[Localization of the antigenic segment of the tick-borne encephalitis virus envelope protein using monoclonal antibodies]. / Lokalizatsiia antigennogo uchstka belka obolochki virusa kleshchevogo éntsefalita s ispol'zovaniem monoklonal'nykh antitel.

The largest cyanogen bromide fragment (GP-14,5; coordinates 78-176) of E protein belonging to the envelope of the tick-borne encephalitis (TBE) virus (Far Eastern subtype, strain Sofjin) interacted with five out of twelve E-specific monoclonal antibodies (MAbs). Having compared; efficiencies of some MAbs binding to the antigens of TBE viruses of Far Eastern and West European subtypes and primary structures of analogous peptides of these viruses, we suggested the epitopes of these MAbs to be located in the vicinity of 89 and/or 116-th amino acid residues of E protein. Effect of denaturing agents and reduction followed by carboxymethylation on the protein E antigenic properties was studied.

[Protein E 98-113 sequence is a fusion site of tick-borne encephalitis virus with cellular membrane]. / Posledovatel'nost' 98-113 belka E virusa kleshchevogo éntsefalita iavliaetsia uchastkom sliianiia virusa s kletochnoi membranoi.

The synthetic peptide with the conservative 98-113 sequence of protein E of tick-borne encephalitis virus was studied in order to elucidate its role in the functioning of flaviviruses. The peptide was shown to inhibit the in vitro infection of macrophages with the virus. An antibody that specifically binds this peptide was found among the set of monoclonal antibodies produced against protein E. This antibody was found to prevent penetration of the virus into liposomes. A correlation was found between our results and data on the spatial structure of protein E and its interspecies homology. The protein E 98-113 sequence of the tick-borne encephalitis virus was found to be the fusion site of the viral envelope with a cellular membrane.

[Identification of individual antigenic epitopes of the envelope protein in the tick-borne encephalitis virus using monoclonal antibodies]. / Identifikatsiia otdel'nykh antigennykh épitopov belka obolochki virusa kleshchevogo éntsefalita s primeneniem monoklonal'nykh antitel.

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. The results of topological mapping and immune typing of TBE virus antigen were compared.

[Preparation and properties of monoclonal antibodies to tick-borne encephalitis viral nonstructural proteins]. / Poluchenie i svoistva monoklonal'nykh antitel k nestrukturnym belkam virusa kleshchevogo entsefalita.

Hybridomas secreting monoclonal antibodies (Mab) to tick-borne encephalitis (TBE) virus are obtained. Immunodiffusion showed that 3 Mabs to TBE protein NS3 belong to class IgM and the rest to IgG1. Mabs to TBE protein NS1 were tested in hemagglutination inhibition, complement fixation, neutralization, and protection tests. Only 1 hybridoma produced Mab specific for protein NS1 of TBE strain Sofyin, the rest reacted with the common antigenic determinants of nonstructural TBE complex.

[Monoclonal antibodies against tick-borne encephalitis virus glycoprotein: preliminary characterization]. / Monoklonal'nye antitela k glikoproteidu virusa kleshchevogo éntsefalita: predvaritel'naia kharakteristika.

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. Further employment of these MAb in practical and research work is discussed.

[Use of protein A in the immunosorbent analysis of antibodies to the tick-borne encephalitis virus]. / Primenenie belka A v immunosorbentnom analize antitel k virusu kleshchevogo éntsefalita.

The results of the studies made with a view to developing the method for the determination of specific antibodies to the antigen of tick-borne encephalitis virus in human blood serum and liquor are presented. The method is based on the capacity of Staphylococcus aureus protein A to bind with Fc-region of immunoglobulins, which makes it possible to use this protein as the "second" system of antibodies. The conditions for the sorption of the antigen on polystyrene test tubes and for binding 125I-or horse radish peroxidase-labeled protein A preparations with antibodies have been determined, and the method has been approved in tests made on sera and liquor obtained from donors and tick-borne encephalitis patients.