ABSTRACT
A monomeric glycoprotein with a molecular mass of 28 kDa in SDS-PAGE was isolated from the Withania somnifera root tubers. The protein designated WSG (Withania somnifera glycoprotein) demonstrated potent antimicrobial activity against the phytopathogenic fungi and bacteria tested. Antifungal effect has been demonstrated in that WSG exerts a fungistastic effect by inhibiting spore germination and hyphal growth in the tested fungi. WSG showed potent antifungal activity against Aspergillus flavus, Fusarium oxysporum, F. verticilloides and antibacterial activity against Clvibacter michiganensis subsp. michiganensis. WSG is an acidic, non-toxic (trypsin-chymotrypsin) protease inhibitor. These results encourage further studies of WSG as a potential therapeutic agent for its antifungal activity.
Subject(s)
Anti-Bacterial Agents/pharmacology , Antifungal Agents/pharmacology , Bacteria/drug effects , Fungi/drug effects , Glycoproteins/pharmacology , Withania/chemistry , Animals , Anti-Bacterial Agents/isolation & purification , Antifungal Agents/isolation & purification , Erythrocytes/drug effects , Glycoproteins/isolation & purification , Glycoproteins/metabolism , Hemolysis/drug effects , Humans , Mice , NIH 3T3 Cells , Plant Proteins/isolation & purification , Plant Proteins/metabolism , Plant Proteins/pharmacology , Withania/physiologyABSTRACT
Three acidic phospholipases A2 from Indian cobra (Naja naja naja) venom inhibited platelet aggregation in platelet rich plasma induced separately by ADP, collagen and epinephrine with different potencies. The order of inhibition was epinephrine > collagen > ADP. They did not inhibit platelet aggregation induced by arachidonic acid (10 microM). The inhibition was dependent on concentration of the protein and the time of incubation of the phospholipases A2 with platelet rich plasma. Parabromophenacyl bromide modified PLA2 enzymes lost their enzymatic activity as well as platelet aggregation inhibition activity suggesting the involvement of catalytic function in platelet aggregation inhibitory activity.
