Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q8IXL6 (RNS)
 1,091 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Enzyme linked immunosorbent assays (ELISAs) and a nested polymerase chain reaction after reverse transcription (RT-PCR) were used for the detection of the Chinese strain (C strain) of classical swine fever virus (CSFV) in blood and tissue samples of experimentally inoculated piglets. One group of 10 piglets was inoculated with C strain material from rabbits and a second one with material from infected minipig kidney (MPK) cell culture. Tested blood samples were taken on the day of inoculation as well as on days 2, 4, 6, 8, 10, 13 and 16. Samples of spleen, tonsil and brain tissue were collected from piglets on days 6, 8, 10, 13 and 16 and tested for glycoprotein E(RNS) and protein NS2-3 using commercially available ELISA kits. E(RNS) and NS2-3 were detected earlier in blood samples of piglets inoculated with the C strain propagated in a cell culture. Regardless of propagation the presence of the viral E(RNS) and NS2-3 was detected in spleen and tonsil samples simultaneously. The C strain propagated in a cell culture was found in only one brain sample, whereas, the virus propagated in rabbits was detected in 70% of the brain samples. For the detection of the CSFV RNA in blood samples, a part within the 5' non-coding region was amplified. The differences in the results gained by antigen detection in blood samples decreased when nested RT-PCR was used.
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PMID:Classical swine fever virus (C strain) distribution in organ samples of inoculated piglets. 1135 13

Bovine viral diarrhoea virus (BVDV) is a member of the genus Pestivirus within the family Flaviviridae. In this report, protein localization studies were performed to assess the mechanism for the release of mature virus particles from infected cells. Since BVDV is an enveloped virus, budding from either intra- or extracellular membranes is feasible. A prerequisite for the latter mechanism is the integration of viral glycoproteins into the host cell membrane. Using monoclonal antibodies (MAbs) directed against the viral envelope glycoproteins E2 and E(RNS), no specific signals were detected on the surface of BVDV-infected cells by indirect fluorescence, confocal microscopy or fluorescence-activated cell sorter analyses. Furthermore, biotin-labelled cell surface proteins of virus-infected and non-infected cells were not detected by immunoprecipitation using MAbs directed against E(RNS) and E2 or the non-structural protein NS2-3. None of these proteins was detected on the cell surface. In addition, to analyse the intracellular localization of the two viral glycoproteins E(RNS) and E2 and the non-structural proteins NS2-3 and NS3, subcellular fractionation of virus-infected cells followed by radioimmunoprecipitation with the MAbs were performed. These results led to the conclusion that the BVDV envelope glycoproteins E(RNS) and E2 as well as the non-structural proteins NS2-3 and NS3 were almost quantitatively associated with intracellular membranes. These findings indicate that BVDV is released by budding into the cisternae of the endoplasmic reticulum and that there seems to be no correlation between the location and function of the analysed proteins.
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PMID:Localization of viral proteins in cells infected with bovine viral diarrhoea virus. 1160 70