tailieunhanh - Báo cáo khoa học: Par j 1 and Par j 2, the two major allergens in Parietaria judaica, bind preferentially to monoacylated negative lipids

Par j 1 and Par j 2 proteins are the two major allergens inParietaria juda-ica pollen, one of the main causes of allergic diseases in the Mediterranean area. Each of them contains eight cysteine residues organized in a pattern identical to that found in plant nonspecific lipid transfer proteins. | ễFEBS Journal Par j 1 and Par j 2 the two major allergens in Parietaria judaica bind preferentially to monoacylated negative lipids Roberto Gonzalez-Rioja1 Juan A. Asturias1 Alberto Martinez1 Felix M. Gobi2 3 and Ana Rosa Viguera2 1 Research and Development Department Bial-Aristegui Bilbao Spain 2 Unidad de Biofisica CSIC-UPV EHU Leioa Spain 3 Departamento de Bioquimica Universidad delPais Vasco Leioa Spain Keywords cavity volume CD lipid binding lipid transfer proteins pyrene fluorescence Correspondence A. R. Viguera Unidad de Biofisica CSIC-UPV EHU Barrio Sarriena s n 48940 Leioa Spain Fax 34 946 01 3360 Tel 34 946 01 3191 E-mail gbbviria@ Received 5 November 2008 revised 5 January 2009 accepted 19 January 2009 doi Par j 1 and Par j 2 proteins are the two major allergens in Parietaria judaica pollen one of the main causes of allergic diseases in the Mediterranean area. Each of them contains eight cysteine residues organized in a pattern identical to that found in plant nonspecific lipid transfer proteins. The 139- and 102-residue recombinant allergens corresponding respectively to Par j 1 and Par j 2 refold properly to fully functional forms whose immunological properties resemble those of the molecules purified from the natural source. Molecular modeling shows that despite the lack of extensive primary structure homology with nonspecific lipid transfer proteins both allergens contain a hydrophobic cavity suited to accommodate a lipid ligand. In the present study we present novel evidence for the formation of complexes of these natural and recombinant proteins from Parietaria pollen with lipidic molecules. The dissociation constant of oleyl-lyso-phos-phatidylcholine is pM for recombinant Par j 1 whereas pyrene-dodecanoic acid shows a much higher affinity with a dissociation constant of approximately 1 M for both recombinant proteins as well as for the natural mixture. Lipid binding does not alter the secondary .

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