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  1. Article: [Genetic characterization of the Batken virus (BKNV) (Orthomyxoviridae, Thogotovirus) isolated from the Ixodidae ticks Hyalomma marginatum Koch, 1844 and the mosquitoes Aedes caspius Pallas, 1771, as well as the Culex hortensis Ficalbi, 1889 in the Central Asia].

    Al'khovskiĭ, S V / L'vov, D K / Shchelkanov, M Iu / Shchetinin, A M / Deriabin, P G / L'vov, D N / L'vov, S S / Samokhvalov, E I / Gitel'man, A K / Botikov, A G

    Voprosy virusologii

    2014  Volume 59, Issue 2, Page(s) 33–37

    Abstract: The prototype strain LEIV-K306 of the Batken virus (BKNV) was isolated from the Ixodidae ticks Hyalomma marginatum Koch, 1844 collected from sheep near town Batken (Kirgizstan) in the April 1970. Later, the BKNV was isolated in Kirgizstan from the mixed ... ...

    Abstract The prototype strain LEIV-K306 of the Batken virus (BKNV) was isolated from the Ixodidae ticks Hyalomma marginatum Koch, 1844 collected from sheep near town Batken (Kirgizstan) in the April 1970. Later, the BKNV was isolated in Kirgizstan from the mixed pool of the Aedes caspius Pallas, 1771 and Culex hortensis Ficalbi, 1889 mosquitoes. From the very beginning, the BKNV was discussed to be very close to the Dhori virus (DHOV) (Orthomyxoviridae, Thogotovirus) isolated from the Ixodidae ticks Hyalomma dromedarii Koch, 1844 in India. In this work, virtually complete genome sequence (MiSeq, Illumina) of the BKNV was determined (ID GenBank KJ396672-4). Structural and non-structural proteins of the BKNV have a high level of homology with DHOV - 98% (PB1) and 96% (PB2, PA, NP, M). Homology of HA protein between the BKNV and DHOV is 90%, which accounts for antigenic difference between these close relative viruses. Since the differences in the other structural and non-structural proteins are about 96-98%, the BKNV could be suggested as the topotypic DHOV strain for Central Asia, Transcaucasia, and Northern Caspian region. The evolution divergence of the BKNV and DHOV for HA could be explained by local ecologic peculiarities of the BKNV areal.
    MeSH term(s) Aedes/virology ; Animals ; Biota ; Birds/virology ; Culex/virology ; Gene Library ; Genome, Viral ; Ixodes/virology ; Orthomyxoviridae/classification ; Orthomyxoviridae/genetics ; Orthomyxoviridae/isolation & purification ; Sequence Analysis, DNA
    Language Russian
    Publishing date 2014-03
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article
    ZDB-ID 201241-8
    ISSN 0507-4088
    ISSN 0507-4088
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  2. Article ; Online: The Dual NOD1/NOD2 Agonism of Muropeptides Containing a Meso-Diaminopimelic Acid Residue.

    Dagil, Yulia A / Arbatsky, Nikolai P / Alkhazova, Biana I / L'vov, Vyacheslav L / Mazurov, Dmitriy V / Pashenkov, Mikhail V

    PloS one

    2016  Volume 11, Issue 8, Page(s) e0160784

    Abstract: ... muropeptides with long and branched peptide chains and requires an intact N-acetylmuramyl residue. Muropeptides ...

