Possible role of the plasminogen receptor as a site of interaction of the human immunodeficiency virus p24 immunosuppressive heptapeptide Ch7 with the host immune system.

Previous work from our laboratory demonstrated that a synthetic heptapeptide (Ch7: RGSDIAG), corresponding to a conserved sequence of human immunodeficiency virus (HIV) core protein p24 (amino acids 232- 238), was able to specifically abrogate antigen-induced responses in cultures of normal human peripheral blood mononuclear cells (PBMC), probably acting at the level of monocytes. The Ch7 peptide displays sequence homology to human plasminogen. In the present report we show that a compound (6-aminoexanoic acid), known to prevent plasminogen binding to monocyte-like cells, greatly reduced the immunosuppressive capacity of Ch7. We suggest that the plasminogen receptor may represent a target structure on human monocytes for the immunosuppressive p24 sequence.