Chimeric synthetic peptides from the envelope (gp46) and the transmembrane(gp21) glycoproteins for the detection of antibodies to human T-Cell leukemia virus type II

Citation
Mh. Marin et al., Chimeric synthetic peptides from the envelope (gp46) and the transmembrane(gp21) glycoproteins for the detection of antibodies to human T-Cell leukemia virus type II, BIOC BIOP R, 289(1), 2001, pp. 7-12
Citations number
28
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN journal
0006291X → ACNP
Volume
289
Issue
1
Year of publication
2001
Pages
7 - 12
Database
ISI
SICI code
0006-291X(20011123)289:1<7:CSPFTE>2.0.ZU;2-2
Abstract
Two chimeric synthetic peptides incorporating immunodominant sequences from HTLV-II virus were synthesized. Monomeric peptides P2 and P3 represent seq uences from transmembrane protein (gp21) and envelope protein (gp46) of the virus. The peptide P2 is a gp21 (370-396) sequence and the peptide P3 is a gp46 (178-205) sequence. Those peptides were arranged in a way that permit s one to obtain different combinations of chimeric peptides (P2-GG-P3 and P 3-GG-P2), separated by two glycine residues as spacer arms. The antigenic a ctivity of these peptides was evaluated by UltramicroEnzyme-linked immunoso rbent assay (UMELISA) by using panels anti-HTLV-II-positive sera (n = 11), anti-HTLV-I/II-positive sera (n = 2), HTLV-positive (untypeable) serum samp les (n = 2), and anti-HTLV-1-positive sera (n = 22), while specificity was evaluated with anti-HIV-positive samples (n = 19) and samples from healthy blood donors (n = 30). The efficacy of the chimeric peptides in solid-phase immunoassays was compared with the monomeric peptides and a mixture of the monomeric peptides. Higher sensitivity was observed for chimeric peptide Q 5 assay. Those results may be related to a higher peptide adsorption capaci ty to the solid surface and for epitope accessibility to the antibodies. Th is chimeric peptide would be very useful for HTLV-II diagnostic. (C) 2001 A cademic Press.