Results 181 to 190 of about 1,365,518 (224)

Bluetongue Virus in Exotic Ruminants

Journal of the American Veterinary Medical Association, 1973
SUMMARY An epizootic of a hemorrhagic disease occurred in 6 species of exotic ruminants at the San Diego Zoo and San Diego Wild Animal Park in 1970 and 1971. The disease was reproduced in deer by inoculation of pericardial and pleural fluids from a muntjac (Muntiacus reeuesi) and the spleen of a kudu (Tragelaphus capensis). The agent was also recovered
G L, Hoff, L A, Griner, D O, Trainer
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Isolation and identification of bluetongue virus

Journal of Virological Methods, 2000
Bluetongue virus (BTV) is an arthropod-borne orbivirus that infects sheep, wild ruminants and occasionally cattle. Detection and specific identification of BTV is a multistep process. The first step involves the isolation of the virus from the animal's blood or other tissues, followed by inoculation of embryonating chicken eggs (ECE).
A, Clavijo, R A, Heckert, G C, Dulac, A, Afshar   +3 more
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Bluetongue Virus Structural Components

1990
The structural components of bluetongue virus (BTV), the prototype of the orbivirus genus, has been the subject of a number of reviews (Verwoerd et al. 1979; Gorman and Taylor 1985; Spence et al. 1984). The main features can be summarized as follows: BTV is an icosahedral-shaped particle consisting of a segmented double-stranded RNA genome encapsidated
H, Huismans, A A, Van Dijk
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Purification and characterization of bluetongue virus

Virology, 1969
Abstract Purified bluetongue virus was shown to possess a double-stranded RNA genome, very similar to that of reovirus, consisting of at least three double-stranded components. A low molecular weight component probably equivalent to the adenine-rich single strand found in reovirus was present in varying amounts.
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Association of bluetongue virus with the cytoskeleton

Virology, 1987
Analysis of the distribution of [35S]methionine-labeled virus proteins following lysis of bluetongue virus (BTV)-infected cells with nonionic detergents showed that a major proportion of the virus-specific proteins was located in the insoluble nuclear-cytoskeletal fraction.
B T, Eaton, A D, Hyatt, J R, White
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Bluetongue Virus Assembly and Morphogenesis

2006
Like other members of the Reoviridae, bluetongue virus faces the same constraints on structure and assembly that are imposed by a large dsRNA genome. However, since it is arthropod-transmitted, BTV must have assembly pathways that are sufficiently flexible to allow it to replicate in evolutionarily distant hosts.
P, Roy, R, Noad
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The impact of bluetongue virus on reproduction

Comparative Immunology, Microbiology and Infectious Diseases, 1994
Bluetongue virus has been recognized as an important noncontagious, arthropodborne infectious viral disease of ruminants. 24 different serotypes of virus have been recognized worldwide. The most severe clinical disease has been associated with severe clinical disease in sheep and some free ranging wild ruminants. A number of reports have implicated the
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Association of Bluetongue Virus with the Cytoskeleton

1989
Eukaryotic cells contain an extensive filamentous network referred to as the cytoskeleton, and it is currently believed that all animal viruses may use the cytoplasmic or nuclear skeletal matrix of cells for at least part of their replication cycle (Luftig, 1982; Penman, 1985).
B T, Eaton, A D, Hyatt
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Bluetongue virus-induced interferon in cattle

American Journal of Veterinary Research, 1985
SUMMARY Calves were inoculated iv with bluetongue virus (btv), serotype 10. Titers of interferon (ifn) in serum and btv in peripheral blood were determined. All inoculated calves produced circulating ifn that persisted for 2 to 4 days. Highest titers of btv in peripheral blood were present after serum ifn was no longer detected.
N J, MacLachlan, J, Thompson
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Bluetongue virus: surface exposure of VP7

Virus Research, 1990
The exposed proteins of bluetongue virus serotype 17 were determined using surface labeling and reactivity with monoclonal antibodies. Iodination of amino groups predominantly labeled VP2; however, iodination of tyrosine residues labeled both VP2 and VP5, with VP7 labeled to a significantly lesser degree.
S A, Lewis, M J, Grubman
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