Serpin A1 (alpha1-proteinase inhibitor) inhibits human immunodeficiency virus 1 (HIV-1) production by mechanisms which remain to be elucidated. The complex formation of serpin A1 with proteinases eliminates the proteolytic activity and generates a fragment corresponding to the serpin C-terminal 36-residue peptide. Here, we show that the C-terminal 26-residue peptide of serpin A1 (A1-C26) inhibits HIV-long terminal repeat (LTR)-driven transcription in epithelial cells transfected with HIV-1 LTR promoter-driven genes. A1-C26 increased STAT1 phosphorylation and strongly reduced viral expression in a monocytic cell line infected with HIV-1 NL4-3. This reduction of expression was also observed in HIV-1 infected, PHA-activated peripheral blood mononuclear cells. In HIV-1 infected cells, the inhibitory activity of HIV-1 caused by B9-C23 and C1-C26, the A1-C26 homologues corresponding to the C-terminal sections of serpin B9 and serpin C1, was much lower than that obtained with A1-C26. These serpin peptides represent a novel class of antiviral agents.
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