One chimeric peptide incorporating antigenic sequences from the gp41 transm
embrane region (peptide H-18) and the gp120 envelope region (peptide H-15)
corresponding to amino acids (587-617) on gp41 and (495-516) on gp120 of hu
man immunodeficiency virus (HIV 1) was synthesized. Both sequences were sep
arated by two glycine residues. This peptide was evaluated as antigen in an
ultramicro-enzyme-linked immunosorbent assay (UMELISA) with samples derive
d from HIV-1 (n = 30) with different titers of antibodies and healthy blood
donors (n = 30). The results were compared to plates coated with monomeric
peptides and to plates coated with two monomeric pep tides together. Resul
ts demonstrated that monomeric peptides gp41 (H-18) and gp120 (H-15) were g
ood as antigens with samples that present antibodies to these regions. The
chimeric peptide was the most antigenic. Those results may be related to th
e peptide structure, adsorption to the solid surface, and epitope accessibi
lity to the antibodies. This chimeric peptide would be very useful for HIV-
1 diagnostics. (C) 2000 Academic Press.