Characterization of murine monoclonal antibodies to HIV-1 induced by synthetic peptides.

Abstract

We have used short synthetic peptides, 12 and 13 amino acids in length, conjugated to carrier proteins to develop monoclonal antibodies (MAb) to the envelope glycoprotein of 120 (kD) (gp120) and the 3' open reading frame protein (3-orf) of the human immunodeficiency virus type 1 (HIV-1). The peptides employed were chosen because of their strong hydrophilicity and in the case of the gp120 peptide because it represents a highly conserved hydrophilic region in the envelope protein. The MAb developed displayed appropriate specificities with their respective peptides and reacted with appropriate HIV-1 components (i.e., a 120 kD glycoprotein and a 27 kD protein, respectively) as determined by Western blot analysis. In indirect immunofluorescence assays the MAb strongly stained syncytia present in cultures of HTLV-3B-infected H9 cells. The MAb to the envelope component reacted with the RF isolate of HIV-1, as well as with the 3B isolate in immunofluorescence.