Smilaxin, a novel protein with immunostimulatory, antiproliferative, and HIV-1-reverse transcriptase inhibitory activities from fresh Smilax glabra rhizomes

A protein, with a novel N-terminal amino acid sequence and a molecular mass of 30 kDa, was purified from fresh Smilax glabra rhizomes by adsorption on DEAE-cellulose, CM-cellulose, Con A-Sepharose, and Mono S, and by fast protein liquid chromatography-gel filtration on Superdex 75. The protein, designated as smilaxin, stimulated uptake of [methyl-H-3]thymidine by murine splenocytes, peritoneal macrophages, and bone marrow cells, and production of nitric oxide by peritoneal macrophages. It inhibited uptake of [methyl-H-3]thymidine by MBL2 and PU5 tumor cells but not uptake by S180 and L1210 cells. Smilaxin augmented glucose uptake into rat adipose tissue. It attenuated the activity of HIV-1-reverse transcriptase with an IC50 of 5.6 mu M. However, it did not display hemagglutinating, antifungal or translation-inhibitory activities, indicating that it is not a lectin, an antifungal protein, or a ribosome-inactivating protein. (c) 2005 Elsevier Inc. All rights reserved.