Antibody-reactive peptide scanning (Pepscan) using overlapping nonapeptides and human sera as probes allows the identification of amino acids contributing significantly to antigen-antibody interaction. Five-hundred and two overlapping nonapeptides derived from the human immunodeficiency virus type 2 strain Rod (HIV-2) external envelope glycoprotein gp125 were synthesized to serve as probes for reactivity with eight sera of HIV-2-infected individuals. Fifteen antibody-binding regions were identified, among which two amino-terminal regions [E3, amino acids (aa) 118 to 132; E4, aa 125 to 141] and four carboxy-terminal regions (E11, aa 303 to 324; E12, aa 340 to 358; E14, aa 436 to 452; E15, aa 486 to 507) were the most antigenic. The amino acids in binding sites E3 and E4 were highly variable among simian immunodeficiency virus (SIV), HIV-2 and HIV-1. The antibody-binding domains E14 and E15 were highly conserved among HIV-2 strains (94% and 86% identity of HIV-2 to HIV-2 and HIV-2, respectively). Both domains had more amino acids in common with SIV (88% for E14, 64% for E15) than with HIV-1 (41% for E14, 45% for E15). Epidemiological studies revealed that the sera of African HIV-2-infected individuals bound the E11 and E15 peptides best (31%, 8/26). The sera of African HIV-1-infected individuals showed significant levels of cross-reactivity to the HIV-2 peptides, especially to the E15 peptide, whereas the sera of European HIV-1-infected individuals showed only moderate levels of cross-reactivity. If peptides covering the E15 epitope were used, African HIV-2-positive sera showed only a low level of cross-reactivity (4%) to E15 of HIV-1 and SIV. African HIV-1-positive sera bound the HIV-1 E15 peptide best (81%, 52/64), but showed high levels of cross-reactivity to SIV E15 (17%, 11/64) and HIV-2 E15 (25%, 16/64). European HIV-1-positive sera showed a high level of reactivity to HIV-1 E15 (91%, 50/55) and a low level of cross-reactivity to the HIV-2 (2%, 1/55), and none to the SIV E15 (0/55) peptide. These results indicate that the immunodominant regions of the HIV-2 external envelope (E11 and E15) align with the most immunodominant regions of HIV-1.


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