RESUMEN
The ability of the salivary protein, secretory leukocyte protease inhibitor (SLPI), to inhibit human immunodeficiency virus-1 (HIV-1) infection in vitro has been reported previously and has led to the suggestion that SLPI may be partially responsible for the low oral transmission rate of HIV-1. However, results contradictory to these findings have also been published. These discrepancies can be attributed to a number of factors ranging from the variability of macrophage susceptibility to HIV infection to the quality of commercially available preparations of SLPI. To resolve these differences and to study further the potential anti-HIV-1 activity of SLPI, the purified and re-folded protein, expressed from a synthetic gene, was examined using human monocytic THP-1 cells. This newly cloned SLPI reduced HIV-1(Ba-L) infection in differentiated THP-1 cells, in contrast to the results observed when using commercially available preparations of SLPI. Interestingly, while the two proteins displayed different anti-HIV effects they had comparable anti-protease activity. The identification of the THP-1 cell line as a system that supports HIV replication, which can be inhibited by a preparation of SLPI now available in large quantities, sets the stage for a thorough investigation of the molecular and structural basis for the anti-HIV activity of SLPI.