Virus Inactivation by Anilinonaphthalene Sulfonate Compounds and Comparison with Other Ligands

Bonafé, Carlos Francisco Sampaio; Gläser, Michael; Voss, Edward W.; Weber, Gregorio; Silva, Jerson L.

doi:10.1006/bbrc.2000.3402

Cited by 14 publications

(11 citation statements)

References 38 publications

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“…NAS probes bind to AS fibrils with apparent dissociation constants in the micromolar range. It has been shown that bis-ANS can interfere with protein-protein interactions, including those in thermally or chemically induced aggregation processes (56), as well as in the assembly of microtubules in vitro (57), bacteriophage P22 capsids (58), vesicular stomatitis virus (59), and amyloid formation of the prion protein (38,39). However, to abolish protein association, a high dye/ protein molar ratio is required.…”

Section: Structural Interpretationsmentioning

confidence: 99%

Fluorescent N-Arylaminonaphthalene Sulfonate Probes for Amyloid Aggregation of α-Synuclein

Celej

Jares‐Erijman

Jovin

2008

Biophysical Journal

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The deposition of fibrillar structures (amyloids) is characteristic of pathological conditions including Alzheimer's and Parkinson's diseases. The detection of protein deposits and the evaluation of their kinetics of aggregation are generally based on fluorescent probes such as thioflavin T and Congo red. In a search for improved fluorescence tools for studying amyloid formation, we explored the ability of N-arylaminonaphthalene sulfonate (NAS) derivatives to act as noncovalent probes of alpha-synuclein (AS) fibrillation, a process linked to Parkinson's disease and other neurodegenerative disorders. The compounds bound to fibrillar AS with micromolar K(d)s, and exhibited fluorescence enhancement, hyperchromism, and high anisotropy. We conclude that the probes experience a hydrophobic environment and/or restricted motion in a polar region. Time- and spectrally resolved emission intensity and anisotropy provided further information regarding structural features of the protein and the dynamics of solvent relaxation. The steady-state and time-resolved parameters changed during the course of aggregation. Compared with thioflavin T, NAS derivatives constitute more sensitive and versatile probes for AS aggregation, and in the case of bis-NAS detect oligomeric as well as fibrillar species. They can function in convenient, continuous assays, thereby providing useful tools for studying the mechanisms of amyloid formation and for high-throughput screening of factors inhibiting and/or reversing protein aggregation in neurodegenerative diseases.

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Section: Structural Interpretationsmentioning

confidence: 99%

Fluorescent N-Arylaminonaphthalene Sulfonate Probes for Amyloid Aggregation of α-Synuclein

Celej

Jares‐Erijman

Jovin

2008

Biophysical Journal

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“…When whole virus was incubated with bis-ANS, an increase in fluorescence occurred especially because of binding to the membrane and to the membrane viral glycoproteins (49,(51)(52)(53). The treatment of intact particles with pressure generated a different pattern from that found for NC particles.…”

Section: Fig 2 Urea-induced Disassembly Of Mayaro Virus and Virus Ncmentioning

confidence: 96%

The Metastable State of Nucleocapsids of Enveloped Viruses as Probed by High Hydrostatic Pressure

Gaspar¹,

Terezan²,

Pinheiro³

et al. 2001

Journal of Biological Chemistry

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Enveloped viruses fuse their membranes with cellular membranes to transfer their genomes into cells at the beginning of infection. What is not clear, however, is the role of the envelope (lipid bilayer and glycoproteins) in the stability of the viral particle. To address this question, we compared the stability between enveloped and nucleocapsid particles of the alphavirus Mayaro using hydrostatic pressure and urea. The effects were monitored by intrinsic fluorescence, light scattering, and binding of fluorescent dyes, including bis(8-anilinonaphthalene-1-sulfonate) and ethidium bromide. Pressure caused a drastic dissociation of the nucleocapsids as determined by tryptophan fluorescence, light scattering, and gel filtration chromatography. Pressure-induced dissociation of the nucleocapsids was poorly reversible. In contrast, when the envelope was present, pressure effects were much less marked and were highly reversible. Binding of ethidium bromide occurred when nucleocapsids were dissociated under pressure, indicating exposure of the nucleic acid, whereas enveloped particles underwent no changes. Overall, our results demonstrate that removal of the envelope with the glycoproteins leads the particle to a metastable state and, during infection, may serve as the trigger for disassembly and delivery of the genome. The envelope acts as a "Trojan horse," gaining entry into the host cell to allow release of a metastable nucleocapsid prone to disassembly.

