The MS2 Coat Protein Shell is Likely Assembled Under Tension: A Novel Role for the MS2 Bacteriophage A Protein as Revealed by Small-angle Neutron Scattering

Kuzmanovic, Deborah A.; Elashvili, Ilya; Wick, Charles H.; O’Connell, Catherine M.; Krueger, Susan

doi:10.1016/j.jmb.2005.11.040

Cited by 29 publications

(27 citation statements)

References 81 publications

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“…The MS2 capsid is assembled under tension, and the virus transforms this stored energy to inject its genome into the host cell. 45 It is feasible that cleaving the CP backbone disrupts the scaffolding required to develop this tension, thereby reducing the energy available for genome injection.…”

Section: ■ Discussionmentioning

confidence: 99%

Virus Inactivation Mechanisms: Impact of Disinfectants on Virus Function and Structural Integrity

Wigginton

Pecson

Sigstam

et al. 2012

Environ. Sci. Technol.

323

355

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Oxidative processes are often harnessed as tools for pathogen disinfection. Although the pathways responsible for bacterial inactivation with various biocides are fairly well understood, virus inactivation mechanisms are often contradictory or equivocal. In this study, we provide a quantitative analysis of the total damage incurred by a model virus (bacteriophage MS2) upon inactivation induced by five common virucidal agents (heat, UV, hypochlorous acid, singlet oxygen, and chlorine dioxide). Each treatment targets one or more virus functions to achieve inactivation: UV, singlet oxygen, and hypochlorous acid treatments generally render the genome nonreplicable, whereas chlorine dioxide and heat inhibit host-cell recognition/binding. Using a combination of quantitative analytical tools, we identified unique patterns of molecular level modifications in the virus proteins or genome that lead to the inhibition of these functions and eventually inactivation. UV and chlorine treatments, for example, cause site-specific capsid protein backbone cleavage that inhibits viral genome injection into the host cell. Combined, these results will aid in developing better methods for combating waterborne and foodborne viral pathogens and further our understanding of the adaptive changes viruses undergo in response to natural and anthropogenic stressors.

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Section: ■ Discussionmentioning

confidence: 99%

Virus Inactivation Mechanisms: Impact of Disinfectants on Virus Function and Structural Integrity

Wigginton

Pecson

Sigstam

et al. 2012

Environ. Sci. Technol.

323

355

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show abstract

“…Comparisons of small angle neutron scattering and crystallography experiments on the bacteriophage MS2 showed a decrease in the thickness of the protein shell of 0.4 nm to 0.6 nm attributable to dehydration (Kuzmanovic et al, 2006). The effect may be more pronounced for surface proteins, like the HA protein fragments protruding from VLP surface loops considered herein, that may flap loosely in solution but collapse on the surface upon dehydration (Kuzmanovic et al, 2006). If all of the difference in external size were attributed to drying then the size of the virus would shrink by 27-43% for the VLP w/o DNA sample.…”

Section: Comparison Of Es-dma and Affff-malsmentioning

confidence: 99%

Quantitative characterization of virus‐like particles by asymmetrical flow field flow fractionation, electrospray differential mobility analysis, and transmission electron microscopy

Pease

Lipin

Tsai

et al. 2008

Biotech & Bioengineering

106

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Here we characterize virus-like particles (VLPs) by three very distinct, orthogonal, and quantitative techniques: electrospray differential mobility analysis (ES-DMA), asymmetric flow field-flow fractionation with multi-angle light scattering detection (AFFFF-MALS) and transmission electron microscopy (TEM). VLPs are biomolecular particles assembled from viral proteins with applications ranging from synthetic vaccines to vectors for delivery of gene and drug therapies. VLPs may have polydispersed, multimodal size distributions, where the size distribution can be altered by subtle changes in the production process. These three techniques detect subtle size differences in VLPs derived from the non-enveloped murine polyomavirus (MPV) following: (i) functionalization of the surface of VLPs with an influenza viral peptide fragment; (ii) packaging of foreign protein internally within the VLPs; and (iii) packaging of genomic DNA internally within the VLPs. These results demonstrate that ES-DMA and AFFFF-MALS are able to quantitatively determine VLP size distributions with greater rapidity and statistical significance than TEM, providing useful technologies for product development and process analytics.

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“…A recent low-angle neutron scattering study suggested that the dimensions of the MS2 capsid proteins are different in the presence or absence of maturation protein, the form lacking maturation protein being considerably thicker (31-37 Å versus 21-25 Å) than in wild-type particles. 31 This difference was ascribed to the formation of a postinfection state within the capsid lattice when both RNA and maturation protein have left the protein shell. This state was not revealed by previous X-ray structures, even those of recombinant shells lacking maturation protein, it was argued because crystallization favours the "thin" pre-infection state.…”

Section: Implications For Phage Infectionmentioning

confidence: 99%

The Three-dimensional Structure of Genomic RNA in Bacteriophage MS2: Implications for Assembly

Toropova

Basnak

Twarock

et al. 2008

Journal of Molecular Biology

105

161

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The MS2 Coat Protein Shell is Likely Assembled Under Tension: A Novel Role for the MS2 Bacteriophage A Protein as Revealed by Small-angle Neutron Scattering

Cited by 29 publications

References 81 publications

Virus Inactivation Mechanisms: Impact of Disinfectants on Virus Function and Structural Integrity

Virus Inactivation Mechanisms: Impact of Disinfectants on Virus Function and Structural Integrity

Quantitative characterization of virus‐like particles by asymmetrical flow field flow fractionation, electrospray differential mobility analysis, and transmission electron microscopy

The Three-dimensional Structure of Genomic RNA in Bacteriophage MS2: Implications for Assembly

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