Publications by authors named "Medvedkina O"

Puumala virus (PUUV) and other Arvicolinae-borne hantaviruses are difficult to cultivate in cell culture. To isolate these hantaviruses efficiently, hantavirus nucleocapsid protein (NP)-positive but seronegative wild rodents were selected by NP-detection ELISA. Three of 68 Myodes glareolus captured in Samara, Russia, were NP-positive and seronegative.

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European Russia is a highly endemic area of hemorrhagic fever with renal syndrome (HFRS), a rodent-borne zoonotic disease, caused by hantaviruses. In total, 145 small mammals of four species (Myodes glareolus, Apodemus flavicollis, A. agrarius, and A.

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Puumala virus (PUUV), a causative agent of hemorrhagic fever with renal syndrome (HFRS), is prevalent in Europe and European Russia. No vaccine has been developed for PUUV-associated HFRS, primarily because of the low viral yield in cultured cells. A PUUV strain known as DTK/Ufa-97 was isolated in Russia and adapted for growth in Vero E6 cells maintained in serum-free medium.

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The effect of specific restriction endonuclease on the simian adenovirus SV20 DNA was studied. It was shown that endonucleases SalI, XbaI, EcoRI, BamHI, HindIII cleaved the viral DNA into 3, 4, 5, 5, 8 specific fragments respectively. The sequence of fragments (physical map) was determined and found to be B-C-A for enzyme SalI, C-D-B-A--for enzyme Xbal, E-A-C-D-B--for enzyme EcoRI, B-E-C-A-D--for enzyme BamHI and B-E-A-C-(GH)-D-F--for enzyme HindIII.

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Extracts from encephalomyocarditis (EMS) virus infected Krebs II ascites carcinoma cells pulse-labeled during the active virus-specific synthesis and then chased were fractionated in a sucrose concentration gradient. It has shown that some radioactivity was detectable in the polysome region as well as in the regions of ribosome monomers and ribosomal subunits. An analysis of the radioactive material in a CsCl density gradient and by polyacrylamide gel electrophoresis has shown that components of the protein-synthesizing system in infected cells are bound to some proteins, the electrophoretic mobility of which corresponds to that of polypeptides found in the infected cells, namely, polypeptides G 16 (18 kdalton) and 22 (22 kdalton).

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