    Abstract Muropeptides are fragments of peptidoglycan that trigger innate immune responses by activating nucleotide-binding oligomerization domain (NOD) 1 and NOD2. Muropeptides from Gram-negative bacteria contain a meso-diaminopimelic acid (meso-DAP) residue in either a terminal or a non-terminal position. While the former ones are known to be recognized by NOD1, much less is known about recognition of muropeptides with non-terminal meso-DAP, which are most abundant moieties of Gram-negative peptidoglycans. Here, we developed a novel system to assess biological activity of muropeptides, based on CRISPR/Cas9-mediated knockout (KO) of NOD1 and NOD2 genes in modified HEK293T cells. Using NOD1/NOD2 knockout and overexpression systems, as well as human monocytes and macrophages, we refine the current view of muropeptide recognition. We show that NOD2 can recognize different natural muropeptides containing a meso-DAP residue (preferably in a non-terminal position), provided they are present at micromolar concentrations. NOD2 accepts muropeptides with long and branched peptide chains and requires an intact N-acetylmuramyl residue. Muropeptides with non-terminal meso-DAP can activate NOD1 as well, but, in this case, probably require peptidase pre-processing to expose the meso-DAP residue. Depending on NOD1/NOD2 ratio in specific cell types, meso-DAP-containing muropeptides can be recognized either primarily via NOD2 (in monocytes) or via NOD1 (in monocyte-derived macrophages and HEK293T-derived cells). The dual NOD1/NOD2 agonism of meso-DAP-containing muropeptides should be taken into account when assessing cellular responses to muropeptides and designing muropeptide immunostimulants and vaccine adjuvants.
    MeSH term(s) Adjuvants, Immunologic/pharmacology ; Cells, Cultured ; Cytokines/metabolism ; Diaminopimelic Acid/pharmacology ; HEK293 Cells ; Humans ; Immunity, Innate/drug effects ; Macrophages/cytology ; Macrophages/drug effects ; Macrophages/immunology ; Macrophages/metabolism ; Monocytes/cytology ; Monocytes/drug effects ; Monocytes/immunology ; Monocytes/metabolism ; Nod1 Signaling Adaptor Protein/agonists ; Nod1 Signaling Adaptor Protein/metabolism ; Nod2 Signaling Adaptor Protein/agonists ; Nod2 Signaling Adaptor Protein/metabolism
    Chemical Substances Adjuvants, Immunologic ; Cytokines ; NOD1 protein, human ; NOD2 protein, human ; Nod1 Signaling Adaptor Protein ; Nod2 Signaling Adaptor Protein ; Diaminopimelic Acid (583-93-7)
    Language English
    Publishing date 2016
    Publishing country United States
    Document type Journal Article
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0160784
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  3. Article: [The Khurdun virus (KHURV): a new representative of the orthobunyavirus (Bunyaviridae)].

    Al'kovskhovskiĭ, S V / Shchetinin, A M / L'vov, D K / Shchelkanov, M Iu / Deriabin, P G / L'vov, D N / Samokhvalov, E I / Gitel'man, A K / Botikov, A G

    Voprosy virusologii

    2013  Volume 58, Issue 4, Page(s) 10–13

    Abstract: ... The KHURV genome comprises three negative-sense RNA segments (L, M, and S); its terminal ...

    Abstract Unidentified Khurdun virus (KHURV) was isolated in 2001 from coot (Fulica atra, Linnaeus, 1758) in the Volga River delta (Astrakhan Region, Russian Federation). Here we report that the KHUV genome was de novo sequenced (on Illumina platform) and the KHURV was classified as a novel prototypic bunyavirus. The KHURV genome comprises three negative-sense RNA segments (L, M, and S); its terminal nucleotide sequences are canonical for the Orthobunyavirus genus. Based on the results of the molecular-genetic and phylogenetic analysis we suggest that the KHURV belongs to the genus Orthobunyavirus (Bunyaviridae).
    MeSH term(s) Animals ; Base Sequence ; Birds/virology ; Cercopithecus aethiops ; Genome, Viral ; Molecular Sequence Data ; Orthobunyavirus/classification ; Orthobunyavirus/genetics ; Orthobunyavirus/isolation & purification ; Phylogeny ; RNA, Viral/genetics ; Sequence Analysis, RNA ; Vero Cells
    Chemical Substances RNA, Viral
    Language Russian
    Publishing date 2013-07
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 201241-8
    ISSN 0507-4088
    ISSN 0507-4088
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  4. Article: [Antiviral activity of sulfated polysaccharide from the brown algae Laminaria japonica against avian influenza A (H5N1) virus infection in the cultured cells].

