Par j 1 and Par j 2, the two major allergens in Parietaria judaica, bind preferentially to monoacylated negative lipids.

摘要: Par j 1 and Par j 2 proteins are the two major allergens in Parietaria judaica pollen, one of main causes allergic diseases Mediterranean area. Each them contains eight cysteine residues organized a pattern identical to that found plant nonspecific lipid transfer proteins. The 139- 102-residue recombinant allergens, corresponding respectively Par j 2, refold properly fully functional forms, whose immunological properties resemble those molecules purified from natural source. Molecular modeling shows that, despite lack extensive primary structure homology with proteins, both contain hydrophobic cavity suited accommodate ligand. In present study, we novel evidence for formation complexes these Parietaria pollen lipidic molecules. dissociation constant oleyl-lyso-phosphatidylcholine is 9.1 ± 1.2 μm Par j 1, whereas pyrenedodecanoic acid much higher affinity, approximately 1 μm as well mixture. Lipid binding does not alter secondary content protein but very efficient protecting disulfide bonds reduction by dithiothreitol. We show only bind lipids micellar dispersions, also able extract negative phospholipids bilayers.