Mechanism of self-assembly of tobacco mosaic virus protein

Schuster, Todd M.; Scheele, Robert B.; Khairallah, L. H.

doi:10.1016/0022-2836(79)90232-8

Cited by 42 publications

(31 citation statements)

References 51 publications

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“…At neutral pH and moderate ionic :~ strength, TMV protein sediments at 20 S, forming a short helix made of about 39 subunits, with a pitch and a diameter very similar to those of the virus (Correia et al 1985). At higher pH much smaller aggregates are present, sedimenting at 4 S. The 4 S--* 20 S transition can be induced by increasing the temperature from 4 °C to 25 °C under suitable pH and salt conditions (Durham et al 1971;Schuster et al 1979).…”

Section: Thermal Denaturation Of the Common Strain Virus: Tmv-smentioning

confidence: 99%

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Scanning calorimetric studies of the stability of tobacco mosaic virus and aggregates of its coat protein

et al. 1992

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The thermal denaturation of the common strain of a rod-shaped plant virus, tobacco mosaic virus, has been investigated by differential scanning calorimetry, and compared to that of various aggregation states of its coat protein and to that of three other TMV strains. The state of the virions was monitored by electron microscopy and analytical ultracentrifugation. The observed endotherms could be analysed in terms of a step-wise dissociation of the virions. The transition temperatures of the three successive structural changes increased with decreasing pH, from pH = 8.0 to pH = 5.0, although the corresponding enthalpy changes did not vary appreciably with pH. TMV-HR showed a stronger pH dependence of the transition temperatures than the other strains, probably reflecting the importance of the changes in affecting the charged amino acids of its coat protein. The first step of the dissociation, which correlates with the breaking up of the virions into three or four shorter rods, implies a conformational change of the particle that may be related to the first step of the in situ decapsidation of TMV.

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Section: Thermal Denaturation Of the Common Strain Virus: Tmv-smentioning

confidence: 99%

“…2; scanning rate: 1 °C/ rain. The 20S sample, first dialyzed in the cold against the pH 6.52 buffer, was allowed to heat slowly to 25°C (Schuster et al 1979). Denaturated protein was removed by low speed centrifugation before microcalorimetry ).…”

Section: Thermal Denaturation Of the Common Strain Virus: Tmv-smentioning

confidence: 99%

Scanning calorimetric studies of the stability of tobacco mosaic virus and aggregates of its coat protein

et al. 1992

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“…1c). [10][11][12][13][14] Specifically, the initial oligomerization of protein monomers is slow and energetically disfavored (nucleation) relative to the subsequent rapid chain propagation into long filaments (elongation). Due to the unique disposition of repeating units within the helix or tubular structure, each protein molecule is simultaneously in contact with multiple neighboring units.…”

Section: Introductionmentioning

confidence: 99%

Nucleation–elongation: a mechanism for cooperative supramolecular polymerization

2003

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The kinetic and thermodynamic characteristics of polymerizations following a cooperative, nucleation-elongation mechanism are discussed in comparison to those of non-cooperative, isodesmic polymerizations. Nucleation-elongation polymerization is a relatively unexplored avenue of synthetic polymer chemistry and offers some unique and interesting thermodynamic and kinetic attributes not found in the more classical mechanisms of polymer chemistry.

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“…The purified proteins were incubated in 10 mM sodium phosphate and 100 mM sodium chloride solution (pH 7.2) at 295 K for 24 h to obtain the four-layer aggregate disk [ 16 , 17 , 18 , 19 , 20 ]. The disk forms were confirmed by SEC and native-PAGE.…”

Section: Methodsmentioning

confidence: 99%

New Strategies and Methods to Study Interactions between Tobacco Mosaic Virus Coat Protein and Its Inhibitors

Chen

Jin

et al. 2016

IJMS

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Studies of the targets of anti-viral compounds are hot topics in the field of pesticide research. Various efficient anti-TMV (Tobacco Mosaic Virus) compounds, such as Ningnanmycin (NNM), Antofine (ATF), Dufulin (DFL) and Bingqingxiao (BQX) are available. However, the mechanisms of the action of these compounds on targets remain unclear. To further study the mechanism of the action of the anti-TMV inhibitors, the TMV coat protein (TMV CP) was expressed and self-assembled into four-layer aggregate disks in vitro, which could be reassembled into infectious virus particles with TMV RNA. The interactions between the anti-TMV compounds and the TMV CP disk were analyzed by size exclusion chromatography, isothermal titration calorimetry and native-polyacrylamide gel electrophoresis methods. The results revealed that assembly of the four-layer aggregate disk was inhibited by NNM; it changed the four-layer aggregate disk into trimers, and affected the regular assembly of TMV CP and TMV RNA. The four-layer aggregate disk of TMV CP was little inhibited by ATF, DFL and BQX. Our results provide original data, as well as new strategies and methods, for research on the mechanism of action of anti-viral drugs.

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Mechanism of self-assembly of tobacco mosaic virus protein

Cited by 42 publications

References 51 publications

Scanning calorimetric studies of the stability of tobacco mosaic virus and aggregates of its coat protein

Scanning calorimetric studies of the stability of tobacco mosaic virus and aggregates of its coat protein

Nucleation–elongation: a mechanism for cooperative supramolecular polymerization

New Strategies and Methods to Study Interactions between Tobacco Mosaic Virus Coat Protein and Its Inhibitors

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