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High-Throughput Screening Method of Inhibitors that Block the Interaction between 2 Helical Regions of HIV-1 gp41

Division of Life Sciences, Korea Institute of Science and Technology, Seoul, Korea and School of Life Sciences and Biotechnology, Korea University, Seoul, Korea

Won-Kyu Lee

Division of Life Sciences, Korea Institute of Science and Technology, Seoul, Korea

Kwangseog Ahn

School of Life Sciences and Biotechnology, Korea University, Seoul, Korea

Myung Kyu Lee

Laboratory of Functional Proteomics, Korea Research Institute of Bioscience and Biotechnology, Taejon, Korea

Yeon Gyu Yu

Division of Life Sciences, Korea Institute of Science and Technology, Seoul, Korea

The HIV-1 envelope glycoprotein transmembrane subunit, gp41, mediates the fusion of viral and target cell membranes. The 2 helical regions in the ectodomain of gp41, the N-helix and the C-helix, form a helical bundle complex that has been suggested as a fusion-active conformation. Previously, an enzyme-linked immunosorbent assay (ELISA) method had been established to measure the interaction of 2 helical regions of gp41. In this study, the ELISA method was modified to apply high-throughput screening (HTS) of an organic compound library. A few compounds had been identified to prevent the interaction between 2 helical regions of gp41, and they were further shown to inhibit the gp41-mediated viral infection. In addition, they specifically quenched the fluorescence of tryptophan in the N-helix region, indicating that these compounds bound to the N-helix rather than the C-helix of gp41. These results suggested that this assay method targeting gp41 could be used for HTS of HIV fusion inhibitors. (Journal of Biomolecular Screening 2005:13-19)

Key Words: HIV-1 • gp41 • inhibitor • membrane fusion • screening

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