scholarly journals A method based on light scattering to estimate the concentration of virus particles without the need for virus particle standards

MethodsX ◽  
2015 ◽  
Vol 2 ◽  
pp. 91-99 ◽  
Author(s):  
István Makra ◽  
Péter Terejánszky ◽  
Róbert E. Gyurcsányi
Keyword(s):  
Light Scattering ◽  
Virus Particle ◽  
Virus Particles

Spontaneous Production of Type C Virus Particles in a Culture Derived from Rat Embryo Cells

1972 ◽  
Vol 30 ◽  
pp. 288-289
Author(s):  
Elizabeth S. Priori ◽  
T. Shigematsu ◽  
B. Myers ◽  
L. Dmochowski
Keyword(s):  
Virus Particle ◽  
Mouse Embryo ◽  
Calf Serum ◽  
Embryo Cell ◽  
Virus Particles ◽  
Extracellular Virus ◽  
Mouse Embryo Cell ◽  
Mature Virus Particle ◽  
Embryo Cells ◽  
Type C

Spontaneous release of type C virus particles in long-term cultures of mouse embryo cells as well as induction of similar particles in mouse embryo cell cultures with IUDR or BUDR have been reported. The presence of type C virus particles in cultures of normal rat embryos has not been reported.NB-1, a culture derived from embryos of a New Zealand Black (NB) rat (rats obtained from Mr. Samuel M. Poiley, N.C.I., Bethesda, Md.) and grown in McCoy's 5A medium supplemented with 20% fetal calf serum was passaged weekly. Extracellular virus particles similar to murine leukemia particles appeared in the 22nd subculture. General appearance of cells in passage 23 is shown in Fig. 1. Two budding figures and one immature type C virus particle may be seen in Fig. 2. The virus particles and budding were present in all further passages examined (currently passage 39). Various stages of budding are shown in Figs. 3a,b,c,d. Appearance of a mature virus particle is shown in Fig. 4.

scholarly journals STRUCTURE OF TYPE 5 ADENOVIRUS

1963 ◽  
Vol 118 (2) ◽  
pp. 295-306 ◽  
Author(s):  
Wesley C. Wilcox ◽  
Harold S. Ginsberg
Keyword(s):  
Virus Particle ◽  
Density Gradient ◽  
Infectious Virus ◽  
Relative Proportion ◽  
Specific Antigen ◽  
Equilibrium Density ◽  
Virus Particles ◽  
Infected Cells ◽  
Specific Antigens ◽  
Virus Antigens

Type 5 adenovirus was purified by fluorocarbon (freon 113) treatment followed by banding in a CsCl equilibrium density gradient. This method permitted separation of virus from normal host cell materials and virus-specific soluble antigens. Virus banded in CsCl with a mean bouyant density of 1.3349 gm/cm3. The three virus-specific soluble antigens (group- and type-specific antigens and toxin) banded together with a mean bouyant density of 1.2832 gm/cm3. The group-specific antigen was the predominant antigen of the purified virus particle, whereas the group- and type-specific antigens were present in equal titers in the antigen band. Infectious virus particles were inactivated by prolonged dialysis at pH 10.5. Centrifugation of inactivated virus preparations in a CsCl equilibrium density gradient resulted in separation of virus DNA from specific antigen: the antigens banded with a mean bouyant density of 1.2832 gm/cm3 and the DNA sedimented to the bottom of the tube. The predominant antigen derived from purified virus particles was the group-specific antigen and it was in the same relative proportion to the type-specific antigen as measured in intact particles. The antigens derived from disrupted virus were immunologically identical with the soluble virus antigens present in infected cells.

ON THE MORPHOLOGY AND DEVELOPMENT OF INSECT CYTOPLASMIC-POLYHEDROSIS VIRUS PARTICLES

1965 ◽  
Vol 11 (3) ◽  
pp. 497-501 ◽  
Author(s):  
F. T. Bird
Keyword(s):  
Virus Particle ◽  
Inner Core ◽  
Cytoplasmic Polyhedrosis Virus ◽  
Virus Particles ◽  
Early Stages ◽  
Polyhedrosis Virus

The cytoplasmic-polyhedrosis virus particle is an icosahedron about 68 mμ in diameter. It consists of a capsid, made up of two concentric rings, and an inner core. The capsid has 12 projections.Large masses consisting mostly of the capsids of virus particles develop in the cytoplasm of gut cells infected with cytoplasmic-polyhedrosis virus. Cores of the virus particles are found on the outer surfaces of these masses or in material adjacent to them. The complete virus particle is assembled just before it is enveloped by protein and incorporated into a developing polyhedron.Granules, tentatively identified as lysosomes, increase in number and size during the early stages of infection. Other granules and bodies observed in the gut cells are described.

scholarly journals Postentry Neutralization of Adenovirus Type 5 by an Antihexon Antibody

2004 ◽  
Vol 78 (22) ◽  
pp. 12320-12332 ◽  
Author(s):  
Robin Varghese ◽  
Yeshi Mikyas ◽  
Phoebe L. Stewart ◽  
Robert Ralston
Keyword(s):  
Virus Particle ◽  
Intracellular Transport ◽  
Nuclear Periphery ◽  
Adenovirus Type ◽  
Nuclear Entry ◽  
Viral Attachment ◽  
Virus Particles ◽  
Negative Stain ◽  
Virus Complex ◽  
Negative Stain Electron Microscopy

