The Antibody Response to the HIV-1 Specific "Out" (vpu) Protein: Identification of an Immunodominant Epitope and Correlation of Antibody Detectability to Clinical Stages

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Abstract
Overlapping decapeptides based on the sequences of two human immunodeficiency virus type 1 (HIV-1) strains (HXB2 and ELI) were used to identify an immunodominant epitope of the nonstructural protein "out" (vpu) of the human immunodeficiency virus type 1. Of 29 HIV-1 antibody-positive sera, 6 reacted with decapeptides corresponding to the C-terminal amino acid sequence VEMGVEMGHHAPWDVDDL of the "out" (vpu) protein. This oligopeptide was synthesized by the solid phase method and used to develop an enzyme-linked immunosorbent assay (ELISA) for screening of 243 HIV-1-seropositive and 75 HIV-1-seronegative sera. It was found that 26% of the HIV-1 antibody-positive sera were reactive in the "out" (vpu) peptide ELISA, whereas none of the HIV-1-negative sera reacted with the oligopeptide. Correlation of reactivity of sera with the Walter Reed (WR) staging classification demonstrated that individuals classified WR 1 (36%) and WR 2 (42%) were more often reactive than patients classified WR 3-6 (11%).