Purification and characterization of a novel lectin with antiphytovirus activities from the wild mushroom Paxillus involutus

A novel lectin was isolated from the dried fruiting bodies of the wild mushroom paxillus involutus. isolation was conducted by anion exchange chromatography on deae-cellulose,q-sepharose and gel filtration on superdex 75 using a fast protein liquid chromatography (fplc) system. this lectin had a molecular mass of 28 kda and was composed of four identical subunits,each with a molecular mass of 7 kda. n-terminal amino acid sequence of the p. involutus lectin was determined to be ctcavflnnttvks,which showed a low level of similarity to mushroom lectin sequences reported previously. the biochemical properties of this lectin were determined,and the hemagglutinating activity was inhibited by inulin and o-nitrophenyl-β-d-galacto-pyranoside. additionally,ca2+,zn2+,cd2+,fe 2+,and al3+ inhibited its hemagglutinating activity,while cu2+ promoted this activity. this lectin exhibited poor thermostability and was sensitive to hcl,but it had a high tolerance to naoh exposure. in terms of biological properties,this lectin manifested antiphytovirus activity towards tobacco mosaic virus (tmv) with a 70.61% inhibition at a concentration of 200 μg/ml. this lectin was devoid of inhibitory activities toward pathogenic fungi and hiv-1 reverse transcriptase,and antiproliferative activities were observed in tumor cell lines including lung cancer a-549 and human colon cancer hct-8 cells. © 2013 bentham science publishers.