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“…Our understanding of these processes has gradually expanded through the careful control of variables such as temperature, pH, ionic strength, and pressure. In particular, the use of high-pressure incubations (up to 300 MPa) has provided important information about the mechanisms of aggregation since pressure produces no significant alterations in the tertiary structure of proteins. − The latter characteristic is important when using high pressure to develop experimental vaccines because viral inactivation without significant structural changes in the viral capsid helps to maintain immunogenic properties. − Virus inactivation by pressure has also been studied as a means of sterilization, ,, and pressure has been used to investigate the thermodynamics of virus dissociation. ,,− Enveloped viruses, which have a lipid membrane in their structure, are also targets of pressure-induced inactivation. , The combined effect of high pressure and other factors, such as subzero temperatures, different conditions of pH, and the presence of subdenaturant concentrations of urea, has provided insights into the protein–protein interactions that drive aggregation, with the advantage that such methods avoid the need to use extreme temperatures to promote protein dissociation . This approach has been used to study urea-mediated denaturation in well-defined conditions. , …”

Section: Introductionmentioning

confidence: 99%

“…5,7,10−13 Enveloped viruses, which have a lipid membrane in their structure, are also targets of pressure-induced inactivation. 14,15 The combined effect of high pressure and other factors, such as subzero temperatures, different conditions of pH, and the presence of subdenaturant concentrations of urea, has provided insights into the protein−protein interactions that drive aggregation, with the advantage that such methods avoid the need to use extreme temperatures to promote protein dissociation. 2 This approach has been used to study ureamediated denaturation in well-defined conditions.…”

Section: ■ Introductionmentioning

confidence: 99%

Entropy and Volume Change of Dissociation in Tobacco Mosaic Virus Probed by High Pressure

et al. 2012

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Virus dissociation and inactivation by high pressure have been extensively studied in recent decades. Pressure-induced dissociation of viral particles involves a reduction in the Gibbs free energy of dissociation and a negative change in volume. In this work, we investigated the combined effect of high pressure and temperature on the dissociation of tobacco mosaic virus (TMV). We assumed the presence of two states of TMV with different tendencies to dissociate. Thus one form presents a low tendency (L) and the other a high tendency (H) to dissociate. Based on the model described here, the L-H transition was favored by an increase in pressure and a decrease in temperature. The volume change of dissociation was pressure- and temperature-dependent, with a highly negative value of -80 mL/mol being recorded at 0 °C and atmospheric pressure. The entropy and enthalpy of dissociation were very temperature- and pressure-dependent, with values of entropy of 450 to -1300 kJ/mol and values of enthalpy of 5.5 × 10(4) to 2.4 × 10(4) kJ/mol. The dissociation of TMV was enthalpy-driven at all temperatures and pressures investigated. Based on these findings, we conclude that the model presented allows accurate predictions of viral dissociation behavior in different experimental conditions.

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Virus Inactivation by Anilinonaphthalene Sulfonate Compounds and Comparison with Other Ligands

Cited by 14 publications

References 38 publications

Fluorescent N-Arylaminonaphthalene Sulfonate Probes for Amyloid Aggregation of α-Synuclein

Fluorescent N-Arylaminonaphthalene Sulfonate Probes for Amyloid Aggregation of α-Synuclein

The Metastable State of Nucleocapsids of Enveloped Viruses as Probed by High Hydrostatic Pressure

Entropy and Volume Change of Dissociation in Tobacco Mosaic Virus Probed by High Pressure

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