ABSTRACT Antibodies against hexon, the major coat protein of adenovirus (Ad), are an important component of the neutralizing activity in serum from naturally infected humans and experimentally infected animals. The mechanisms by which antihexon antibodies neutralize the virus have not been defined. As a model system, murine monoclonal antibodies raised against Ad type 5 (Ad5) were screened for antihexon binding and neutralization activity; one monoclonal antibody, designated 9C12, was selected for further characterization. The minimum ratio of 9C12 to Ad5 required for neutralization was 240 antibody molecules per virus particle, or 1 antibody per hexon trimer. Analysis of antibody-virus complexes by dynamic light scattering and negative-stain electron microscopy (EM) showed that the virus particles were coated with electron-dense material but not aggregated at neutralizing ratios. Cryo-EM image reconstruction of the antibody-virus complex showed that the surface of the virus particle was covered by a meshwork of 9C12 antibody density, consistent with bivalent binding at multiple sites. Confocal analysis revealed that viral attachment, cell entry, and intracellular transport to the nuclear periphery still occur in the presence of neutralizing levels of 9C12. A model is presented for neutralization of Ad by an antihexon antibody in which the hexon capsid is cross-linked by antibodies, thus preventing virus uncoating and nuclear entry of viral DNA.

scholarly journals Virus particle assembly into crystalline domains enabled by the coffee ring effect

Soft Matter ◽  
2014 ◽  
Vol 10 (30) ◽  
pp. 5458-5462 ◽  
Author(s):  
Ronald Gebhardt ◽  
Jean-Marie Teulon ◽  
Jean-Luc Pellequer ◽  
Manfred Burghammer ◽  
Jacques-Philippe Colletier ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Virus Particle ◽  
Contact Line ◽  
Capillary Flow ◽  
Particle Assembly ◽  
Virus Particles ◽  
Coffee Ring ◽  
Coffee Ring Effect ◽  
Crystalline Domains

Tobacco mosaic virus particles can be rapidly assembled into 3D-domains by capillary flow-driven alignment at the triple contact-line of an evaporating droplet.

Interactions and Dimensions of fd-Virus Particles Determined from Electric Light Scattering

1995 ◽  
Vol 171 (1) ◽  
pp. 173-178 ◽  
Author(s):  
Viktor Peikov ◽  
Stoyl Stoylov ◽  
Ivana Petkanchin
Keyword(s):  
Light Scattering ◽  
Virus Particles ◽  
Electric Light ◽  
Fd Virus

scholarly journals THE STRUCTURE OF ANTIGEN-ANTIBODY COMPLEXES

1963 ◽  
Vol 118 (3) ◽  
pp. 327-340 ◽  
Author(s):  
June Almeida ◽  
Bernhard Cinader ◽  
Allan Howatson
Keyword(s):  
Electron Microscope ◽  
Virus Particle ◽  
Cross Linking ◽  
Short Axis ◽  
Antibody Molecule ◽  
Virus Particles ◽  
Ring Structures ◽  
Antigenic Relation ◽  
Antigen Antibody ◽  
Beaded Appearance

Negatively stained aggregates of antigen (polyoma or verruca vulgaris virus) and antibody (from rabbit or goat) were examined in the electron microscope. The antibody molecules appeared as cylindrical rods (often, but not always, showing a beaded appearance) with a long axis of 250 to 270 A and a short axis of 35 to 40 A. The combining sites were at the opposite short ends of the antibody molecules separated by the length of 250 to 270 A of the antibody molecule. Aggregates of antigen and antibody showed regions of orderly arrangements and frequently ring structures of five or more linked virus particles. Sometimes a virus particle in the center of these ring structures was linked to the peripheral particles. In extreme antibody excess, cross-linking was only rarely observed and virus particles were surrounded by a dense aura of antibody molecules. The specificity of the two combining sites of most antibody molecules is identical. This was utilized to examine the antigenic relation between the normal (icosahedral) and aberrant forms of polyoma virus.

Research on Measures of Reducing Environmental Pollutions by Empty Capsid Virus Particles with Vaccine of Foot and Mouth Disease Virus to Control FMD

2014 ◽  
Vol 1023 ◽  
pp. 257-261
Author(s):  
Qi Hong ◽  
Zi Hong Liu ◽  
Duan Dan Han
Keyword(s):  
Virus Particle ◽  
Foot And Mouth Disease ◽  
Mouth Disease ◽  
Promising Candidate ◽  
Effective Measure ◽  
Virus Particles ◽  
Empty Capsid ◽  
Mouth Disease Virus ◽  
Foot And Mouth ◽  
Potential Benefits

Foot-and-mouth disease (FMD) is a highly contagious disease in cloven-hoofed animals, and had been broken out worldwide several times in recent years. In order to extinct outbreak of FMD, a large number of infected animals are slaughtered in some countries, and the slaughterings had been caused a series of environmental pollutions seriously. To reduce this kind of pollution, vaccination is an effective measure to protect animals against FMD, however, FMD virus (FMDV) escaping from manufacturing plant and inactivated incompletely during vaccine production could cause an outbreak of FMD. Therefore, inactivated FMDV vaccines are not safe to animals and environment. FMDV empty capsid (lacking nucleic acid) can elicit the same antibody response as infectious FMDV, thus, empty capsid virus particle vaccine of FMDV would be the most promising candidate vaccine for its safety and protection against FMDV. In this report, we studied the empty capsid virus particle vaccine of FMDV to control FMD and its potential benefits to the environment.

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