    Makarenkova, I D / Deriabin, P G / L'vov, D K / Zviagintseva, T N / Besednova, N N

    Voprosy virusologii

    2010  Volume 55, Issue 1, Page(s) 41–45

    Abstract: The antiviral activity of the sulfated polysaccharide fucoidan from the brown sea algae Laminaria japonica against infection caused by highly virulent avian influenza virus (Alduck/Novosibirsk/02/05, H5N1) in the sensitive pig embryo kidney cell cultures ...

    Abstract The antiviral activity of the sulfated polysaccharide fucoidan from the brown sea algae Laminaria japonica against infection caused by highly virulent avian influenza virus (Alduck/Novosibirsk/02/05, H5N1) in the sensitive pig embryo kidney cell cultures was studied. Fucoidan was ascertained to have no cytotoxic activity and to show virucidal activity against influenza A/H5N1 virus. When given at concentrations of 50 to 500 microg/ml, fucoidan protected the cell cultures from the cytopathogenic activity of influenza virus in a dose of 0.01 TCID50/1.0 ml and was able to suppress influenza A/H5N1 virus production within 24 hours of infection when prophylactic and therapeutic-and-prophylactic treatment regimens were used.
    MeSH term(s) Animals ; Antiviral Agents/chemistry ; Antiviral Agents/isolation & purification ; Antiviral Agents/pharmacology ; Cell Line ; Cytopathogenic Effect, Viral/drug effects ; Influenza A Virus, H5N1 Subtype/drug effects ; Influenza A Virus, H5N1 Subtype/physiology ; Laminaria/chemistry ; Polysaccharides/chemistry ; Polysaccharides/isolation & purification ; Polysaccharides/pharmacology ; Swine ; Virus Replication/drug effects
    Chemical Substances Antiviral Agents ; Polysaccharides ; fucoidan (9072-19-9)
    Language Russian
    Publishing date 2010-03-18
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article
    ZDB-ID 201241-8
    ISSN 0507-4088
    ISSN 0507-4088
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  5. Article: [Estimation of activity of bis-netropsin derivatives based on a model of an experimental cutaneous herpes simplex virus disease of guinea pigs].

    andronova, V L / Grokhovskiĭ, S L / Surovaia, A N / Gurskiĭ, G V / Deriabin, P G / L'vov, D K / Galegov, G A

    Voprosy virusologii

    2013  Volume 58, Issue 1, Page(s) 32–35

    Abstract: Using the model of an experimental cutaneous infection of guinea pig males caused by herpes simple virus type 1, it is shown that application of dimerico derivatives of netropsin Lys-bis Nt and 15Lys-bis Nt in the form of polietilenglicol-based ointment ... ...

    Abstract Using the model of an experimental cutaneous infection of guinea pig males caused by herpes simple virus type 1, it is shown that application of dimerico derivatives of netropsin Lys-bis Nt and 15Lys-bis Nt in the form of polietilenglicol-based ointment suppresses viral infection more effectively than acyclovir.
    MeSH term(s) Acyclovir/pharmacology ; Administration, Topical ; Animals ; Antiviral Agents/pharmacology ; Disease Models, Animal ; Guinea Pigs ; Herpes Simplex/drug therapy ; Herpes Simplex/pathology ; Herpesvirus 1, Human ; Male ; Netropsin/analogs & derivatives ; Netropsin/pharmacology ; Ointments
    Chemical Substances Antiviral Agents ; Ointments ; Netropsin (64B3O0RD7N) ; Acyclovir (X4HES1O11F)
    Language Russian
    Publishing date 2013-01
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 201241-8
    ISSN 0507-4088
    ISSN 0507-4088
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  6. Article: [Pathogenicity of West Nile virus: molecular markers].

