Inventors at the National Institutes of Health have recently characterized and cloned both the yeast and human recombinant versions of the enzyme deoxyhypusine hydroxylase (DOHH) that catalyzes the final step in the modification of eIF5A.

Translation initiation factor eIF5A is a highly conserved eukaryotic protein. One of its lysine residues is enzymatically modified, using spermidine, to form an unusual amino acid, hypusine, a posttranslational modification unique to eIF-5A. This eukaryotic initiation factor (eIF5A) and its hypusine modification are essential for mammalian cell proliferation. Inventors at the National Institutes of Health have recently cloned and characterized the enzyme deoxyhypusine hydroxylase (DOHH) that catalyzes the final step in the modification of eIF5A. The inventors have characterized and cloned both the yeast and human recombinant versions of this enzyme. Studies have shown that metal chelating compounds like deferiprone and ciclopirox olamine that inhibit DOHH activity in cells also inhibit HIV-1 replication in cell culture. These findings suggest potential utility of DOHH as a novel target for anti-cancer and anti-retroviral therapy. These advances could also conceivably lead to the development of small molecule inhibitors that bind to specific sites in the enzyme.

U.S. Provisional Application No. 60/748,879 filed 09 Dec 2005 (HHS Reference No. E-051-2006/0-US-01) Inventors: Myung Hee Park et al. (NIDCR)

Licensees sought. In addition to licensing, the technology is available for further development through collaborative research opportunities with the inventors.