La Crosse virus soluble cell culture antigen

1977 ◽  
Vol 6 (6) ◽  
pp. 618-626
Author(s):  
H S Lindsey ◽  
R A Klimas ◽  
J F Obijeski
Keyword(s):  
Mouse Brain ◽  
Nucleocapsid Protein ◽  
Complement Fixation ◽  
Polyacrylamide Gel Electrophoresis ◽  
Soluble Antigen ◽  
La Crosse Virus ◽  
Suckling Mouse ◽  
Soluble Cell ◽  
Brain Antigen ◽  
Antigen Protein

A virus-free soluble antigen, obtained by ammonium sulfate precipitation of the supernatant fluids of La Crosse virus-infected BHK-21 cell cultures, was more reactive and more specific than infected suckling mouse brain antigen when compared by immunodiffusion and counterelectrophoresis tests. By complement fixation tests, the antigen was cross-reactive with heterologous California group arbovirus hyperimmune mouse ascitic fluids, but to a lesser degree than was the standard sucrose-acetone-extracted infected suckling mouse brain antigen. The major virion nucleocapsid protein of La Crosse virus was found by polyacrylamide gel electrophoresis to be the soluble antigen protein responsible for precipitation in immunodiffusion and counterelectrophoresis tests.

scholarly journals A comparison of complement-fixation titres in poliomyelitis-infected tissue-culture fluids and mouse brains

1958 ◽  
Vol 56 (2) ◽  
pp. 254-259 ◽  
Author(s):  
Golda Selzer
Keyword(s):  
Tissue Culture ◽  
Technical Assistance ◽  
Complement Fixation ◽  
Kidney Tissue ◽  
The Other ◽  
Soluble Antigen ◽  
Infective Virus ◽  
Suckling Mouse ◽  
Poliomyelitis Virus

Ultra-centrifugation of emulsions from suckling mouse brains infected with the MEF1 strain of poliomyelitis virus separates a non-infective antigen, or soluble antigen, from infective virus. This antigen is responsible for most of the complement fixation and explains the high titres obtained. On the other hand, the same virus, and also Mahoney, Type 1 poliomyelitis virus, grown in monkey kidney tissue culture, fail to produce this soluble antigen, and this is probably a factor in the low complement-fixing titres obtained in tests with these fluids.The author would like to express her appreciation of Miss M. Butchart's valuable technical assistance.

scholarly journals Diagnosis of California La Crosse virus infection by counterimmunoelectrophoresis

1978 ◽  
Vol 7 (6) ◽  
pp. 603-608
Author(s):  
H S Lindsey ◽  
W H Thompson ◽  
J F Obijeski
Keyword(s):  
Cell Culture ◽  
Virus Infection ◽  
Complement Fixation Test ◽  
Complement Fixation ◽  
Fixation Test ◽  
Soluble Antigen ◽  
La Crosse Virus ◽  
Convalescent Phase ◽  
Human Sera

La Crosse virus cell culture-derived soluble antigen was used in a counterimmunoelectrophoresis procedure to assess the presence or absence of La Crosse antibodies in 79 paired acute- and convalescent-phase human sera. The counterimmunoelectrophoresis test appeared to measure the same antibody as the complement fixation test but was more sensitive and rapid.

scholarly journals Gel diffusion test in feline infectious peritonitis with infected suckling mouse brain antigen.

1982 ◽  
Vol 44 (4) ◽  
pp. 695-697
Author(s):  
Hiroyuki NAKAYAMA ◽  
Toshiharu HAYASHI ◽  
Yoshinori WATABE ◽  
Toshihiko YANAGISAWA ◽  
Kosaku FUJIWARA
Keyword(s):  
Mouse Brain ◽  
Suckling Mouse ◽  
Diffusion Test ◽  
Feline Infectious Peritonitis ◽  
Brain Antigen ◽  
Gel Diffusion

scholarly journals Complement fixation with antigens prepared from bluetongue virus-infected mouse brains

1956 ◽  
Vol 54 (1) ◽  
pp. 79-88 ◽  
Author(s):  
A. Kipps
Keyword(s):  
Particle Size ◽  
Infected Mouse ◽  
Bluetongue Virus ◽  
Complement Fixation ◽  
Soluble Antigen ◽  
Suckling Mouse ◽  
Serological Specificity

Six strains of bluetongue virus were compared by cross complement-fixation tests performed on Perspex sheets according to the method of Fulton & Dumbell using antigens derived from crude saline extracts, and acetone and ether extracts, of infected suckling mouse brains. Only minor differences were encountered with the former and no significant differences with the latter. The reasons for this are discussed.In the neutralization tests important differences were demonstrated between strains.There is evidence that the soluble antigen is composed of particles of varying size, that the smaller particles are responsible for the marked overlapping in the complement-fixation tests, and that increasing complexity associated with increasing particle size may be concerned with increasing serological specificity.

