Search PubMed⌕ Search

Biomedical subjects

V M Blinov

Publications and source records attributed to V M Blinov.

At least 37 records · Page 2Linked to original sources
PubMed1993

Ankyrin-like proteins of variola and vaccinia viruses.

Computer analysis of full coding sequences of variola major virus strain India-1967 genome and vaccinia virus strain Copenhagen genome have been carried out. A wide set of proteins containing ankyrin-like repeats have been identified for both viruses. Only three proteins of this family of the studied viruses are highly homologous. The rest of the proteins are different. The possible role of such proteins in determination of virus tissue tropism is discussed.

Amino Acid Sequence↗
PubMed1993

Analysis of the nucleotide sequence of a 43 kbp segment of the genome of variola virus India-1967 strain.

Sequencing and computer analysis of the nucleotide sequence of the variola virus strain India-1967 (VAR) genome segment (43069 bp) from the region of HindIII C, E, R, Q, K, H DNA fragments has been carried out. Forty-three potential open reading frames (ORFs) have been identified, and the polypeptides encoded by them have been compared with the analogous proteins of vaccinia virus strain Copenhagen (COP). ORF E7R of VAR is much shorter than the COP analog. The other polypeptides coded by the potential ORFs of VAR are highly conserved in comparison with COP. Possible functions of the predicted viral polypeptides are discussed.

African Swine Fever Virus↗
PubMed1993

Nucleotide sequence analysis of variola virus HindIII M, L, I genome fragments.

DNA of the variola major virus strain India-1967 in the region of HindIII M, L, I fragments has been sequenced. Analysis of this sequence of 18029 bp revealed 19 potential open reading frames (ORFs). Four proposed proteins (L2R, H9R, L5L, L6R) contain metal-binding domains. Comparison of the variola virus (VAR) and vaccinia virus strain Copenhagen (COP) sequences show that the main differences are between proteins L1R and I5R. L1R contains 6 additional amino acid residues on the C-terminus. The protein I5R of VAR contains three Ca2+ binding domains but this COP has deletions in 2 of the 3 established domains. Possible functions of the predicted viral polypeptides are discussed.

Amino Acid Sequence↗
PubMed1993

[The molecular mechanism of the action of antiviral preparations in the adamantane series].

Regions of possible interaction between remantadine and transmembrane M2 protein are revealed by analysis of amino acid substitutions in remantadine- and deutiforin-resistant influenza viruses. The major region includes 5-6 amino acid residues at position 25-31, partially involving the premembrane region and the first position of a hydrophobic membrane-associated domain. The proposed model action of remantadine and its derivatives suggests that remantadine is included into the cell membrane lipid bimolecular layer by its adamantane share and its positively charged NH2-group is exposed to the cell surface. This allows remantadine and its analog to be regarded as molecular "hindrances" for viral particle decapsidation and budding.

Adamantane↗
PubMed1992

The envelope glycoprotein of Ebola virus contains an immunosuppressive-like domain similar to oncogenic retroviruses.

Genomic RNA of a Zaire strain of Ebola virus was cloned, and cDNA inserts specific for the glycoprotein gene were isolated and sequenced. The determined sequence has only one open reading frame encoding 318 amino acids and is part of ORF-4 on the plus RNA strand. The putative transcriptional stop site (3' AAUUCUUUUU 5') and the transcriptional start site (3' AACUACUUCUAAUU..5') were identified. Computer-assisted comparison of the amino acid sequence of the C-terminal part of protein encoded by ORF-4 of Ebola virus with sequences of the proteins present in the SWISSPROT and EMBL banks revealed significant homology with the 'immunosuppressive domain' of the p15E envelope proteins of various oncogenic retroviruses. The possible role of such a homology is discussed.

Amino Acid Sequence↗
PubMed1992

Cytochrome C (Fe2+) as a competitive inhibitor of NADPH-dependent reduction of cytochrome P450 LM2: locating protein-protein interaction sites in microsomal electron carriers.

The kinetics of NADPH-dependent reduction of cytochrome P450 LM2 in the soluble monomeric reconstituted system in the absence of any substrate is shown to be monophasic. We show that ferrous cytochrome c acts as a competitive inhibitor of the reduction. In the presence of 1 mM benzphetamine an additional extremely fast phase was observed. Under these conditions ferrous cytochrome c was found to be a competitive inhibitor of the slow phase of the reduction process, which accounted for 80% of the total reduction amplitude. Inhibition experiments yield a dissociation constant for the LM2-reductase complex of 3.0 +/- 1.5 microM. This constant was the same both in the presence and in the absence of benzphetamine. Based on these data we conclude that cytochromes P450 and c bind to the same center on the NADPH-cytochrome P450 reductase molecule. Comparative analysis of the amino acid sequences reveals a detectable similarity between cytochrome c and cytochrome P450 LM2 at positions 68-87 and 121-145, respectively. In addition, a substantial similarity was shown for sequence fragments 204-224 of NADPH-cytochrome P450 reductase and 40-60 of cytochrome b5. Based on these findings a hypothesis for the location of the centers of intermolecular interactions on the molecules of cytochrome P450 LM2 and NADPH-cytochrome P450 reductase is proposed.

