Immunoreactivity of synthetic peptides, corresponding to B-cellular epitopes of human type I T-lymphotrophic virus structural proteins

• Published in: Molekuliarnaia biologiia Vol. 27; no. 4; p. 880
• Main Authors: Rasuli, A M, Klepikov, N N, Andreev, S M, Sidorova, M V, Vafina, M G, Seniuta, N B, Pavlish, O A, Syrtsev, A V, Gurtsevich, V E
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01-07-1993
• Subjects: Amino Acid Sequence; B-Lymphocytes - immunology; Enzyme-Linked Immunosorbent Assay; HTLV-I Antibodies - immunology; Human T-lymphotropic virus 1 - immunology; Human T-lymphotropic virus 1 - metabolism; Humans; Immunodominant Epitopes - immunology; Molecular Sequence Data; Peptides - metabolism; Sequence Homology, Amino Acid; Viral Structural Proteins - immunology
• ISSN: 0026-8984

The immunoreactivity of 25 synthetic peptides corresponding to amino acid fragments of the HTLV-I structural proteins p19 gag, gp46 and gp21 env were studied in enzyme linked immunosorbent assay using a serum panel of 70 reference positive specimens with anti-HTLV-I antibodies. The location of the synthetic peptides containing the B-cell epitopes of HTLV-I was established. Anti-HTLV-I antibodies effectively recognized these peptides. The significance of some amino acids for forming the HTLV-I antigenic determinants was estimated. The synthetic peptides with amino acid sequences 100-130 p19 gag and 176-201 gp46 env were found to have most immunoreactivity (90-99% recognition by sera of HTLV-I infected patients) and mimic the immunodominant B-cell epitopes of HTLV-I structural proteins.