Abstract
The binding of the synthetic fragment from the CD4 binding site of HIV (gp 120) with polymorphonuclear neutrophils (PMN) in 13 healthy donors and 31 HIV-infected patients was studied using a biotin-streptavidin-texas-red complex. The largest percentage of PMN-bound peptide was reached at a final peptide concentration of 10 micrograms/ml. The increase of peptide concentration did not raise the per cent of positive PMN. Preliminary incubation of PMN or mononuclear cells with non-biotinylated peptide abolished subsequent binding of these cells with biotinylated peptide, while preliminary treatment of the cells by anti-CD4 monoclonal antibody did not lead to such abrogation. It was revealed that about 14% of PMN but no lymphocytes from healthy donors were able to bind peptide. The number of such PMN in HIV-infected patients was significantly less (6.3 +/- 8.9%, P less than 0.05). A connection between peptide-bound PMN and their functional activity was found. The percentage of such cells was 13.0 +/- 11.5% in patients with normal values in a stimulated nitroblue tetrazolium reduction test and only 2.6 +/- 2.8% in patients with low values in this test (P less than 0.05).
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