Abstract
Four allergenic proteins of Bahia (BA) grass pollen with estimated molecular weights of 45, 33, 31 and 28 kD were previously detected. Although all four proteins were reactive with BA grass allergic patient sera, the 33kD component was previously verified as a major allergen. The investigators report here for the first time, the similarities between the group I 33 kD allergen of BA grass, Pas n 1, and Group I allergen of Timothy grass, Phl p 1, using N-terminal amino acid sequencing and monoclonal antibodies, IG12 and BOT14, made to Timothy Phl p 1.
Highlights
Eleven groups of allergens have been previously identified and found in a number of different grass species [1,2]
Another study showed that IgE from grass pollen allergic patients cross-reacted extensively with various allergens from different grass species, but few of the sera reacted with the subtropical grass species, including BA [3]
We reported the separation of four allergenic proteins of BA pollen with estimated molecular weights of 45, 33, 31, and 28 kD by SDS-PAGE and showed these to be reactive with IgE in BA allergic patient sera [5]
Summary
Eleven groups of allergens have been previously identified and found in a number of different grass species [1,2]. Another study showed that IgE from grass pollen allergic patients cross-reacted extensively with various allergens from different grass species, but few of the sera reacted with the subtropical grass species, including BA [3]. We previously reported the purification of the BA 33 kD component using a combination of isoelectric focusing and continuous elution electrophoresis [7]. This component was reactive with IgE from pooled BA skin test positive patient antisera or the same antisera absorbed to remove asparagine-linked glycans [7]. Pas n 1 has not been previously sequenced nor has a comparison been made with the amino acid sequence
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