scholarly journals Effect of NaCl on the Stability of Oncolytic Vaccinia Virus

2016 ◽  
Vol 26 (1) ◽  
pp. 23-33 ◽  
Author(s):  
Seong-Geun Kim ◽  
Gui Shao Ran ◽  
Hyuk-Chan Kwon ◽  
Tae-Ho Hwang
Keyword(s):  
Vaccinia Virus ◽  
The Stability

scholarly journals Genetic and Cell Biological Characterization of the Vaccinia Virus A30 and G7 Phosphoproteins

2005 ◽  
Vol 79 (11) ◽  
pp. 7146-7161 ◽  
Author(s):  
Jason Mercer ◽  
Paula Traktman
Keyword(s):  
Vaccinia Virus ◽  
Temperature Sensitive ◽  
Phenotypic Analysis ◽  
Virion Morphogenesis ◽  
Release Assay ◽  
The Stability ◽  
Temperature Sensitive Phenotype

ABSTRACT The vaccinia virus proteins A30 and G7 are known to play essential roles in early morphogenesis, acting prior to the formation of immature virions. Their repression or inactivation results in the accumulation of large virosomes, detached membrane crescents, and empty immature virions. We have undertaken further study of these proteins to place them within the context of the F10 kinase, the A14 membrane protein, and the H5 phosphoprotein, which have been the focus of previous studies within our laboratory. Here we confirm that both A30 and G7 undergo F10 kinase-dependent phosphorylation in vivo and recapitulate that modification of A30 in vitro. Although the detached crescents observed upon loss of A30 or G7 echo those seen upon repression of A14, no interaction between A30/G7 and A14 could be detected. We did, however, determine that the A30 and G7 proteins are unstable during nonpermissive tsH5 infections, suggesting that the loss of A30/G7 is the underlying cause for the formation of lacy or curdled virosomes. We also determined that the temperature-sensitive phenotype of the Cts11 virus is due to mutations in two codons of the G7L gene. Phenotypic analysis of nonpermissive Cts11 infections indicated that these amino acid substitutions compromise G7 function without impairing the stability of either G7 or A30. Utilizing Cts11 in conjunction with a rifampin release assay, we determined that G7 acts at multiple stages of virion morphogenesis that can be distinguished both by ultrastructural analysis and by monitoring the phosphorylation status of several viral proteins that undergo F10-mediated phosphorylation.

scholarly journals Effects of a Temperature Sensitivity Mutation in the J1R Protein Component of a Complex Required for Vaccinia Virus Assembly

2005 ◽  
Vol 79 (13) ◽  
pp. 8046-8056 ◽  
Author(s):  
Wen-Ling Chiu ◽  
Patricia Szajner ◽  
Bernard Moss ◽  
Wen Chang
Keyword(s):  
Vaccinia Virus ◽  
Virus Assembly ◽  
Terminal Region ◽  
Temperature Sensitive ◽  
Loss Of Function ◽  
Wild Type ◽  
Reading Frame ◽  
Infected Cells ◽  
The Stability ◽  
Virus C

ABSTRACT Vaccinia virus J1R protein is required for virion morphogenesis (W. L. Chiu and W. Chang, J. Virol. 76:9575-9587, 2002). In this work, we further characterized the J1R protein of wild-type vaccinia virus and compared it with the protein encoded by the temperature-sensitive mutant virus Cts45. The mutant Cts45 was found to contain a Pro-to-Ser substitution at residue 132 of the J1R open reading frame, which is responsible for a loss-of-function phenotype. The half-life of the J1R-P132S mutant protein was comparable at both 31 and 39°C, indicating that the P132S mutation did not affect the stability of the J1R protein. We also showed that the J1R protein interacts with itself in the virus-infected cells. The N-terminal region of the J1R protein, amino acids (aa) 1 to 77, interacted with the C-terminal region, aa 84 to 153, and the P132 mutation did not abolish this interaction, as determined by two-hybrid analysis. Furthermore, we demonstrated that J1R protein is part of a viral complex containing the A30L, G7L, and F10L proteins in virus-infected cells. In immunofluorescence analyses, wild-type J1R protein colocalized with the A30L, G7L, and F10L proteins in virus-infected cells but the loss-of-function P132 mutant did not. Furthermore, without a functional J1R protein, rapid degradation of A30L and the 15-kDa forms of the G7L and F10L proteins was observed in cells infected with Cts45 at 39°C. This study thus demonstrated the importance of the J1R protein in the formation of a viral assembly complex required for morphogenesis.

