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Group V allergens in grass pollens. II. Investigation of group V allergens in pollens from 10 grasses
Author(s) -
MATTHIESEN F.,
LøWENSTEIN H.
Publication year - 1991
Publication title -
clinical and experimental allergy
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.462
H-Index - 154
eISSN - 1365-2222
pISSN - 0954-7894
DOI - 10.1111/j.1365-2222.1991.tb01662.x
Subject(s) - phleum , allergen , lolium perenne , immunoglobulin e , pollen , immunoelectrophoresis , group a , chemistry , allergy , antibody , immunology , biology , botany , poaceae , medicine
Summary In an earlier study an allergen from Phleum pratense (timothy) pollen. Phl p V. has been isolated and physicochemically characterized. In this study Phl p V and immunochemically simitar components from other grass pollens (group V allergens) have been investigated using immunoelectrophoretic techniques. To study the allergenic importance of the group V allergens, the allergenic compositions of 10 grass pollen extracts were investigated in crossed radioimmunoelectrophoresis (CRIE) using 20 sera from grass pollen‐allergic donors. Group V allergens were identified using monospecific rabbit antibodies raised against Phl p V, anti‐ phl p V, which react with other group V allergens usually producing dense precipitates in immunoelectrophoresis. In this way group V allergens were identified in eight extracts, and when present the precipitate corresponding to the group V allergen was the dominant IgE binding precipitate. All identified group V allergens bound IgE in at least 17 of the 20 investigated sera. Monospecific rabbit antibodies raised against the group I allergen of Lolium perenne (rye grass), anit‐Lol p I. do not precipitate group V allergens, indicating that there are no immunochemical similarities between group I and group V allergens. In SDS‐PAGE anti‐ Phl p V identifies IgE‐binding components with molecular weights between 26 and 33 kD. In contrast, anti‐Lol p I binds to components of slightly higher molecular weight. Apparently, the group V components are allergens that are physicochemically and immunochemically distinct from group I allergens.