    Anishchenko, M / Shchelkanov, M Iu / Alekseev, V V / Lipnitskiĭ, A V / Antonov, V A / Dzharkenov, A F / Bushkieva, B Ts / L'vov, D N / Deriabin, P G / Kolobukhina, L V / L'vov, D K

    Voprosy virusologii

    2010  Volume 55, Issue 1, Page(s) 4–10

    Abstract: The review describes the phenotypic properties, structure, and expression pattern of West Nile virus genome (Flaviviridae, Flavivirus, Japanese encephalitis antigenic complex), as well as the clinical picture and pathogenesis of its etiologically related ...

    Abstract The review describes the phenotypic properties, structure, and expression pattern of West Nile virus genome (Flaviviridae, Flavivirus, Japanese encephalitis antigenic complex), as well as the clinical picture and pathogenesis of its etiologically related disease West Nile fever. It also analyzes the available data on the impact of genetic mutations in the genome on the biological properties of the virus.
    MeSH term(s) Animals ; Capsid Proteins/genetics ; Genetic Markers ; Genome, Viral ; Humans ; Viral Nonstructural Proteins/genetics ; Viral Structural Proteins/genetics ; Virulence/genetics ; West Nile Fever/diagnosis ; West Nile Fever/physiopathology ; West Nile Fever/virology ; West Nile virus/classification ; West Nile virus/genetics ; West Nile virus/pathogenicity
    Chemical Substances Capsid Proteins ; Genetic Markers ; Viral Nonstructural Proteins ; Viral Structural Proteins
    Language Russian
    Publishing date 2010-01
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article ; Review
    ZDB-ID 201241-8
    ISSN 0507-4088
    ISSN 0507-4088
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  7. Article: [Susceptibility of pandemic influenza virus A 2009 H1N1 and highly pathogenic avian influenza virus A H5N1 to antiinfluenza agents in cell culture].

    Fediakina, I T / Shchelkanov, M Iu / Deriabin, P G / Leneva, I A / Gudova, N V / Kondrat'eva, T V / L'vov, D K

    Antibiotiki i khimioterapiia = Antibiotics and chemoterapy [sic

    2011  Volume 56, Issue 3-4, Page(s) 3–9

    Abstract: The data on cytotoxicity and antiviral activity of commercial antivirals, such as Remantadine, Oseltamivir, Arbidol and Ribavirin in the MDCK cell culture infected with highly pathogenic (H5N1) and pandemic 2009 (H1N1) influenza A viruses are presented. ... ...

    Abstract The data on cytotoxicity and antiviral activity of commercial antivirals, such as Remantadine, Oseltamivir, Arbidol and Ribavirin in the MDCK cell culture infected with highly pathogenic (H5N1) and pandemic 2009 (H1N1) influenza A viruses are presented. The study of the antiviral activity of antivirals in the MDCK cells culture demonstrated that Arbidol, Rimantadine and Ribavirin efficiently inhibited reproduction of the highly pathogenic H5N1 influenza viruses isolated from sick birds. Arbidol and Oseltamivir carboxylate selectively inhibited reproduction of the pandemic 2009 H1N1 influenza A viruses with changed specificity to the cell receptors, causing severe influenza in men, while remantadine had no effect on their reproduction.
    MeSH term(s) Animals ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Birds ; Cell Line ; Drug Resistance, Viral/drug effects ; Humans ; Indoles/pharmacology ; Indoles/therapeutic use ; Influenza A Virus, H1N1 Subtype/drug effects ; Influenza A Virus, H5N1 Subtype/drug effects ; Influenza in Birds/drug therapy ; Influenza, Human/drug therapy ; Oseltamivir/pharmacology ; Oseltamivir/therapeutic use ; Ribavirin/pharmacology ; Ribavirin/therapeutic use ; Rimantadine/pharmacology ; Rimantadine/therapeutic use ; Virus Replication/drug effects
    Chemical Substances Antiviral Agents ; Indoles ; Rimantadine (0T2EF4JQTU) ; Oseltamivir (20O93L6F9H) ; Ribavirin (49717AWG6K) ; umifenovir (93M09WW4RU)
    Language Russian
    Publishing date 2011-08-31
    Publishing country Russia (Federation)
    Document type Journal Article
    ZDB-ID 269110-3
    ISSN 0235-2990
    ISSN 0235-2990
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  8. Article ; Online: The Dual NOD1/NOD2 Agonism of Muropeptides Containing a Meso-Diaminopimelic Acid Residue.