scholarly journals THE STABILITY OF VARIOLA VIRUS PROPAGATED IN EMBRYONATED EGGS

1943 ◽  
Vol 78 (4) ◽  
pp. 231-239 ◽  
Author(s):  
John B. Nelson
Keyword(s):  
Vaccinia Virus ◽  
Significant Alteration ◽  
Variola Virus ◽  
Species Identity ◽  
Apparent Change ◽  
The Stability

After 24 transfers in embryonated eggs a strain of variola virus (Chinese) was established in the testis of the rabbit and maintained for 11 passages at intervals of 7 days. Residence in the rabbit testis was not accompanied by any significant alteration in the species identity of the virus. A second strain of variola virus (Minnesota) was transferred 180 times in embryonated eggs with no apparent change in its behavior. Subsequent attempts, however, to maintain this strain in the rabbit by serial testicular passage were unsuccessful. These observations are discussed in relation to the so called transformation of variola to vaccinia virus by animal passage.

scholarly journals Vaccinia Virus G7L Protein Interacts with the A30L Protein and Is Required for Association of Viral Membranes with Dense Viroplasm To Form Immature Virions

2003 ◽  
Vol 77 (6) ◽  
pp. 3418-3429 ◽  
Author(s):  
Patricia Szajner ◽  
Howard Jaffe ◽  
Andrea S. Weisberg ◽  
Bernard Moss
Keyword(s):  
Vaccinia Virus ◽  
Protein A ◽  
Direct Interaction ◽  
Uncharacterized Protein ◽  
Lethal Mutant ◽  
C Terminus ◽  
Infected Cells ◽  
The Stability

ABSTRACT The vaccinia virus A30L protein is required for the association of electron-dense, granular, proteinaceous material with the concave surfaces of crescent membranes, an early step in viral morphogenesis. For the identification of additional proteins involved in this process, we used an antibody to the A30L protein, or to an epitope appended to its C terminus, to capture complexes from infected cells. A prominent 42-kDa protein was resolved and identified by mass spectrometry as the vaccinia virus G7L protein. This previously uncharacterized protein was expressed late in infection and was associated with immature virions and the cores of mature particles. In order to study the role of the G7L protein, a conditional lethal mutant was made by replacing the G7L gene with an inducible copy. Expression of G7L and formation of infectious virus was dependent on the addition of inducer. Under nonpermissive conditions, morphogenesis was blocked and viral crescent membranes and immature virions containing tubular elements were separated from the electron-dense granular viroplasm, which accumulated in large spherical masses. This phenotype was identical to that previously obtained with an inducible, conditional lethal A30L mutant. Additional in vivo and in vitro experiments provided evidence for the direct interaction of the A30L and G7L proteins and demonstrated that the stability of each one was dependent on its association with the other.

Open discussion

1982 ◽  
Vol 99 ◽  
pp. 605-613
Author(s):  
P. S. Conti
Keyword(s):  
Buenos Aires ◽  
Large Mass ◽  
List Type ◽  
Common Phenomenon ◽  
Open Discussion ◽  
The Stability ◽  
Ring Nebulae

Conti: One of the main conclusions of the Wolf-Rayet symposium in Buenos Aires was that Wolf-Rayet stars are evolutionary products of massive objects. Some questions:–Do hot helium-rich stars, that are not Wolf-Rayet stars, exist?–What about the stability of helium rich stars of large mass? We know a helium rich star of ∼40 MO. Has the stability something to do with the wind?–Ring nebulae and bubbles : this seems to be a much more common phenomenon than we thought of some years age.–What is the origin of the subtypes? This is important to find a possible matching of scenarios to subtypes.

Symmetric Multistep Methods Revisited: II. Numerical Experiments

1999 ◽  
Vol 173 ◽  
pp. 309-314 ◽  
Author(s):  
T. Fukushima
Keyword(s):  
Multistep Methods ◽  
Computational Time ◽  
Integration Time ◽  
Implicit Methods ◽  
Symmetric Methods ◽  
Celestial Bodies ◽  
The Stability ◽  
Predictor Corrector ◽  
Symmetric Multistep Methods ◽  
Integration Errors

AbstractBy using the stability condition and general formulas developed by Fukushima (1998 = Paper I) we discovered that, just as in the case of the explicit symmetric multistep methods (Quinlan and Tremaine, 1990), when integrating orbital motions of celestial bodies, the implicit symmetric multistep methods used in the predictor-corrector manner lead to integration errors in position which grow linearly with the integration time if the stepsizes adopted are sufficiently small and if the number of corrections is sufficiently large, say two or three. We confirmed also that the symmetric methods (explicit or implicit) would produce the stepsize-dependent instabilities/resonances, which was discovered by A. Toomre in 1991 and confirmed by G.D. Quinlan for some high order explicit methods. Although the implicit methods require twice or more computational time for the same stepsize than the explicit symmetric ones do, they seem to be preferable since they reduce these undesirable features significantly.

