Biomedical subjects

V M Sorokin

Publications and source records attributed to V M Sorokin.

At least 19 recordsLinked to original sources

PubMed2000

[Species- and genus-specific antigenic epitopes of Francisella tularensis lipopolysaccharides].

Lipopolysaccharide (LPS) antigenic epitopes of natural virulent and isogenic avirulent Francisella tularensis strains and other species of the Francisella genus (F. novicida, F. novicida-like, and F. philomiragia) were studied by dot and immunoblotting. Polyclonal rabbit and human sera to virulent F. tularensis strains and monoclonal antibodies to F. tularensis LPS O-side chain were used for detecting species- and genus-specific LPS epitopes. Typical virulent F. tularensis strains produce two types of S-LPS with different antigenic specificity simultaneously. Antigenic determinants of two LPS types were located in LPS O-polysaccharide but not in the core oligosaccharide. The epitopes of the first LPS type were characterized by species specificity for F. tularensis in contrast to determinants of the second LPS type, which had epitopes common with F. novicida. Cross exhaustion of human and rabbit antitularemic sera by F. tularensis and F. novicida LPS showed that F. novicida LPS molecules contained at least two epitopes--highly specific for F. novicida and common with the second type of F. tularensis LPS. The immune response of rabbits and humans to F. tularensis LPS epitopes was different in principle. Sera from rabbits immunized with vaccine and virulent F. tularensis strains contained antibodies "recognizing" antigenic epitopes of two S-LPS forms of the bacterium: type 1 species-specific (in high titers) and type 2 epitopes common with F. novicida LPS (in low titers). In addition to these, sera from patients with tularemia contain immunoglobulins to species-specific epitopes of F. novicida LPS in high titers. Experiments on avirulent mutants showed that in some cases attenuation of F. tularensis can involve loss of species-specific LPS form, while S-LPS with epitopes common with F. novicida LPS will be retained. The difference in specificity of human and rabbit antitularemic antibodies is due to individual features in the host immune system.

Animals↗

PubMed1998

[Characterization of structure and antigenic activity of lipopolysaccharides of genus Francisella].

Wild-type representatives of Francisella genus (F. tularensis, F. novicida, F. novicida-like, and F. philomiragia) produce S-type lipopolysaccharides (LPS) possessing different antigenic activity and common antigenic determinants in the core oligosaccharide. Electrophoretic analysis showed that F. philomiragia produced S-LPS containing two major molecular components with minor fractions between them, whereas S-LPS of F. tularensis, F. novicida, and F. novicida-like are characterized by the typical frequency distribution of molecules. A characteristic feature of Francisella LPS was the ability to form the dominant molecular components with similar electrophoretic mobility of major fractions of the original F. philomiragia LPS upon long storage in water solution. Natural virulent F. tularensis strains produce at least two types of S-LPS. Polysaccharide chains of type I S-LPS possess O-species-specific antigens, whereas the polysaccharide part of type II S-LPS has nonspecific antigenic epitopes. A decrease of F. tularensis virulence can be associated with impaired production of both S-LPS types or loss of S-LPS with O-species-specific antigenic activity.

Antigens, Bacterial↗

PubMed1996

Francisella tularensis resistance to bactericidal action of normal human serum.

Lipopolysaccharide and outer membranes from the three virulent encapsulated (Cap(+)) strains of three subspecies of Francisella tularensis and their isogenic avirulent capsule-deficient (Cap(-)) mutants were isolated. It was shown that the Cap cells and their outer membranes almost completely consumed the available complement of normal human serum whereas Cap(-) LPS (R-LPS), Cap(+) cells and their components activated the complement less effectively. Absorption of normal human serum with Cap(-) strain dramatically reduced the complement consumption for homologous strain and its surface structures. This reduction reflected the loss of bactericidal antibodies. Addition of antibodies to whole cells of F. tularensis completely restored complement activity. The cross-absorbing experiments demonstrated that Cap(-) cells more effectively deplete bactericidal antibodies than homologous virulent strain. From these results it can be concluded that normal human serum is bactericidal for serum-sensitive Cap(-) F. tularensis strains through the action of complement initiated by the classical complement pathway and serum resistance of virulent strains is not due to absence of targets for bactericidal antibodies, but is due to their low accessibility because of O-side chains of lipopolysaccharide.

Antibodies, Bacterial↗

PubMed1990

[Relation between the Yersinia phage and bacteriophages isolated from the environment].

The bacteriophage designated RD2 has been isolated from the sewage in Rostov-on-Don city and studied. The morphology of bacteriophage particles and the biological properties of the bacteriophage make it related to the plague bacteriophage isolated by D'Errel. The molecular masses of the compared bacteriophages are almost identical being 26.4 +/- 0.4 Md for RD2 and 24.7 +/- 0.2 Md for D'Errel bacteriophage. The DNAs of the bacteriophages share 80% of homology and possess 15 nonhomologous regions scattered along the genomes. The phages are serologically related. The DNAs of both bacteriophages give the similar pattern of hydrolysis by restriction endonuclease EcoRV, but have the different sensitivity to many other restriction endonucleases. The protein specter of bacteriophage RD2 contains 18 polypeptides (11 minor ones), while the one of D'Errel bacteriophage contains 7 polypeptides similar in molecular mass with the polypeptides of RD2. The bacteriophage RD2 cannot be considered one of the plague causative agents of bacteriophages since the region where it has been isolated has a long epidemiological and epizootical record of absence of plague.

Bacteriophage Typing↗

PubMed1989

[Transcription map of a recombinant plasmid carrying a gene for the synthesis of pesticine I and a protein for pesticine I immunity in the plague microbe].

Molecules of the plasmids pBR322 and pRD17 have been compared by electron microscopy technique of R-loops visualization. Comparative location of R-loops on the plasmids has been computerized on minicomputer HP9825A due to the program making possible to define the coordinates of the transcription start and direction. The 5.1 kb fragment coding for pesticin I and immunity protein to pesticin I and cloned in pBR322 vector plasmid is flanked by Bam HI-EcoRI sites. Five promoter regions and direction of transcription were localized on the fragment.

Bacteriocins↗

PubMed1986

[Restriction map of pesticinogenicity plasmid pYP1 of Yersinia pestis].

The restriction map of Yersinia pestis pesticinogenicity plasmid pYP1 has been constructed with the use of 18 restriction endonucleases. Plasmid dimensions (6.3 Md) have been specified, the genes for pesticin synthesis, for pesticin immunity protein, fibrinolysin and plasmocoagulase have been localized by molecular cloning of single plasmid DNA fragments in vector plasmid pBR322.

Bacteriocins↗

PubMed1986

[Detection of modification-restriction systems in Yersinia enterocolitica].

Four Y. enterocolitica strains (10166, 10373, 2119, 5513) have been studied for the presence of the enzymatic systems of modification-restriction (M-R). As revealed with the use of cross titration, strains 10166 and 10373 contain M-R systems, supposedly of type II.

Adsorption↗

PubMed1984