IgE-binding proteins from pine (Pinus radiata D. Don) pollen: evidence for cross-reactivity with ryegrass (Lolium perenne).
A complex mixture of pine (Pinus radiata D. Don) pollen proteins are rapidly released into aqueous solutions. IgE-binding proteins have been identified in these extracts using combined SDS-PAGE immunoblotting techniques. These IgE-binding proteins were detected using atopic patient and commercial pooled human sera known to be high in ryegrass-specific IgE. Enzyme-immunoassay inhibition studies revealed that leached P. radiata pollen proteins could partially inhibit serum IgE binding to ryegrass RAST discs thus providing preliminary evidence for allergen cross-reactivity between these two unrelated species.
Cornford
C A
CA
Department of Botany and Zoology, Massey University, Palmerston North, New Zealand.
Fountain
D W
DW
Burr
R G
RG
D000943:Antigens, Differentiation / Q000378:metabolism*; D003429:Cross Reactions; D037502:Galectin 3; D006801:Humans; D015151:Immunoblotting; D066298:In Vitro Techniques; D008970:Molecular Weight; D010940:Plant Proteins / Q000276:immunology; D011058:Pollen / Q000276:immunology*; D012434:Secale / Q000276:immunology; D014197:Trees
D000943:Antigens, Differentiation; D037502:Galectin 3; D010940:Plant Proteins