    Yulia A Dagil / Nikolai P Arbatsky / Biana I Alkhazova / Vyacheslav L L'vov / Dmitriy V Mazurov / Mikhail V Pashenkov

    PLoS ONE, Vol 11, Iss 8, p e

    2016  Volume 0160784

    Abstract: ... muropeptides with long and branched peptide chains and requires an intact N-acetylmuramyl residue. Muropeptides ...

    Abstract Muropeptides are fragments of peptidoglycan that trigger innate immune responses by activating nucleotide-binding oligomerization domain (NOD) 1 and NOD2. Muropeptides from Gram-negative bacteria contain a meso-diaminopimelic acid (meso-DAP) residue in either a terminal or a non-terminal position. While the former ones are known to be recognized by NOD1, much less is known about recognition of muropeptides with non-terminal meso-DAP, which are most abundant moieties of Gram-negative peptidoglycans. Here, we developed a novel system to assess biological activity of muropeptides, based on CRISPR/Cas9-mediated knockout (KO) of NOD1 and NOD2 genes in modified HEK293T cells. Using NOD1/NOD2 knockout and overexpression systems, as well as human monocytes and macrophages, we refine the current view of muropeptide recognition. We show that NOD2 can recognize different natural muropeptides containing a meso-DAP residue (preferably in a non-terminal position), provided they are present at micromolar concentrations. NOD2 accepts muropeptides with long and branched peptide chains and requires an intact N-acetylmuramyl residue. Muropeptides with non-terminal meso-DAP can activate NOD1 as well, but, in this case, probably require peptidase pre-processing to expose the meso-DAP residue. Depending on NOD1/NOD2 ratio in specific cell types, meso-DAP-containing muropeptides can be recognized either primarily via NOD2 (in monocytes) or via NOD1 (in monocyte-derived macrophages and HEK293T-derived cells). The dual NOD1/NOD2 agonism of meso-DAP-containing muropeptides should be taken into account when assessing cellular responses to muropeptides and designing muropeptide immunostimulants and vaccine adjuvants.
    Keywords Medicine ; R ; Science ; Q
    Subject code 572
    Language English
    Publishing date 2016-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
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  9. Article: Tungsten-containing enzymes.

    L'vov, N P / Nosikov, A N / Antipov, A N

    Biochemistry. Biokhimiia

    2002  Volume 67, Issue 2, Page(s) 196–200

    Abstract: The biological importance of tungsten has been fully proved in the last decade due to isolation of a number of tungsten-containing enzymes (W-enzymes) from hyperthermophilic archaea. Tungsten was previously considered only as an antagonist of molybdenum, ...

