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parietaria judaica/sisteina
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Assignment of disulphide bridges in Par j 2.0101, a major allergen of Parietaria judaica pollen.
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Par j 2.0101, a major allergen of the Parietaria judaica pollen, was expressed in E. coli, purified to homogeneity and fully characterised both at the structural and the functional level. The recombinant rPar j 2.0101 protein showed an allergenic activity in histamine release, skin prick tests and
Par j 1 and Par j 2, the two major allergens in Parietaria judaica, bind preferentially to monoacylated negative lipids.
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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
Par j 1 and Par j 2, the major allergens from Parietaria judaica pollen, have similar immunoglobulin E epitopes.
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BACKGROUND
Parietaria judaica is the main cause of allergy in Mediterranean countries. The major allergens from P. judaica pollen, Par j 1 and Par j 2, have amino acid sequence identity of 45% and contain eight cysteine residues involved in disulphide bonds that compact the structure.
OBJECTIVE
The
Detection and localisation of disulphide bonds in a synthetic peptide reproducing the sequence 1-30 of Par j 1.0101 by electrospray ionisation mass spectrometry.
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The structural characterisation of a synthetic peptide reproducing the sequence 1-30 of Par j 1.0101, a major allergenic protein present in the pollen of Parietaria judaica, by combined use of chemical and enzymatic cleavage, reversed-phase high-performance liquid chromatography and electrospray
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