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Tol’yatti, Russia

Lomakina N.F.,Russian Academy of Agricultural Sciences | Boravleva E.Yu.,Russian Academy of Medical Sciences | Kropotkina E.A.,Russian Academy of Medical Sciences | Yamnikova S.S.,Ivanovskii Institute of Virology | And 2 more authors.
Molecular Genetics, Microbiology and Virology | Year: 2011

The highly pathogenic A/chicken/Kurgan/3/2005, (K/05) H5N1 influenza virus was attenuated using selection in an environment simulating the life cycle of wild duck influenza viruses. The goal of this work was the selection of viruses which are more stable for protease cleavage and low pH than the parent virus. The attenuated virus (K/at) was nonpathogenic for mice and did not induce mortality in embryonated chicken eggs. The pH of K/at hemagglutinin conformational change decreased by 0.45-0.50 units compared with the initial K/05 virus. K/at increased the affinity for fucosylated receptors in contrast to K/05. The total sequencing and analysis of the viral genome identified ten amino acid substitutions (1 in PB2, PB1, NP, and NS1; 2 in NA; and 4 in HA) in K/at relative to the initial K/05 located in functionally important regions. K/at substitutions Asp54Asn in HA1 and Val48Ile in HA2 in hemagglutinine are the reverses to the sequence char- acteristic of wild duck viruses. These substitutions, like the substitution Lys131Thr in HA2, change the mobil- ity of molecules and can influence the parameters of conformation transition of hemagglutinin. The fourth substitution in HA1 Lys222Thr was located in the region of interaction with the receptor. Substitutions in NS1 (Arg37His) and PB1 (Leu218Met) were identified in the region of nuclear localization signal, and muta- tions in proteins PB2 (Asp256Asn) and NP (Trp386Cys) were located at sites involved in the transcription and replication of the viral genome. © Allerton Press, Inc., 2011.


Bulgakov A.D.,Moscow State University of Food Production | Grebennikova T.V.,Ivanovskii Institute of Virology | Yuzhakov A.G.,Ivanovskii Institute of Virology | Aliper T.I.,Ivanovskii Institute of Virology | Nepoklonov E.A.,Moscow State University of Food Production
Molecular Genetics, Microbiology and Virology | Year: 2014

A molecular genetic analysis of genomes of porcine reproductive respiratory syndrome virus (PRRSV) and porcine circovirus type 2 (PCV-2) circulating in the territory of the Russian Federation is given. The results of the study showed the presence of circulation of European genotypes of PRRSV strains that are similar to isolates found in France and Denmark from 1998 to 2001. We explained the homology of a fragment of one of the genes between the Russian isolates and the vaccine strain used in Porcilis PRRS (Intervet) vaccine, but this requires further study. Strains of the North American genotype of PRRS were not found. The PCV-2 genomes fall into three separate groups. One (genotype 2b) is formed by isolates in Malaysia, Brazil, Switzerland, China, Slovakia, the United Kingdom, and the United States, which were isolated during the period from 2004 to the present time. The second group consists of the field sequences of viruses isolated in 2000–2012 in Canada, the United States, China, and South Korea (genotype 2a). The third group is formed by highly pathogenic isolates evolved in 2013 in China (genotype 2c). The circulation of all three known genotypes of PCV-2-2a, 2b, and 2c-in the Russian Federation was shown. © 2014, Allerton Press, Inc.


Vorkunova G.K.,Ivanovskii Institute of Virology | Lupandin S.I.,Ivanovskii Institute of Virology | Bukrinskaya A.G.,Ivanovskii Institute of Virology
Molecular Biology | Year: 2011

HIV-1 matrix protein (MA) is a multifunctional structural protein located on the N-terminus of Gag precursor p55 and is responsible for its transport to the plasma membrane, the site of virus assembly. In the present paper, it has been shown that MA is cleaved from Gag precursor at an early stage of the virus infection and participates in virus assembly. MA is transported into the nuclei wherein it associates with viral RNA (vRNA). The MA-vRNA complex is transported to the plasma membrane. Mutant MA, which lost its membranotropic signal, does not reach the plasma membrane and MA-vRNA complex remains in the nuclei and cytoskeleton. Thus, MA seems to deliver vRNA from the nuclei to plasma membrane through the cytoskeleton, initiating virus assembly. © 2011 Pleiades Publishing, Ltd.

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