Uniformity of Magnification from Different Electron Microscopes

1967 ◽  
Vol 25 ◽  
pp. 32-33
Author(s):  
Godfrey C. Hoskins ◽  
V. Williams ◽  
V. Allison
Keyword(s):  
Diffraction Grating ◽  
The Other ◽  
Carbon Replica ◽  
Electron Microscopes ◽  
The Stability

The method demonstrated is an adaptation of a proven procedure for accurately determining the magnification of light photomicrographs. Because of the stability of modern electrical lenses, the method is shown to be directly applicable for providing precise reproducibility of magnification in various models of electron microscopes.A readily recognizable area of a carbon replica of a crossed-line diffraction grating is used as a standard. The same area of the standard was photographed in Phillips EM 200, Hitachi HU-11B2, and RCA EMU 3F electron microscopes at taps representative of the range of magnification of each. Negatives from one microscope were selected as guides and printed at convenient magnifications; then negatives from each of the other microscopes were projected to register with these prints. By deferring measurement to the print rather than comparing negatives, correspondence of magnification of the specimen in the three microscopes could be brought to within 2%.

Effect of Improved ThO2 Particle Dispersion in Nickel on High-Temperature Strength

1970 ◽  
Vol 28 ◽  
pp. 444-445
Author(s):  
E. R. Kimmel ◽  
H. L. Anthony ◽  
W. Scheithauer
Keyword(s):  
High Temperature ◽  
Metal Matrix ◽  
Oxide Particle ◽  
Oxide Phase ◽  
Dislocation Motion ◽  
Particle Dispersion ◽  
High Temperature Strength ◽  
Strengthening Effect ◽  
Oxide Particles ◽  
The Stability

The strengthening effect at high temperature produced by a dispersed oxide phase in a metal matrix is seemingly dependent on at least two major contributors: oxide particle size and spatial distribution, and stability of the worked microstructure. These two are strongly interrelated. The stability of the microstructure is produced by polygonization of the worked structure forming low angle cell boundaries which become anchored by the dispersed oxide particles. The effect of the particles on strength is therefore twofold, in that they stabilize the worked microstructure and also hinder dislocation motion during loading.

An Analysis of Dissociation of Molecules in a High Resolution Electron Microscope

1973 ◽  
Vol 31 ◽  
pp. 486-487
Author(s):  
Mihir Parikh
Keyword(s):  
Electron Microscope ◽  
High Resolution ◽  
Cross Sections ◽  
Resolving Power ◽  
Peak Intensity ◽  
Molecular Film ◽  
Resolution Electron ◽  
Dissociation Cross Section ◽  
High Resolution Electron Microscope ◽  
The Stability

It is well known that the resolution of bio-molecules in a high resolution electron microscope depends not just on the physical resolving power of the instrument, but also on the stability of these molecules under the electron beam. Experimentally, the damage to the bio-molecules is commo ly monitored by the decrease in the intensity of the diffraction pattern, or more quantitatively by the decrease in the peaks of an energy loss spectrum. In the latter case the exposure, EC, to decrease the peak intensity from IO to I’O can be related to the molecular dissociation cross-section, σD, by EC = ℓn(IO /I’O) /ℓD. Qu ntitative data on damage cross-sections are just being reported, However, the microscopist needs to know the explicit dependence of damage on: (1) the molecular properties, (2) the density and characteristics of the molecular film and that of the support film, if any, (3) the temperature of the molecular film and (4) certain characteristics of the electron microscope used

Formation and Structure of Casein Micelles in Lactating Mammary Tissue

1970 ◽  
Vol 28 ◽  
pp. 150-151
Author(s):  
Robert J. Carroll ◽  
Marvin P. Thompson ◽  
Harold M. Farrell
Keyword(s):  
Size Distribution ◽  
G Protein ◽  
Milk Proteins ◽  
Mammary Tissue ◽  
Colloidal System ◽  
Casein Micelles ◽  
The Stability

Milk is an unusually stable colloidal system; the stability of this system is due primarily to the formation of micelles by the major milk proteins, the caseins. Numerous models for the structure of casein micelles have been proposed; these models have been formulated on the basis of in vitro studies. Synthetic casein micelles (i.e., those formed by mixing the purified αsl- and k-caseins with Ca2+ in appropriate ratios) are dissimilar to those from freshly-drawn milks in (i) size distribution, (ii) ratio of Ca/P, and (iii) solvation (g. water/g. protein). Evidently, in vivo organization of the caseins into the micellar form occurs in-a manner which is not identical to the in vitro mode of formation.

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