Reversible Pressure Dissociation of R17 Bacteriophage

Poian, Andrea T. Da; Oliveira, Andréa C.; Gaspar, Luciane P.; Silva, Jerson L.; Weber, Gregorio

doi:10.1006/jmbi.1993.1347

Cited by 50 publications

(30 citation statements)

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“…Together with similar results on the effects of urea on R17 phage (23,40), and the observation that increased osmolarity prevents rather than promotes viral inactivation, the present findings indicate that the concurrent use of pressurization and molar concentrations of urea may be useful as a general procedure for viral inactivation. The fluorescence studies indicated that as the urea concentration increased, the disrupting effect of pressure occurred at progressively lower values.…”

Section: Discussionsupporting

confidence: 76%

Virus Inactivation by Anilinonaphthalene Sulfonate Compounds and Comparison with Other Ligands

Bonafé

Gläser

Voss

et al. 2000

Biochemical and Biophysical Research Communications

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Section: Discussionsupporting

confidence: 76%

Virus Inactivation by Anilinonaphthalene Sulfonate Compounds and Comparison with Other Ligands

Bonafé

Gläser

Voss

et al. 2000

Biochemical and Biophysical Research Communications

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“…However, investigation of the reversible subunit dissociation of several oligomers by hydrostatic pressure has revealed significant deviations from the law of mass action [8,23–25]. This anomalous behavior ranges from the reduced dependence on protein concentration for subunit association/dissociation in trimers and tetramers [9,25] to a complete lack of protein concentration dependence for the association of large protein aggregates such as viral particles [26,27]. This behavior has been investigated in detail in the case of dimeric triosephosphate isomerase (TIM) [8,10].…”

Section: Persistent Conformational Heterogeneity and Deterministic Bementioning

confidence: 99%

“…For example, for virus particles a clear need for a distribution of conformations that can be regarded as ‘frozen’ in time was pointed out by Weber and co‐workers [26,27]. A typical virus shell consists of the non‐covalent assembly of dozens of copies of one or a few types of coat proteins.…”

Section: Persistent Conformational Heterogeneity and Deterministic Bementioning

confidence: 99%

Protein dynamics, folding and misfolding: from basic physical chemistry to human conformational diseases

Ferreira

Felice

2001

FEBS Letters

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Proteins exhibit a variety of motions ranging from amino acid side-chain rotations to the motions of large domains. Recognition of their conformational flexibility has led to the view that protein molecules undergo fast dynamic interconversion between different conformational substates. This proposal has received support from a wide variety of experimental techniques and from computer simulations of protein dynamics. More recently, studies of the subunit dissociation of oligomeric proteins induced by hydrostatic pressure have shown that the characteristic times for subunit exchange between oligomers and for interconversion between different conformations may be rather slow (hours or days). In such cases, proteins cannot be treated as an ensemble of rapidly interconverting conformational substates, but rather as a persistently heterogeneous population of different long-lived conformers. This is reminiscent of the deterministic behavior exhibited by macroscopic bodies, and may have important implications for our understanding of protein folding and biological functions. Here, we propose that the deterministic behavior of proteins may be closely related to the genesis of conformational diseases, a class of pathological conditions that includes transmissible spongiform encephalopathies, Alzheimer's disease and other amyloidosis. ß 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

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“…Virus samples within a 100-fold range of dilutions incubated for 1 hr at 200 MPa followed the same inactivation profile (data not shown). This result indicates that with respect to pressure the viral population behaves as individual units that undergo independent inactivation (18). The inactivation is unlikely to be directly related to the dissociation into subunits, as observed in icosahedral viruses (brome mosaic, cowpea) but rather to effects produced in the nucleoproteins under the compressible lipid membrane, as observed in vesicular stomatitis virus (5).…”

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confidence: 98%

Inactivation of simian immunodeficiency virus by hydrostatic pressure.

Jurkiewicz

Villas-Boas

Silva

et al. 1995

Proc. Natl. Acad. Sci. U.S.A.

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The inactivation of the simian immunodeficiency viruses SIVmac251 and SIVagm by pressures of 150 and 250 MPa was determined. The extent of inactivation depended on the time that the virus was subjected to compression as well as the level of the pressure and at 150 Mpa reached 5 log1l dilution units after '10 hr. The inactivations, which were uniformly carried out at room temperature, were independent of the concentration of the virus. Possible applications of pressure inactivation for molecular biological and clinical use are discussed.The development of effective methods for eliminating unwanted or harmful components, such as viruses, present in biological samples and preparations is an important scientific endeavor with many possible practical applications. Sterilizing biological preparations and introducing new vaccines are obvious motives; moreover, all procedures that modify the biological activity of viruses can lead to a better understanding of their requirements for successful infectivity. Key considerations in practical, large-scale applications are the simplicity and reproducibility of the procedures. Physical methods are not always highly selective but they are simple, easy to reproduce, universally applicable, and relatively easy to apply on a large scale. High pressure can be applied to almost all biological preparations, is readily implemented routinely and safely in a laboratory environment, and is often selective in its action on macromolecular structures. In this report we present results showing that subjecting virus samples to pressures under 250 MPa (1 MPa = 10 atmospheres) can inactivate the simian immunodeficiency viruses SIVmac251 and SIVagm. Pressure often perturbs selectively the properties of biological molecules and complex biological systems by disrupting noncovalent associations, while leaving unaffected the covalent architecture of the separate components (1-3). This is of particular interest in prospective viral vaccines because the precise relations of the capsid proteins with each other, with the lipid membrane when there is one, and with the nucleic acids must be responsible for the specific infectivity, whereas an intact covalent framework of the proteins is necessary for the proper immune response. Hydrostatic pressures under 300 MPa can disrupt icosahedral viruses (4) and a membrane-enveloped animal virus, causing loss of infectivity with retention of the immunogenic capacity (5, 6). Therefore hydrostatic pressure procedures may by themselves, or in conjunction with other physical, chemical, or biochemical techniques, offer a suitable procedure for the preparation of vaccines. MATERIALS AND METHODSSIVmac251 was isolated from a rhesus monkey (Macaca mulatta) (7) and SIVagm Tyo 7 was isolated from an African green monkey (Cercopithecus aethiops) (8). The simian immunodeficiency viruses were grown in the CEM human T-cell line. The medium for cell growth and for virus inactivation was RPMI 1640 supplemented with 20% fetal bovine serum. The high-pressure inactivation of th...

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Reversible Pressure Dissociation of R17 Bacteriophage

Cited by 50 publications

References 0 publications

Virus Inactivation by Anilinonaphthalene Sulfonate Compounds and Comparison with Other Ligands

Virus Inactivation by Anilinonaphthalene Sulfonate Compounds and Comparison with Other Ligands

Protein dynamics, folding and misfolding: from basic physical chemistry to human conformational diseases

Inactivation of simian immunodeficiency virus by hydrostatic pressure.

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