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Wrenger, S.; Hoffmann, T.; Faust, J.; Mrestani-Klaus, C.; Brandt, W.; Neubert, K.; Kraft, M.; Olek, S.; Frank, R.; Ansorge, S.; Reinhold, D.; The N-terminal Structure of HIV-1 Tat Is Required for Suppression of CD26-dependent T Cell Growth J. Biol. Chem. 272, 30283-30288, (1997) DOI: 10.1074/jbc.272.48.30283
Evidence exists that the human immunodeficiency virus-1 (HIV-1) transactivator Tat occurs extracellularly and is involved in the immunosuppression of non-HIV-1-infected T cells of acquired immunodeficiency syndrome (AIDS) patients. The mechanism of this immunosuppressive activity of Tat has been controversially discussed. Interestingly, Tat binds to the T cell activation marker CD26, which has been shown to play a key role in the regulation of growth of lymphocytes and to inhibit its dipeptidyl peptidase IV (DP IV) activity. Here we show that the N-terminal nonapeptide MDPVDPNIE of Tat is a competitive inhibitor of DP IV and suppresses DNA synthesis of tetanus toxoid-stimulated peripheral blood mononuclear cells. Amino acid exchanges at positions 5 and 6 strongly weaken these effects.1H nuclear magnetic resonance and molecular dynamics simulations of Tat(1–9), I5-Tat(1–9), and L6-Tat(1–9) suggest a similar backbone conformation for Tat(1–9) and L6-Tat(1–9). The solution conformation of I5-Tat(1–9) considerably differs from the other two. However, Tat(1–9) fits into our previously proposed active site model of DP IV in contrast to I5-Tat(1–9) and L6-Tat(1–9). Conformational alterations with regard to the parent peptide and spatial hindrances between these both compounds and DP IV can explain the loss of inhibitory activity. Our data suggest that the N-terminal residues of HIV-1 Tat do interact directly with the active site of DP IV and that DP IV does mediate Tat’s immunosuppressive effects.