The crystallographic structure of brome mosaic virus

Lucas, Robert W.; Larson, Steven B.; McPherson, Alexander

doi:10.1006/jmbi.2001.5389

Cited by 136 publications

(197 citation statements)

References 34 publications

(44 reference statements)

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“…Thus, VLP 9 is similar to a pseudoT ϭ 2 arrangement previously determined for the RNA-controlled 120-unit BMV capsid (24) (Fig. 4C).…”

supporting

confidence: 81%

“…Crystals were grown according to a protocol modified from the one outlined by Lucas et al for BMV (24). Three-dimensional crystals of BMV and VLP have been prepared by the hanging drop vapor diffusion method.…”

Section: Transmission Electron Microscopymentioning

confidence: 99%

“…BMV is a small icosahedral virus (Ϸ280 Å) that infects Poaceae species (23). The crystal structure of the native BMV has been solved and is composed of 180 identical proteins of 20 kDa that form pentameric or hexameric subunits in a T ϭ 3 lattice (24). The basic subunit of assembly is a dimer.…”

mentioning

confidence: 99%

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Core-controlled polymorphism in virus-like particles

Sun

Dufort²,

Daniel³

et al. 2007

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

271

363

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This study concerns the self-assembly of virus-like particles (VLPs) composed of an icosahedral virus protein coat encapsulating a functionalized spherical nanoparticle core. The recent development of efficient methods for VLP self-assembly has opened the way to structural studies. Using electron microscopy with image reconstruction, the structures of several VLPs obtained from brome mosaic virus capsid proteins and gold nanoparticles were elucidated. Varying the gold core diameter provides control over the capsid structure. The number of subunits required for a complete capsid increases with the core diameter. The packaging efficiency is a function of the number of capsid protein subunits per gold nanoparticle. VLPs of varying diameters were found to resemble to three classes of viral particles found in cells (T ‫؍‬ 1, 2, and 3). As a consequence of their regularity, VLPs form three-dimensional crystals under the same conditions as the wild-type virus. The crystals represent a form of metallodielectric material that exhibits optical properties influenced by multipolar plasmonic coupling. metamaterials ͉ protein cage ͉ self-assembly ͉ surface plasmon ͉ virus assembly E ngineered virus capsids and protein cage structures have shown increasing promise as therapeutic and diagnostic vectors (1-6), imaging agents (7-10), and as templates and microreactors for advanced nanomaterials synthesis (11)(12)(13)(14)(15)(16)(17). Here, we address the rules for the formation of symmetric protein cages consisting of viral capsid subunits formed over a functionalized inorganic nanoparticle core, called virus-like particles (VLPs).VLPs provide an example of how biomimetic self-organization can combine the natural characteristics of virus capsids with the exquisite physical properties of nanoparticles (18)(19)(20). Interactions between the artificial cargo and the protein carrier affects both the self-assembly and the stability of the resulting structure, yet very little is known about them. Progress toward the basic development and the practical use of VLPs requires an understanding of how relevant parameters contribute to complex formation.Symmetric VLPs may provide a technology for therapeutic or diagnostic agent delivery that is improved over amorphous shell nanoparticles that are already known to be efficient in similar applications (21). The advantage of a regular surface protein motif is that the binding domains are functionally identical by virtue of their equivalent environment. It has been shown in several situations that receptor-mediated targeting can be achieved even when using amorphous coatings (22). However, the principle challenges for nanoparticle delivery currently include: limited life-time in body fluids, nanoparticle transduction across the cellular membrane, avoidance of the exocytotic pathways, and target specificity. To optimize their infectivity, viruses have evolved to overcome these challenges. We still must learn how to apply virus strategies to targeted delivery. A simple question is central to this o...

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“…Thus, VLP 9 is similar to a pseudoT ϭ 2 arrangement previously determined for the RNA-controlled 120-unit BMV capsid (24) (Fig. 4C).…”

supporting

confidence: 81%

Section: Transmission Electron Microscopymentioning

confidence: 99%

See 1 more Smart Citation

Core-controlled polymorphism in virus-like particles

Sun

Dufort²,

Daniel³

et al. 2007

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

271

363

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“…22 The virions are about 280 Å in diameter 23 and the structure of the native TZ3 particle has been solved in this laboratory by X-ray crystallography. 24 BMV virions are frequently characterized structurally as being rather loose assemblies that depend upon protein-nucleic acid interactions and divalent cations to maintain their integrity. 24,25,26 Indeed, Mg 2C on quasi-3-fold axes coordinated to three quasi-symmetrically equivalent aspartic acid residues are observed in the native structure.…”

