The three-dimensional structure of the bacterial virus MS2

Valegård, K.; Liljas, Lars; Fridborg, K.; Unge, Torsten

doi:10.1038/345036a0

Cited by 383 publications

(376 citation statements)

References 41 publications

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“…12,20−22 In phage and VLPs, the MS2 CP forms dimers that assemble into an icosahedron with 12 pentameric and 20 hexameric facesa so-called T = 3 geometry. The structure of MS2 particles has been extensively characterized, [23][24][25][26]14 but, as with other multimeric assemblies, no point mutations are known to confer uniform changes in the icosahedral supramolecular structure adopted by the CP. If these could be identified, the mutants would serve as useful tools for exploring the effects of VLP size on engineered MS2 VLP performance for drug delivery and imaging applications.…”

mentioning

confidence: 99%

A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle

Asensio¹,

Morella²,

Jakobson³

et al. 2016

Nano Lett.

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Virus-like particles are used to encapsulate drugs, imaging agents, enzymes, and other biologically active molecules in order to enhance their function. However, the size of most virus-like particles is inflexible, precluding the design of appropriately sized containers for different applications. Here, we describe a chromatographic selection for virus-like particle assembly. Using this selection, we identified a single amino acid substitution to the coat protein of bacteriophage MS2 that mediates a uniform switch in particle geometry from T = 3 to T = 1 icosahedral symmetry. The resulting smaller particle retains the ability to be disassembled and reassembled in vitro and to be chemically modified to load cargo into its interior cavity. The pair of 27 and 17 nm MS2 particles will allow direct examination of the effect of size on function in established applications of virus-like particles, including drug delivery and imaging.

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mentioning

confidence: 99%

A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle

Asensio¹,

Morella²,

Jakobson³

et al. 2016

Nano Lett.

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“…and M.G.R., manuscript in preparation). Difference Fouriers at various resolutions showed that the Babinet opposite solution had been obtained 41,56 . The phases were, therefore, flipped (α → π + α) before plotting the final electron density map.…”

Section: Figmentioning

confidence: 99%

“…The eight-stranded antiparallel virus fold has now been found in many RNA and DNA viral capsids 39 , yet its presence is not entirely universal (for example in the plant RNA tobacco mosaic virus 54,55 , in the RNA phage MS2 56 and in the animal RNA Sindbis virus 57 ). Hence, the eight-stranded antiparallel β-barrel fold is not a prerequisite for assembly of icosahedral structures 58 .…”

Section: Evolutionmentioning

confidence: 99%

Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications

McKenna

Xia

Willingmann

et al. 1992

Nature

217

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The mechanism of DNA ejection, viral assembly and evolution are related to the structure of bacteriophage ΦX174. The F protein forms a T = 1 capsid whose major folding motif is the eightstranded antiparallel β barrel found in many other icosahedral viruses. Groups of 5 G proteins form 12 dominating spikes that enclose a hydrophilic channel containing some diffuse electron density. Each G protein is a tight β barrel with its strands running radially outwards and with a topology similar to that of the F protein. The 12 'pilot' H proteins per virion may be partially located in the putative ion channel. The small, basic J protein is associated with the DNA and is situated in an interior cleft of the F protein. Tentatively, there are three regions of partially ordered DNA structure, accounting for about 12% of the total genome.Bacteriophage ΦX174 is a small icosahedral virus that contains a single-stranded, closed circular DNA molecule with 5,386 nucleotide bases (for a recent review, see ref. 1). Of the 11 gene products, four (J, F, G and H) participate in the structure of the virion. There are 60 copies each of the J, F and G proteins and 12 copies of the H protein per virion [2][3][4] (Table 1). Electron microscopy of shadowed or negatively stained particles [5][6][7][8] , as well as a threedimensional reconstruction of frozen-hydrated virions (Fig. 1a), clearly show large spikes at the vertices of the icosahedral particles (N.H.O., T.S.B., P.W. and N.L.I., manuscript in preparation). These spikes are about 32 Å long and have a mean diameter of 70 Å. Edgell et al. 3 have shown that these spikes, which can be removed from the capsid with 4 M urea treatment, are composed of G and H proteins. Assuming all 12 spikes are identical, then each spike will contain five G and one H protein 2 . The capsid itself has an external diameter of roughly 260 Å, with a protein shell that is about 30 Å thick, and contains the F and J proteins as well as the single-stranded (ss) DNA. The phage recognizes a lipopolysaccharide (LPS) receptor on the outer cell membrane of Escherichia coli [8][9][10][11] . Host range mutants, which determine which strains of E. coli are infected by ΦX174, map into the F, G and H genes [12][13][14][15] The infectious virion has a relative molecular mass of 6.2 × 10 6 (M r 6,200K) (26% is DNA) 32 . Lysates of infected E. coli contain two components which can be separated by sedimentation through a sucrose gradient 32,33 . The fast band contains the infectious 114S particles whereas the slow band contains noninfectious, 70S particles 32,34,35 . The latter contains about 20% of the normal DNA content with all of the genome represented in the population of particles. Both types of particles can be crystallized into isomorphous monoclinic crystals with space group P2 1 , and cell dimensions a = 305.6, b = 360.8, c = 299.5 Å, β = 92.89° that diffract at least to 2.6-Å resolution 33 . The asymmetric unit of the crystal cell contains one complete particle. We report here the three-dimensional structure...

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“…(9) It is a non-enveloped virus similar in physical characteristics to pathogenic enteroviruses and commonly used as a surrogate for human viruses. An individual MS2 virion is nearly spherical with an average diameter ∼28 nm, making it one of the smallest viruses.…”

Section: Ms2 Virusmentioning

confidence: 99%

Performance of Conventional and Antimicrobial-Treated Filtering Facepiece Respirators Challenged with Biological Aerosols

Lore

Sebastian

Brown

et al. 2012

Journal of Occupational and Environmental Hygiene

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The three-dimensional structure of the bacterial virus MS2

Cited by 383 publications

References 41 publications

A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle

A Selection for Assembly Reveals That a Single Amino Acid Mutant of the Bacteriophage MS2 Coat Protein Forms a Smaller Virus-like Particle

Atomic structure of single-stranded DNA bacteriophage ΦX174 and its functional implications

Performance of Conventional and Antimicrobial-Treated Filtering Facepiece Respirators Challenged with Biological Aerosols

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