Immunological relationships among group I and group V allergens from grass pollen.
Specific IgE antibodies have been affinity-purified from recombinant grass pollen allergens, and used to identify isoforms of the two major allergens of rye-grass pollen, Lol p I and Lol p V and cross-reactive allergens in other grasses. Lol p I-specific IgE (affinity-purified from the recombinant protein expressed by clone 13R which encodes amino acids 96-240 of Lol p I) identified four isoforms of the allergen. The same probe recognized cross-reactive epitopes in pollen proteins from 14 out of 16 grasses. The allergens identified by Lol p V-specific IgE (affinity-purified from the recombinant protein expressed by clones 12R or 19R which encode the full Lol p V protein) varied more in their physicochemical characteristics than the Group I isoforms. At least eight isoforms of Lol p V were identified by the Lol p V-specific IgE. The same probe recognized cross-reactive epitopes in pollen protein from 13 out of 16 grasses. Group I proteins were identified in grasses from two sub-families of the Poaceae, while the Group V allergens were only identified in pollen of grasses from one sub-family, the Pooideae.
Smith
P M
PM
School of Botany, University of Melbourne, Parkville, Victoria, Australia.
Ong
E K
EK
Knox
R B
RB
Singh
M B
MB
D000485:Allergens / Q000145:classification* / Q000276:immunology*; D000918:Antibody Specificity; D052179:Antigens, Plant; D003429:Cross Reactions; D000939:Epitopes; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology; D008129:Lolium / Q000276:immunology*; D010940:Plant Proteins / Q000276:immunology; D006109:Poaceae / Q000276:immunology; D011058:Pollen / Q000276:immunology*; D011993:Recombinant Fusion Proteins / Q000276:immunology
D000485:Allergens; D052179:Antigens, Plant; D000939:Epitopes; C042814:Lol p I protein, Lolium perenne; C084941:Lol p V protein, Lolium perenne; D010940:Plant Proteins; D011993:Recombinant Fusion Proteins; D007073:Immunoglobulin E