Cell-fusion properties of Sendai virus prepared by polyethylene-glycol precipitation

1972 ◽  
Vol 18 (5) ◽  
pp. 607-610 ◽  
Author(s):  
Gregory J. Cook ◽  
Lorne A. Babiuk ◽  
James B. Hudson
Keyword(s):  
Cell Fusion ◽  
Sendai Virus ◽  
Allantoic Fluid ◽  
Electron Microscopic Examination ◽  
Electron Microscopic ◽  
Polyethylene Glycol Precipitation ◽  
Chicken Eggs ◽  
Fusion Ability ◽  
Maximum Retention ◽  
Embryonated Chicken

Sendai virus was concentrated from the allantoic fluid of embryonated chicken eggs by polyethyleneglycol (PEG) precipitation. A concentration of 6–8% PEG sufficed to precipitate essentially all of the virus (measured by hemagglutination) with maximum retention of cell-fusion ability. Electron-microscopic examination of the 6% PEG pellet revealed only intact virions. Thus the method is suitable for preparing Sendai virus for cell-fusion experiments.

An Ultrastructural Study of Interspecific Cell Fusion Induced by Inactivated Sendai Virus

1966 ◽  
Vol 1 (4) ◽  
pp. 401-406
Author(s):  
E. E. SCHNEEBERGER ◽  
H. HARRIS
Keyword(s):  
Cell Fusion ◽  
Hela Cells ◽  
Sendai Virus ◽  
Electron Microscopic Examination ◽  
Electron Microscopic ◽  
Virus Particles ◽  
Large Numbers ◽  
Ehrlich Ascites ◽  
Ehrlich Ascites Cells ◽  
Cytoplasmic Bridges

An electron-microscopic examination was made of the process of cell fusion induced by Sendai virus inactivated by ultraviolet light. Ehrlich ascites cells, HeLa cells, rabbit macrophages, rat lymphocytes and nucleated hen erythrocytes were chosen for study because it had previously been shown that these cells could be fused together, with varying degrees of facility, to form artificial heterokaryons. Cells which had large numbers of microvilli on their surfaces fused together more readily than those which had not, but the presence of microvilli was not essential for fusion to occur. Fusion appeared in all cases to be initiated by the formation of small cytoplasmic bridges between the cells; but virus particles, although present elsewhere on the surface of the cells, were not detected at or near the cytoplasmic bridges. HeLa-hen erythrocyte heterokaryons were formed by the fusion of HeLa cells with red cell ghosts.

scholarly journals High level expression of soluble glycoproteins in the allantoic fluid of embryonated chicken eggs using a Sendai virus minigenome system

2007 ◽  
Vol 7 (1) ◽  
pp. 17 ◽  
Author(s):  
Teresa Corral ◽  
Lorena S Ver ◽  
Geneviève Mottet ◽  
Olga Cano ◽  
Blanca García-Barreno ◽  
...  
Keyword(s):  
Sendai Virus ◽  
Allantoic Fluid ◽  
High Level Expression ◽  
High Level ◽  
Chicken Eggs ◽  
Embryonated Chicken ◽  
Minigenome System

Production of recombinant human lactoferrin in the allantoic fluid of embryonated chicken eggs and its characteristics

2009 ◽  
Vol 65 (1) ◽  
pp. 100-107 ◽  
Author(s):  
Irina L. Tutykhina ◽  
Olga A. Bezborodova ◽  
Maxim M. Shmarov ◽  
Denis Y. Logunov ◽  
Galina L. Neugodova ◽  
...  
Keyword(s):  
Allantoic Fluid ◽  
Human Lactoferrin ◽  
Recombinant Human Lactoferrin ◽  
Chicken Eggs ◽  
Embryonated Chicken

Electron Microscopic Observations on the Rescue of SV40 Virus From Transformed Cells

1972 ◽  
Vol 30 ◽  
pp. 278-279
Author(s):  
Ronald Glaser ◽  
Ross Farrugia
Keyword(s):  
Electron Microscopy ◽  
Cell Fusion ◽  
Sendai Virus ◽  
Simian Virus 40 ◽  
Simian Virus ◽  
Transformed Cells ◽  
Density Gradients ◽  
Electron Microscopic ◽  
Sv40 Virus ◽  
Virus Particles

Several laboratories have reported that simian virus 40 (SV40) was rescued from transformed cells when the nonproducing cells were cocultivated or fused in the presence of ultraviolet inactivated Sendai virus (UV-SV), to potentially susceptible cells. Evidence obtained from studies in which nuclei from heterokaryons were isolated and separated on density gradients, indicated that rescued virus was first detected in the transformed nuclei of the heterokaryons formed during cell fusion. The present study was performed to determine how long after fusion SV40 virus particles could be found in the nuclei of the heterokaryons and to investigate the site of rescue by electron microscopy.