scholarly journals La Crosse Virus Shows Strain-Specific Differences in Pathogenesis

Pathogens ◽  
2021 ◽  
Vol 10 (4) ◽  
pp. 400
Author(s):  
Sarah N. Wilson ◽  
Krisangel López ◽  
Sheryl Coutermash-Ott ◽  
Dawn I. Auguste ◽  
Danielle L. Porier ◽  
...  
Keyword(s):  
Public Health ◽  
North America ◽  
Viral Encephalitis ◽  
Strain Selection ◽  
La Crosse Virus ◽  
Murine Models ◽  
Suckling Mouse ◽  
Important Public Health ◽  
Representative Strain ◽  
Ancestral Strain

La Crosse virus (LACV) is the leading cause of pediatric viral encephalitis in North America, and is an important public health pathogen. Historically, studies involving LACV pathogenesis have focused on lineage I strains, but no former work has explored the pathogenesis between or within lineages. Given the absence of LACV disease in endemic regions where a robust entomological risk exists, we hypothesize that some LACV strains are attenuated and demonstrate reduced neuroinvasiveness. Herein, we compared four viral strains representing all three lineages to determine differences in neurovirulence or neuroinvasiveness using three murine models. A representative strain from lineage I was shown to be the most lethal, causing >50% mortality in each of the three mouse studies. However, other strains only presented excessive mortality (>50%) within the suckling mouse neurovirulence model. Neurovirulence was comparable among strains, but viruses differed in their neuroinvasive capacities. Our studies also showed that viruses within lineage III vary in pathogenesis with contemporaneous strains, showing reduced neuroinvasiveness compared to an ancestral strain from the same U.S. state (i.e., Connecticut). These findings demonstrate that LACV strains differ markedly in pathogenesis, and that strain selection is important for assessing vaccine and therapeutic efficacies.

scholarly journals STUDIES ON INFLUENZA VIRUS

1941 ◽  
Vol 73 (5) ◽  
pp. 581-599 ◽  
Author(s):  
Edwin H. Lennette ◽  
Frank L. Horsfall
Keyword(s):  
Influenza Virus ◽  
Chick Embryo ◽  
Influenza A Virus ◽  
Influenza A ◽  
Complement Fixation ◽  
Soluble Antigen ◽  
Swine Virus ◽  
Specific Fixation ◽  
Mouse Lungs

Influenza complement fixation tests designed for use with ferret serum are described. Complement-fixing antigens derived from influenza ferret lungs were unsatisfactory due to their low content of soluble antigen; those prepared from mouse lungs or developing chick embryo membranes proved to be better antigenically and were reliable when the various reagents in the test were properly adjusted to eliminate non-specific fixation of complement. The results of cross complement fixation tests indicated that the soluble antigens of the PR8 and W.S. strains of influenza A virus were closely similar, if not identical. They indicated also that the soluble antigen of swine virus possessed components present in the antigens of the human strains of virus.

scholarly journals Analysis of the forms of acetylcholinesterase from adult mouse brain

1975 ◽  
Vol 147 (2) ◽  
pp. 205-214 ◽  
Author(s):  
E D Adamson ◽  
S E Ayers ◽  
Z A Deussen ◽  
C F Graham
Keyword(s):  
Enzyme Activity ◽  
Mouse Brain ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Gel Filtration ◽  
Acetylcholinesterase Activity ◽  
Total Activity ◽  
Polyacrylamide Gel ◽  
Soluble Extract ◽  
Molecular Sizes

The solubilization of 80% of the acetylcholinesterase activity of mouse brain was performed by repeated 2h incubations of homogenates at 37 degrees C in an aqueous medium. Analysis of the soluble extract by gel filtration on Sephadex G-200 showed that up to 80% of the enzyme activity was eluted in a peak which was estimated to consist of molecules of about 74000mol.wt. This peak was called the monomer form of the enzyme. After 3 days at 4 degrees C, the soluble extract was re-analysed and was eluted from the column in four peaks of about 74000, 155000, 360000 and 720000 mol.wt. Since the total activity of the enzyme in these peaks was the same as that in the predominantly monomer elution profile of fresh enzyme, we concluded that the monomer had aggregated, possibly into dimers, tetramers and octomers. Extracts of the enzyme were analysed by polyacrylamide-gel electrophoresis and the resulting multiple bands of enzyme activity on gels were shown to separate according to their molecular sizes, that is by molecular sieving. All these forms had similar susceptibilities to the inhibitors eserine, tetra-isopropyl pyrophosphoramide and compound BW 284c51 [1,5-bis-(4-allyldimethylammoniumphenyl)pentan-3-one dibromide]. Thus the forms of the enzyme in mouse brain which can be detected by gel filtration and polyacrylamide-gel electrophoresis may all be related to a single low-molecular-weight form which aggregates during storage. This supports similar suggestions made for the enzyme in other locations.

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