Section: Introductionmentioning

confidence: 99%

Crystallographic Structure of the T=1 Particle of Brome Mosaic Virus

Larson

Lucas

McPherson

2005

Journal of Molecular Biology

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TZ1 icosahedral particles of amino terminally truncated brome mosaic virus (BMV) protein were created by treatment of the wild-type TZ3 virus with 1 M CaCl 2 and crystallized from sodium malonate. Diffraction data were collected from frozen crystals to beyond 2.9 Å resolution and the structure determined by molecular replacement and phase extension. The particles are composed of pentameric capsomeres from the wild-type virions which have reoriented with respect to the original particle pentameric axes by rotations of 378, and formed tenuous interactions with one another, principally through conformationally altered C-terminal polypeptides. Otherwise, the pentamers are virtually superimposable upon those of the original TZ3 BMV particles. The TZ1 particles, in the crystals, are not perfect icosahedra, but deviate slightly from exact symmetry, possibly due to packing interactions. This suggests that the TZ1 particles are deformable, which is consistent with the loose arrangement of pentamers and latticework of holes that penetrate the surface. Atomic force microscopy showed that the TZ3 to TZ1 transition could occur by shedding of hexameric capsomeres and restructuring of remaining pentamers accompanied by direct condensation. Knowledge of the structures of the BMV wild-type and TZ1 particles now permit us to propose a tentative model for that process. A comparison of the BMV TZ1 particles was made with the reassembled TZ1 particles produced from the coat protein of trypsin treated alfalfa mosaic virus (AlMV), another bromovirus. There is little resemblance between the two particles. The BMV particle, with a maximum diameter of 195 Å , is made from distinctive pentameric capsomeres with large holes along the 3-fold axis, while the AlMV particle, of approximate maximum diameter 220 Å , has subunits closely packed around the 3-fold axis, large holes along the 5-fold axis, and few contacts within pentamers. In both particles crucial linkages are made about icosahedral dyads.

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“…The crystallographic structure of BMV virions has been determined (23). RNA regions or elements involved in the packaging of BMV RNAs have been assigned to the coding region of BMV RNA1 by UV cross-linking and band-shift assays (11) as well as to the 3Ј-proximal region of the 3a open reading frame (ORF) in RNA3 (9).…”

mentioning

confidence: 99%

cis -Acting Elements Required for Efficient Packaging of Brome Mosaic Virus RNA3 in Barley Protoplasts

Damayanti

Tsukaguchi

Mise

et al. 2003

J Virol

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Viral RNAs are specifically selected for packaging during viral infection. Specific packaging occurs through an interaction between viral RNAs and structural coat proteins (CPs). The specific recognition of viral RNAs by CPs plays a crucial role in diverse facets of the viral life cycle and in the packaging event. The binding of CP to specific RNA elements is required for viral protein translation during infection initiation in alfalfa mosaic virus (28) and for the regulation of translation and the initiation of RNA packaging in the RNA phages (38). In retroviruses, nucleocapsid protein is thought to stimulate genomic RNA dimerization, which is required for efficient RNA packaging, reverse transcription, and recombination (14, 31). Many plant viruses require RNA packaging for systemic spread and for cell-to-cell movement (3, 10). Therefore, the CP-RNA interaction is a critical event in the viral life cycle. Compared with the characterization of trans-acting factors such as CP in RNA packaging, however, the RNA elements involved in specific packaging have not been well characterized for many viruses. One of the best-characterized RNA elements is "origin of assembly" of tobacco mosaic virus (36, 40). cis-acting sequences for RNA packaging have also been demonstrated in several icosahedral viruses, including flock house virus (39), Sindbis virus (37), hepatitis B virus (17), the human immunodeficiency viruses (2,14,22), and turnip crinkle virus (32).Brome mosaic virus (BMV) is an icosahedral plant RNA virus and is the type member of the genus Bromovirus in the family Bromoviridae in the alphavirus-like superfamily (18). The genome of BMV consists of three species of messenger sense single-stranded RNA (1). RNA1 (3.2 kb) and RNA2 (2.9 kb), which encode the 1a and 2a replicase proteins, respectively (1, 13, 19), are packaged separately into individual particles (21). RNA3 (2.1 kb), which encodes the 3a cell-to-cell movement protein (35), is packaged into a single particle together with subgenomic RNA4 (0.9 kb) (21). RNA4 is synthesized from the minus strand of RNA3 (25) and encodes CP. CP is required for packaging, cell-to-cell movement, and the systemic spread of the virus (29,33,34).A highly conserved N-terminal arginine-rich motif in BMV CP plays an important role in BMV RNA packaging through RNA-CP interactions (4,5,33,34). The crystallographic structure of BMV virions has been determined (23). RNA regions or elements involved in the packaging of BMV RNAs have been assigned to the coding region of BMV RNA1 by UV cross-linking and band-shift assays (11) as well as to the 3Ј-proximal region of the 3a open reading frame (ORF) in RNA3 (9). The tRNA-like structures (TLS) in the 3Ј-untranslated regions of BMV RNAs also play a crucial role in BMV RNA packaging in vitro (6). In the present study, we delimit a nucleotide sequence required for the efficient packaging of BMV RNA3 and show that 69 nucleotides (nt) in the 3Ј-proximal region of the BMV 3a ORF, especially a predicted stem-loop structure (30 nt), is essential fo...

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The crystallographic structure of brome mosaic virus

Cited by 136 publications

References 34 publications

Core-controlled polymorphism in virus-like particles

Core-controlled polymorphism in virus-like particles

Crystallographic Structure of the T=1 Particle of Brome Mosaic Virus

cis -Acting Elements Required for Efficient Packaging of Brome Mosaic Virus RNA3 in Barley Protoplasts

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