Purification and characterization of a novel anti-HSV-2 protein with antiproliferative and peroxidase activities from <italic>Stellaria media</italic>

Abstract

A novel antiviral protein, designated as Stellarmedin A, was purified from Stellaria media (L.) Vill. (Caryophyllaceae) by using ammonium sulfate precipitation, cation-exchange chromatography system. Gel electrophoresis analysis showed that Stellarmedin A is a highly basic glycoprotein with a molecular weight of 35.1 kDa and an isoelectric point of ∼8.7. The N-terminal 14-amino acid sequence, MGNTGVLTGERNDR, is similar to those of other plant peroxidases. This protein inhibited herpes simplex virus type 2 (HSV-2) replication in vitro with an IC50 of 13.18 µg/ml and a therapeutic index exceeding 75.9. It was demonstrated that Stellarmedin A affects the initial stage of HSV-2 infection and is able to inhibit the proliferation of promyelocytic leukemia HL-60 and colon carcinoma LoVo cells with an IC50 of 9.09 and 12.32 µM, respectively. Moreover, Stellarmedin A has a peroxidase activity of 36.6 µmol/min/mg protein, when guaiacol was used as substrate. To our knowledge, this is the first report about an anti-HSV-2 protein with antiproliferative and peroxidase activities from S. media.