    Abstract The biological importance of tungsten has been fully proved in the last decade due to isolation of a number of tungsten-containing enzymes (W-enzymes) from hyperthermophilic archaea. Tungsten was previously considered only as an antagonist of molybdenum, because the replacement of molybdenum by tungsten (due to their chemical similarity) leads to inactivation of molybdenum-containing enzymes (Mo-enzymes). In addition to the "true W-enzymes" in which tungsten cannot be replaced by molybdenum, recently some enzymes have been isolated which can use either molybdenum or tungsten in the catalytic process. This review briefly summarizes data on the participation of tungsten in catalysis by some enzymes and the structure of the active sites of W-enzymes.
    MeSH term(s) Bacteria/enzymology ; Bacterial Proteins/metabolism ; Binding Sites ; Enzymes/metabolism ; Models, Molecular ; Molybdenum/metabolism ; Tungsten/metabolism
    Chemical Substances Bacterial Proteins ; Enzymes ; Molybdenum (81AH48963U) ; Tungsten (V9306CXO6G)
    Language English
    Publishing date 2002-01-28
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 1109-5
    ISSN 1608-3040 ; 0006-2979 ; 0320-9717
    ISSN (online) 1608-3040
    ISSN 0006-2979 ; 0320-9717
    DOI 10.1023/a:1014461913945
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  10. Article: [Taxonomic status of the Chim virus (CHIMV) (Bunyaviridae, Nairovirus, Qalyub group) isolated from the Ixodidae and Argasidae ticks collected in the great gerbil (Rhombomys opimus Lichtenstein, 1823) (Muridae, Gerbillinae) burrows in Uzbekistan and Kazakhstan].

    L'vov, D K / Al'khovskiĭ, S V / Shchelkanov, M Iu / Shchetinin, A M / Aristova, V A / Morozova, T N / Gitel'man, A K / Deriabin, P G / Botikov, A G

    Voprosy virusologii

    2014  Volume 59, Issue 3, Page(s) 18–23

    Abstract: ... polyprotein GnGc (M-segment), whereas 50%--for the nucleocapsid N (S-segment). The data obtained permit ... The amino acid homology between the CHIMV and QYBV is 87% for the RdRp catalytic center (L-segment) that is ...

    Abstract Full-length genome of the Chim virus (CHIMV) (strain LEIV-858Uz) was sequenced using the next-generation sequencing approach (ID GenBank: KF801656). The CHIMV/LEIV-858Uz was isolated from the Ornithodoros tartakovskyi Olenev, 1931 ticks collected in the great gerbil (Rhombomys opimus Lichtenstein, 1823) burrow in Uzbekistan near Chim town (Kashkadarinsky region) in July of 1971. Later, four more CHIMV strains were isolated from the O. tartakovskyi, O. papillipes Birula, 1895, Rhipicephalus turanicus Pomerantsev, 1936 collected in the great gerbil burrows in Kashkadarinsky, Bukhara, and Syrdarya regions of Uzbekistan, and three strains--from the Hyalomma asiaticum Schulze et Schlottke, 1930 from the great gerbil burrows in Dzheskazgan region of Kazakhstan. The virus is a potential pathogen of humans and camels. The phylogenetic analysis revealed that the CHIMV is a novel member of the Nairovirus genus (Bunyaviridae) and closely related to the Qalyub virus (QYBV), which is prototype for the group of the same name. The amino acid homology between the CHIMV and QYBV is 87% for the RdRp catalytic center (L-segment) that is coincident with both QYBV and CHIMV associated with the Ornithodoros ticks and burrow of rodents as well. The CHIMV homologies with other nairoviruses are 30-40% for the amino acid sequences of precursor polyprotein GnGc (M-segment), whereas 50%--for the nucleocapsid N (S-segment). The data obtained permit to classify the CHIMV as a member of the QYBV group in the genus of Nairovirus (Bunyaviridae).
    MeSH term(s) Amino Acid Sequence ; Animals ; Argasidae/virology ; Base Sequence ; Bunyaviridae Infections/veterinary ; Bunyaviridae Infections/virology ; Genome, Viral ; Gerbillinae/parasitology ; Gerbillinae/virology ; Ixodes/virology ; Kazakhstan ; Molecular Sequence Data ; Nairovirus/classification ; Nairovirus/genetics ; Nairovirus/isolation & purification ; Phylogeny ; RNA Replicase/genetics ; Rodent Diseases/virology ; Sequence Homology, Amino Acid ; Uzbekistan
    Chemical Substances RNA Replicase (EC 2.7.7.48)
    Language Russian
    Publishing date 2014-05
    Publishing country Russia (Federation)
    Document type English Abstract ; Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 201241-8
    ISSN 0507-4088
    ISSN 0507-4088
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