, which consists of a 12 nm diameter spherical polypeptide shell enclosing a 5-6 nm sized iron oxide core [15] is known to readily form two-dimensional (2D) superlattices on various substrates [16] and can be clustered into aggregates in solution using biotin-streptavidin linkages or inorganic nanoparticles.[17] It should therefore be possible to control the self-assembly of discrete nanometersized ferritin crystals, and as a consequence use these nanocrystals as porous templates for the fabrication of hybrid nanoparticles with ordered mesostructured interiors.Here, we use water-in-oil microemulsion droplets as a medium for controlling the aggregation of entrapped ferritin molecules to produce discrete protein nanocrystals that can be stabilized by in situ silicification of the intracrystalline voids to produce mesostructured silica-ferritin hybrids. Microemulsions are versatile reaction media for the confinement and synthesis of inorganic nanoparticles, [18] nanowires, [19] nanoparticle superlattices, [20] and complex hierarchical architectures.[21] In addition, microemulsion droplets have been used for the encapsulation of drugs, [22] exploration of organic chemical reactions, [23] entrapment of functional enzymes, [24] and for the separation of protein mixtures.[25]Although droplet instability can often be a problem in these applications, herein we demonstrate that protein-mediated aggregation of the water pools can be exploited to produce discrete ferritin nanocrystals and silicified counterparts with well-ordered close packed structures. As silicification of the interstitial pores occurs with high precision and without degradation of the protein, it should be possible to ex...

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“…To determine the coordinates of three symmetrically nonequivalent positions of the fourth (Caspar-Klug) tiling, the following system of equations should be solved (2) where r n = (x n ,y n ,z n ), n=1..3 are the coordinates of the target symmetrically nonequivalent positions, defining the idealized tessellation, matrix defines rotation by an angle of -2π/3 about the three-fold axis (1, 0, τ 2 ). The first five equations correspond to the equality of six symmetrically nonequivalent edges of tiling structural elements, the sixth equation corresponds to the requirement that two symmetrically nonequivalent internal angles of the spherical hexagon would be equal (Fig.…”

Section: Construction Of Idealized Spherical Tilingsmentioning

confidence: 99%

“…It is well known that host cell infection by a virus strongly depends on the protein arrangement in the capsid [1][2][3], i.e., the solid viral shell consisting of molecules of the same type (more rarely, of several types) and protecting the virus genome from external influences. This arrangement is regular, symmetric, and has a high degree of positional and orientational ordering of protein molecules.…”

Section: Introductionmentioning

confidence: 99%

Structures of spherical viral capsids as quasicrystalline tilings

2015

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Abstract-Spherical viral shells with icosahedral symmetry have been considered as quasicrystalline tilings. Similarly to known Caspar-Klug quasi-equivalence theory, the presented approach also minimizes the number of conformations necessary for the protein molecule bonding with its neighbors in the shell, but is based on different geometrical principles. It is assumed that protein molecule centers are located at vertices of tiles with identical edges, and the number of different tile types is minimal. Idealized coordinates of nonequivalent by symmetry protein positions in six various capsid types are obtained. The approach describes in a uniform way both the structures satisfying the well-known Caspar-Klug geometrical model and the structures contradicting this model.

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Self-assembly approaches to nanomaterial encapsulation in viral protein cages

Abstract: A perspective on abiotic material encapsulation inside virus capsids is provided. The emphasis is on the physical principles of virus assembly relevant to packaging, strategies for encapsulation and capsid modification, and on emerging applications.

Cited by 105 publications

References 92 publications

Viral Delivery of dsRNA for Control of Insect Agricultural Pests and Vectors of Human Disease: Prospects and Challenges

Viral Delivery of dsRNA for Control of Insect Agricultural Pests and Vectors of Human Disease: Prospects and Challenges

Microemulsion‐Mediated Self‐Assembly and Silicification of Mesostructured Ferritin Nanocrystals

Structures of spherical viral capsids as quasicrystalline tilings

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