[Antigenic activity of human herpes virus type 8 proteins coding orfK8.1 and orf65].

A peptide scanning of the sequences of human herpes virus type 8 (HHV-8) proteins coding orfK8.1 and orf65 was made. The antigenic activity of peptides was evaluated by ELISA.

[Study of the diagnostic potential of various regions of tick-borne encephalitis virus glycoprotien E].

Bioinformation techniques were used to analyze envelope glycoprotein of tick-borne encephalitis virus in order to determine the potential diagnostically significant antigenic clusters. Five selected regions of the amino acid sequence of protein E were retranslated to nucleic sequences, by employing the optimum code for E. coli.

[Comparison of the diagnostic value of recombinant antigens and synthetic peptides that mimic the immunogenic epitopes of the envelop protein gp41 in the enzyme immunodetection of HIV-1 antibodies].

The study was undertaken to comparatively examine the efficiency of HIV antibody detection by enzyme immunoassay using recombinant antigens and synthetic peptides containing the most immunodominant region of the human immunodeficiency virus envelop protein gp41-cytotoxic T-lymphocytic (CTL) epitope. The application of the synthetic peptides that mimic this region has been to be inadequately effective. The recombinant proteins that contain the CTL epitope may be successfully used for the diagnosis of HIV-1, by using enzyme immunoassay as they show a higher sensitivity in detecting antibodies than do the synthetic peptises.

[Test for specific antibodies to virus hepatitis delta based on synthetic peptides].

Solid-phase synthesis of three linear peptides overlapping the major immunodominant epitope of HDAg, which located within amino acid (aa) segment 53-108, and peptide aa 167-179 was carried out. The structure of the peptides corresponded to the sequences of isolates HDV type I. Their antigen reactivity was studied by indirect enzyme immunoassay with sera from patients with hepatitis D and from asymptomatic carriers of anti-delta antibodies.

Characterization of monoclonal antibodies and epitope mapping of the NS4 protein of hepatitis C virus.

Recombinant DNA containing sequences of HCV NS4 protein was expressed in Escherichia coli cells. Six hybridoma clones producing monoclonal antibodies (MAB) to recombinant NS4 protein (rNS4), aa 1677-1756, were developed. Mapping with a panel of 33 peptides and reciprocal competitive EIA have shown that MAB obtained revealed five antigen determinants, not described earlier: MAB 3F11 and 3F12-one genotype-independent epitope of NS4A (aa 1700-1707) common for genotypes 1, 2 and 3; MAB 1D11-genotype-independent epitope (aa 1713-1728) and MAB 1D3-genotype (subtype 1b)-specific epitope of NS4B (aa 1711-1731); MAB 6B11 and C1-two conformation-dependent determinants in 5-1-1 region.