A strain of Tick-borne encephalitis virus designated Zausaev (Za) was isolated in Siberia from a patient who died of a progressive (2-year) form of tick-borne encephalitis 10 years after being bitten by a tick. The complete genomic sequence of this virus was determined, and an attempt was made to correlate the sequence with the biological characteristics of the virus. Phylogenetic analysis demonstrated that this virus belongs to the Siberian subtype of Tick-borne encephalitis virus.
View Article and Find Full Text PDFAnalysis of low-molecular virus-specific proteins of all the known members of the tick-borne encephalitis (TBE) complex viruses: TBE (2 strains), Langat, louping-ill, Negishi, Kyasanur Forest disease, Omsk hemorrhagic fever (2 strains), and Powassan, was performed. The cells infected with the above viruses were found to contain low-molecular virus-specific NVX (with the exception of Powassan, Omsk hemorrhagic fever, and Kyasanur Forest disease viruses), NV21/2, NV2, NV11/2, and NV1 proteins. These proteins (except NV1) differ in the electrophoretic mobility in the viruses under study and in TBE strains No.
View Article and Find Full Text PDFA comparative analysis of tryptic hydrolysates of virus-specific proteins NV5, V3 and NV3 of the tick-borne encephalitis complex viruses showed proteins NV5 to have considerable regions of similar amino acid sequences, V3 proteins to have significantly differing primary structures, and NV3 proteins to have different amino acid sequences.
View Article and Find Full Text PDFA comparative study of high molecular virus-specific proteins in cells infected with flaviviruses from 5 serological subgroups was carried out. Proteins NV5, NV4, and V3 were found to have similar electrophoretic mobility in viruses of the tick-borne encephalitis (TBE) complex with the exception of Powassan virus protein. Proteins NV5 and NV4 of mosquito-borne flaviviruses differ in electrophoretic mobility both from the corresponding proteins of the TBE complex viruses and from each other.
View Article and Find Full Text PDFSynthesis of virus-specific polypeptides occurs in pig embryo kidney cells infected with tick-borne encephalitis virus and treated with actinomycin D, cycloheximide, and hypertonic concentrations of NaCl in various combinations. Despite the fact that virus-specific matrix RNAs function under such conditions, production of infectious virus particles is inhibited considerably. Virus yield is greatly decreased by treatment with actinomycin D alone and by combined effect of actinomycin D and cycloheximide.
View Article and Find Full Text PDFElectron microscopic studies of morphological lesions in pig embryo kidney cells (PEK) infected with tick-borne encephalitis (TBE) virus as well as morphology and features of TBE morphogenesis after treatment with actinomycin D, cycloheximide and hypertonic NaC1 concentrations in the medium were carried out. Most marked morphological lesions were observed in the cells after combined effect of high NaC1 concentrations in the medium and inhibitors of protein synthesis. After all kinds of treatment, smooth-contour membrane structures were observed in TBE-infected cells.
View Article and Find Full Text PDFPig embryo kidney and BHK-21 cells infected with tick-borne encephalitis virus synthesize a nonvirion antigen differing in its immunological properties from the virion antigens. The antigen has a high thermostability. According to the results of ultrafiltration and gel filtration, its molecular weight is approximately 70-100 kilodaltons.
View Article and Find Full Text PDFThe polyacrylamide gel analysis of large intracellular virus-specific proteins NV5, NV4, and the intracellular form of structural protein V3 established differences in the electrophoretic mobility of each of these proteins formed in cells infected with tick-borne encephalitis, Powassan, Langat, and West Nile viruses. It is assumed that these differences in the electrophoretic mobility of NV5, NV4 proteins, and the intracellular form of V3 protein reflect the differences in the primary structure of each of these proteins in the viruses examined.
View Article and Find Full Text PDF