A comparative differential scanning calorimetric study of tobacco mosaic virus and of its coat protein ts mutant

Орлов, В. Н.; Kust, S. V.; Kalmykov, P V; Krivosheev, V.P.; Добров, Е. Н.; Drachev, V. A.

doi:10.1016/s0014-5793(98)00924-7

Cited by 20 publications

(14 citation statements)

References 28 publications

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“…Regrettably, we cannot be certain that it is not a measurement artifact. On the other hand, the T m for isolated TMV CP is as low as 40°C [17], and that for isolated PVX CP is 35°C [16]. Hence, free PVA CP can indeed lack any meltable structures, and thus, support our suggestion that isolated PVA CP in 10 mM phosphate buffer has a significant fraction of disordered structures.…”

Section: Resultssupporting

confidence: 81%

“…To our knowledge, it is the first published DSC melting profile for any of potyviruses . Such curves were reported for rod-like TMV and flexuous PVX [16], [17], and we also present them in Fig. 6.…”

Section: Resultssupporting

confidence: 78%

“…TMV had the highest temperature stability (T m = 80.5°C), while PVA was the least stable (T m = 55°C). In contrast to other HPV, the DSC melting curve for intact PVA had the width typical for proteins (W hight/2 = 2.7°), while those for intact TMV and potato virus X featured abnormally large widths (W hight/2 = 5–7°), which can be due to some kind of virion heterogeneity [17].…”

Section: Resultsmentioning

confidence: 72%

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Partially Disordered Structure in Intravirus Coat Protein of Potyvirus Potato Virus A

et al. 2013

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Potyviruses represent the most biologically successful group of plant viruses, but to our knowledge, this work is the first detailed study of physicochemical characteristics of potyvirus virions. We measured the UV absorption, far and near UV circular dichroism spectra, intrinsic fluorescence spectra, and differential scanning calorimetry (DSC) melting curves of intact particles of a potato virus A (PVA). PVA virions proved to have a peculiar combination of physicochemical properties. The intravirus coat protein (CP) subunits were shown to contain an unusually high fraction of disordered structures, whereas PVA virions had an almost normal thermal stability. Upon heating from 20°C to 55°C, the fraction of disordered structures in the intravirus CP further increased, while PVA virions remained intact at up to 55°C, after which their disruption (and DSC melting) started. We suggest that the structure of PVA virions below 55°C is stabilized by interactions between the remaining structured segments of intravirus CP. It is not improbable that the biological efficiency of PVA relies on the disordered structure of intravirus CP.

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Section: Resultssupporting

confidence: 81%

Section: Resultssupporting

confidence: 78%

Section: Resultsmentioning

confidence: 72%

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Partially Disordered Structure in Intravirus Coat Protein of Potyvirus Potato Virus A

et al. 2013

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“…The structure of BSMV virions was further analyzed by their heat denaturation using differential scanning calorimetry (DSC) [30]. The DSC curves obtained for the BSMV virions had single thermal peaks with melting temperatures of 61°C and ΔH of 700 kJ/mole (Fig.…”

Section: Resultsmentioning

confidence: 99%

Structural Lability of Barley Stripe Mosaic Virus Virions

et al. 2013

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Virions of Barley stripe mosaic virus (BSMV) were neglected for more than thirty years after their basic properties were determined. In this paper, the physicochemical characteristics of BSMV virions and virion-derived viral capsid protein (CP) were analyzed, namely, the absorption and intrinsic fluorescence spectra, circular dichroism spectra, differential scanning calorimetry curves, and size distributions by dynamic laser light scattering. The structural properties of BSMV virions proved to be intermediate between those of Tobacco mosaic virus (TMV), a well-characterized virus with rigid rod-shaped virions, and flexuous filamentous plant viruses. The BSMV virions were found to be considerably more labile than expected from their rod-like morphology and a distant sequence relation of the BSMV and TMV CPs. The circular dichroism spectra of BSMV CP subunits incorporated into the virions, but not subunits of free CP, demonstrated a significant proportion of beta-structure elements, which were proposed to be localized mostly in the protein regions exposed on the virion outer surface. These beta-structure elements likely formed during virion assembly can comprise the N- and C-terminal protein regions unstructured in the non-virion CP and can mediate inter-subunit interactions. Based on computer-assisted structure modeling, a model for BSMV CP subunit structural fold compliant with the available experimental data was proposed.

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“…The TMV CP molecular weight was taken to be 17.5 kDa. The data processing method was the same as in our previous works 18, 33…”

Section: Experimental Partmentioning

confidence: 99%

Surfactant‐Induced Amorphous Aggregation of Tobacco Mosaic Virus Coat Protein: A Physical Methods Approach

Panyukov

Nemykh

Добров

et al. 2008

Macromolecular Bioscience

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The interactions of non-ionic surfactant Triton X-100 and the coat protein of tobacco mosaic virus, which is an established model for both ordered and non-ordered protein aggregation, were studied using turbidimetry, differential scanning calorimetry, isothermal titration calorimetry, and dynamic light scattering. It was found that at the critical aggregation concentration (equal to critical micelle concentration) of 138 x 10(-6) M, Triton X-100 induces partial denaturation of tobacco mosaic virus coat protein molecules followed by protein amorphous aggregation. Protein aggregation has profound ionic strength dependence and proceeds due to hydrophobic sticking of surfactant-protein complexes (start aggregates) with initial radii of 46 nm. It has been suggested that the anionic surfactant sodium dodecyl sulfate forms mixed micelles with Triton X-100 and therefore reverses protein amorphous aggregation with release of protein molecules from the amorphous aggregates. A stoichiometric ratio of 5 was found for Triton X-100-sodium dodecyl sulfate interactions.

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A comparative differential scanning calorimetric study of tobacco mosaic virus and of its coat protein ts mutant

Cited by 20 publications

References 28 publications

Partially Disordered Structure in Intravirus Coat Protein of Potyvirus Potato Virus A

Partially Disordered Structure in Intravirus Coat Protein of Potyvirus Potato Virus A

Structural Lability of Barley Stripe Mosaic Virus Virions

Surfactant‐Induced Amorphous Aggregation of Tobacco Mosaic Virus Coat Protein: A Physical Methods Approach

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