Amino Acid Sequence↗
PubMed1991

The complete sequence of the group-specific antigen, VP7, of African horsesickness disease virus serotype 4 reveals a close relationship to bluetongue virus.

The complete sequence of the S7 RNA that codes for the major group-specific coat protein. VP7, of African horsesickness virus serotype 4 (AHSV-4) was determined from cDNA analyses and found to be 1179 nucleotides in length. One single open reading frame of 353 codons was observed defining a protein of Mr 38,107 with a net charge of -1.5 at neutral pH. Comparison of the AHSV-4 VP7 sequence with that of bluetongue virus serotype 10 revealed an overall similarity of 44%, with the amino- and carboxy-terminal regions exhibiting the greatest levels of homology. In addition, potential secondary structures of the terminal sequences of the S7 RNA segments of AHSV-4 and BTV serotypes 10, 13 and 17 are presented.

African Horse Sickness Virus↗
PubMed1991

[Malignant fibrous histiocytoma of the larynx].

A rare case of larynx malignant fibrous histiocytoma is presented. Histologically and ultrastructurally, the tumour was similar to malignant fibrous histiocytoma of other organs. The patient was followed up for 2 years after surgical treatment and preoperative irradiation. No recurrence and metastases were observed.

Aged↗
PubMed1991

[Evolution of drug treatment of rhabdomyosarcoma in children].

Rhabdomyosarcoma is the most frequently occurring type of malignant solid tumors in children. The tumor site, aggressive growth, proneness to recurrence, metastatic spreading, and high neglect predetermine the negligible share of the surgical method in multimodality treatment of rhabdomyosarcomas. Of importance are the development and the use of different types and schemes of drug therapy which can be employed in combination with radiotherapy. Drug therapy of rhabdomyosarcomas has large practical potentialities which rise from year to year.

Antineoplastic Agents↗
PubMed1991

Nucleotide sequence of cDNA coding for mink proopiomelanocortin (POMC) and its comparative analysis with POMC mRNA primary structures from pituitaries of other animal species and man.

cDNA for proopiomelanocortin (POMC) of mink has been cloned and sequenced. A comparative analysis of the primary structures of mRNAs coding for proopiomelanocortins of eight animal species and man has been performed. The analysis has revealed conserved and variable POMC mRNA regions. High variability of some of the regions is suggested to be due to the peculiarities of their structural organization. A putative mechanism responsible for the mutations in variable regions is proposed. A tree of the evolutionary relations of POMC has been developed.

Amino Acid Sequence↗
PubMed1991

[Marburg virus: the first determined nucleotide sequence of two genes].

The preparations of purified Marburg virus were isolated from blood plasma of infected guinea pigs and characterized. Viral RNA was extracted from the virions. The cDNA was synthesized on the isolated RNA matrix by the reverse transcriptase with the use of dissipated priming. The obtained cDNA was inserted into the plasmid pBR322 by the connector technique and the resulting recombinant plasmids were cloned in Escherichia coli cells. The specific clones selected by molecular hybridization method were analyzed by the restriction mapping and cross-hybridization. Four overlapping cDNA clones were found and the virus specific 5012 bp fragment of the viral genome was sequenced. Three open reading frames were found and the preliminary analysis of the coded amino acid sequence and corresponding genes was fulfilled.

Amino Acid Sequence↗
PubMed1991

[Nucleotide sequence of genes and complete amino acid sequence of tick-borne encephalitis virus strain 205].

The 10466 nucleotide long sequence of the cDNA copy of the tick-borne encephalitis strain 205 viral genome has been determined. It includes the 5'-nontranslating region, the genes for structural as well as nonstructural proteins and the first 93 nucleotides of 3'-nontranslating region. The difference in amino acid sequences of structural and nonstructural proteins of strains 205. Sofjin and Neudoerfl of the tick-borne encephalitis virus and the nucleotide changes in 5'- and 3'-nontranslating of these strains are discussed.

Amino Acid Sequence↗
PubMed1990

Mapping mutations in influenza A virus resistant to norakin.

To elucidate the mode of action of norakin against influenza A virus we sequenced the hemagglutinin gene of 11 norakin-resistant mutants. Resistance was coupled with 1-3 amino acid exchanges. The majority of mutations was localized in the HA2 polypeptide and was mostly associated with changes in charge or polarity of the amino acids. The amino acid substitutions are discussed in the context of the 3D structure of X31 hemagglutinin considered to be representative of the influenza hemagglutinins. Most of the mutations appear to destabilize the pH 7.0 structure by distorting or destroying hydrogen bonds as well as salt-bridges which are responsible for intra- and intersubunit contacts, while others destabilize the location of the fusion peptide, facilitating conformational changes in the presence of the inhibitor.

Amino Acids↗