Electron microscopic studies on ultrathin frozen sections of lactating mouse mammary gland

1978 ◽  
Vol 36 (2) ◽  
pp. 46-47
Author(s):  
Jan Zarzycki ◽  
Joseph Szroeder
Keyword(s):  
Mammary Gland ◽  
Protein Denaturation ◽  
Chemical Constituents ◽  
Freeze Substitution ◽  
Electron Microscopic Examination ◽  
Mouse Mammary Gland ◽  
Electron Microscopic ◽  
Preparation Methods ◽  
Microscopic Studies ◽  
Ultrathin Frozen Sections

The mammary gland ultrastructure in various functional states is the object of our investigations. The material prepared for electron microscopic examination by the conventional chemical methods has several limitations, the most important are the protein denaturation processes and the loss of large amounts of chemical constituents from the cells. In relevance to this,one can't be sure about a degree the observed images are adequate to the realy ultrastructure of a living cell. To avoid the disadvantages of the chemical preparation methods,some autors worked out alternative physical methods based on tissue freezing / freeze-drying, freeze-substitution, freeze-eatching techniqs/; actually the technique of cryoultraraicrotomy,i,e.cutting ultrathin sections from deep frozen specimens is assented as a complete alternative method. According to the limitations of the routine plastic embbeding methods we were interested to analize the mammary gland ultrastructure during lactation by the cryoultramicrotomy method.

An Electron Microscopic Study of an Avian Reovirus that Causes Arthritis

1971 ◽  
Vol 29 ◽  
pp. 254-255
Author(s):  
E, R. Walker ◽  
N. O. Olson ◽  
M. H. Friedman
Keyword(s):  
Electron Microscopy ◽  
Viral Genome ◽  
Inner Core ◽  
Avian Reovirus ◽  
Electron Microscopic ◽  
Outer Coat ◽  
Acid Type ◽  
Chicken Eggs ◽  
Icosahedral Particle ◽  
Mature Virus

An unidentified virus, responsible for an arthritic-like condition in chickens was studied by electron microscopy and other methods of viral investigation. It was characterized in chorio-allantoic membrane (CAM) lesions of embryonating chicken eggs and in tissue culture as to: 1) particle size; 2) structure; 3) mode of replication in the cell; and 4) nucleic acid type.The inoculated virus, coated and uncoated, is first seen in lysosomal-like inclusions near the nucleus; the virions appear to be uncoated in these electron dense inclusions (Figure 1), Although transfer of the viral genome from these inclusions is not observable, replicating virus and mature virus crystals are seen in the cytoplasm subsequent to the uncoating of the virions.The crystals are formed in association with a mass of fibrils 50 to 80 angstroms in diameter and a ribosome-studded structure that appears to be granular endoplasmic reticulum adapted to virus replication (Figure 2). The mature virion (Figure 3) is an icosahedral particle approximately 75 millimicrons in diameter. The inner core is 45 millimicrons, the outer coat 15 millimicrons, and the virion has no envelope.

A Comparative Study of Fractographic Replicas

1974 ◽  
Vol 32 ◽  
pp. 566-567
Author(s):  
Loren Anderson ◽  
Pat Pizzo ◽  
Glen Haydon
Keyword(s):  
Electron Microscopy ◽  
Electron Microscopic Examination ◽  
Direct Examination ◽  
Electron Microscopic ◽  
Reliable Technique ◽  
Service Failures ◽  
Transmission Electron ◽  
Mode Of Failure ◽  
Scanning Electron Microscopic ◽  
Scanning Electron

Transmission electron microscopy of replicas has long been used to study the fracture surfaces of components which fail in service. Recently, the scanning electron microscope (SEM) has gained popularity because it allows direct examination of the fracture surface. However, the somewhat lower resolution of the SEM coupled with a restriction on the sample size has served to limit the use of this instrument in investigating in-service failures. It is the intent of this paper to show that scanning electron microscopic examination of conventional negative replicas can be a convenient and reliable technique for determining mode of failure.

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