[Study of the antigenic structure of tick-borne encephalitis virus using synthetic peptides].

A number of peptides, fragments of the envelope protein E of the tick-borne encephalitis virus (Sofjin strain), were synthesized. Their binding to the polyclonal antiserum to protein E was studied. Rats were immunized with both the free peptides and their KLH-conjugates, and the resulting antisera were tested for their reactivity toward protein E and for their neutralizing activity toward the virus in cell culture.

[Identification of individual antigenic epitopes of the envelope protein in the tick-borne encephalitis virus using monoclonal antibodies].

A variant analysis of virus antigens of tick-borne encephalitis complex was carried out by enzyme immunoassays and topographic mapping of this protein using a panel of monoclonal antibodies to the structural glycoprotein of tick-borne encephalitis (TBE) virus of the Far East subtype. The results of the study confirmed the existence on the structural protein of both identical determinants typical of all the antigens of the complex and of subgroup-specific determinants. The topological analysis of the epitopes binding monoclonal antibodies revealed 3 separate domains possessing different functional properties.

[Monoclonal antibodies against tick-borne encephalitis virus glycoprotein: preliminary characterization].

Characterization of 12 clones of monoclonal antibodies (MAb) generated for the main immunogen of tick-borne encephalitis virus, glycoprotein E, is presented. The following MAb parameters have been determined: constants of binding with antigen, classes and subclasses of immunoglobulins, the activity in two variants of solid-phase enzyme-immunoassay, binding with protein A, and MAb behavior in serologic tests: hemagglutination-inhibition, diffuse precipitation in agar, and virus neutralization. The preliminary studies revealed the presence in these MAb of at least three groups of antibody complementary to various nonoverlapping sites on the structural virus glycoprotein.

[Dhori virus--a causative agent of human disease. 5 cases of laboratory infection].

The materials presented in the paper are first indications of the pathogenicity of Dhori virus for man and prove the role of this agent in the occurrence of 5 cases of the disease in laboratory workers accidentally infected during the preparation of cultural agents. Clinically, Dhori infection was characterized by an acute course with marked general toxicity and a febrile period of 2 to 4 days. Two out of 5 patients had changes on the part of the nervous system of the type of encephalitic reaction predominantly with subcortical symptoms and mild involvement of the pyramidal system or in the form of encephalopolyradiculoneuritis with paresthesia and sensitivity disorders.

[Subunit immunogen of the tick-borne encephalitis virus. The immunological characteristics of glycoprotein V3 from 2 antigenic types of tick-borne encephalitis virus].

V3 glycoprotein isolated from virions of two antigenic types of TBE virus was found to be a valuable immunogen in experimental immunizations of rabbits and mice. The immune sera contained high titres of antibodies to TBE virus and other viruses of the TBE antigenic complex detectable in three serological tests. Species-, type-, and group-specific antibodies to TBE viruses were demonstrated.

[Subunit immunogen of the tick-borne encephalitis virus. The isolation of glycoprotein V3 from 2 types of the tick-borne encephalitis virus and a study of its amino acid composition].

An effective method for isolation of the membrane structural E protein, the so-called V3 glycoprotein, is described. Preliminary data of its amino acid composition have been obtained.

[Cloning and primary structure of DNA copies of genome fragments of the tick-borne encephalitis virus].

RNA of a flavivirus-tick-borne encephalitis virus (Far-East, type 1, strain Sofin) was subjected to reverse transcription and the DNA copy was transformed into double-stranded DNA by action of E. coli DNA-polymerase (Klenow's fragment) without primer. The hairpin structures were removed by S1 nuclease.