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Biomedical subjects

N A Perevozchikova

Publications and source records attributed to N A Perevozchikova.

13 recordsLinked to original sources
PubMed1999

[Strain differentiation of the Newcastle disease virus by reverse transcriptase-polymerase chain reaction and sequencing population exchange].

A system for detection and strain differentiation of Newcastle disease virus (NDV) by reverse transcription of polymerase chain reaction (RT-PCR) (isolation of RNA, choice of primers for nested PCR, and purification of PCR products) and sequencing is developed and optimized. A nucleotide sequence of gene F site, coding for the F2/F1 cleavage site of F0 fusion protein and including several hypervariable regions, is determined for 10 Russian strains and vaccine strains. The data indicate a replacement of NDV populations in Russia and a rapid evolution of the virus. The origin of pathogenic NDV strains which have been circulating up to the present time is still unknown.

Base Sequence↗
PubMed1998

[Molecular basis of changes in biological properties of foot and mouth disease virus of subtype A22].

Primary structure of capsid proteins and RNA polymerase of three closely related strains of foot and mouth disease virus (FMDV), subtype A22, differing by biological properties (the initial epitheliotropic strain A22 550 and its derivatives: thermoresistant myotropic A22 550/4 and thermosensitive attenuated A22 645) are compared by nucleic acid sequencing and analysis of the amino acid sequencing. The study revealed 1 substitute in VPI and 8 in RNA polymerase in the myotropic variant and 1 substitute in VP2, 2 in VP3, 13 in VP1, and 3 in RNA polymerase. Alteration of A22 550/4 tropism is probably due to a single substitution Gly 145-->Thr in the RGD site of capsid protein VP1. Analysis of the origin and biological properties of the attenuated strain A22 645 and the results of studies of the primary structure of proteins permit us to hypothesize that attenuation is polygenic, caused by adaptation to a heterologous host (continuous porcine cell culture), and can be expressed by changes in the structure of virus antireceptor providing its binding to cell receptors. Sites responsible for the reproduction of A22 FMDV at certain temperatures are presumably located in RNA polymerase.

Amino Acid Sequence↗
PubMed1997

Three-dimensional structure of infectious bursal disease virus determined by electron cryomicroscopy.

Infectious bursal disease virus (IBDV), a member of the Birnaviridae group, is a commercially important pathogen of chickens. From electron micrographs of frozen, hydrated, unstained specimens, we have computed a three-dimensional map of IBDV at about 2 nm resolution. The map shows that the structure of the virus is based on a T=13 lattice and that the subunits are predominantly trimer clustered. The subunits close to the fivefold symmetry axes are at a larger radius than those close to the two- or threefold axes, giving the capsid a markedly nonspherical shape. The trimer units on the outer surface protrude from a continuous shell of density. On the inner surface, the trimers appear as Y-shaped units, but the set of units surrounding the fivefold axes appears to be missing. It is likely that the outer trimers correspond to the protein VP2, carrying the dominant neutralizing epitope, and the inner trimers correspond to protein VP3, which has a basic carboxy-terminal tail expected to interact with the packaged RNA.

Animals↗
PubMed1997

[Bacterial synthesis of immunogenic epitopes of foot-and-mouth disease virus fused either to human necrosis factor or to hepatitis B core antigen].

Using recombinant DNA technology, construction and bacterial expression of genes was carried out which code for hybrid proteins, human tumor necrosis factor and hepatitis B core protein fused to immunogenic epitopes of foot-and-mouth disease virus, strains A22 and O1-194. Hybrids of tumor necrosis factor with foot-and-mouth disease antigenic determinants protected laboratory animals against the experimental challenge with a homologous strain of foot-and-mouth disease virus. Hybrid protein that contained immunogenic regions of two strains, A22 and O1-194, protected animals against infection with both A and O serotypes. Hybrid proteins based on hepatitis B virus core antigen retained the ability to assemble into core-like particles.

Animals↗
PubMed1997

[A simple method for RNA isolation and purification].

RNAs from Escherichia coli cells, Syrian hamster kidney cells, foot-and-mouth disease virus, and Newcastle disease virus were isolated using glass fiber filters GF/F or GF/C. The RNA was reversibly adsorbed on the filters in the presence of 2 M guanidine thiocyanate and 50% ethanol (or isopropanol) and eluted with water. The fraction composition of the isolated RNA depended on the guanidine thiocyanate and alcohol concentrations in the adsorption and washing procedures. The RNA preparations obtained by this method can be used in reverse transcription and reverse transcription-polymerase chain reaction without additional purification.

Animals↗
PubMed1996

[Use of aerosol A-300 amd GF/F (GF/C) filters for purifying fragments of DNA, plasmid DNA, and RNA].

Aerosil A-300 and GF/F (GF/C) filters were used for purifying plasmid DNA and intact RNA as well as for the recovery of DNA fractionated on agarose gels. In the presence of guanidinium thiocyanate Aerosil A-300 and GF/F (GF/C) filters selectively bind nucleic acids, while proteins, agarose polysaccharides and salts are washed off. Nucleic acids desorbed from the Aerosil and filters are available immediately as substrates: DNA for restriction analysis, ligation and sequencing; RNA--for RT-PCR.

DNA↗