|Select ||PubMed ID ||Description |
Int Arch Allergy Appl Immunol. 1987;83(1):96-103.
Distribution of a major allergen of rye grass (Lolium perenne) pollen between
other grass species.
Standring R, Spackman V, Porter SJ.
Polyacrylamide gel electrophoresis in sodium dodecyl sulphate (SDS) followed by
protein staining has shown that extracts from 11 different grass pollens
contained proteins with similar molecular weights to that of the allergen R7 from
rye grass (Lolium perenne) pollen extract (i.e. 29,000-31,000 daltons). Western
blotting and detection with polyclonal (rabbit) antibodies raised against the
purified R7 (Rye I) allergen indicated that these proteins were antigenically
related and their allergenic properties were demonstrated by the binding of human
IgE to immunoblots. The distribution of cross-reacting antigenic determinants was
further investigated by immunoblotting with 2 mouse monoclonal antibodies, R7M1
and R7M2, produced with purified R7 as the initial immunogen. The 2 monoclonal
antibodies were shown to react with 'R7-like' components of grass pollen extracts
other than the component from rye grass. Differences in the distribution of R7M1
and R7M2 binding were found indicating that they are directed at separate R7
PMID: 2437060 [Indexed for MEDLINE]
Mol Immunol. 1989 Jun;26(6):557-61.
Isolation and characterization of a major cross-reactive grass group I allergenic
Esch RE(1), Klapper DG.
|2462587|| J Immunol. 1989 Jan 1;142(1):179-84.|
Identification and localization of allergenic determinants on grass group I
antigens using monoclonal antibodies.
Esch RE(1), Klapper DG.
|7930302|| J Allergy Clin Immunol. 1994 Oct;94(4):689-98.|
Complementary DNA cloning of the major allergen Phl p I from timothy grass
(Phleum pratense); recombinant Phl p I inhibits IgE binding to group I allergens
from eight different grass species.
Laffer S(1), Valenta R, Vrtala S, Susani M, van Ree R, Kraft D, Scheiner O,
|9500760|| J Allergy Clin Immunol. 1998 Feb;101(2 Pt 1):258-64.|
IgE antibodies to recombinant pollen allergens (Phl p 1, Phl p 2, Phl p 5, and
Bet v 2) account for a high percentage of grass pollen-specific IgE.
Niederberger V(1), Laffer S, Fröschl R, Kraft D, Rumpold H, Kapiotis S, Valenta
R, Spitzauer S.
|19895591|| Clin Exp Allergy. 2010 Mar;40(3):505-19. doi: 10.1111/j.1365-2222.2009.03380.x.|
Epub 2009 Nov 5.
Molecular variability of group 1 and 5 grass pollen allergens between Pooideae
species: implications for immunotherapy.
Chabre H(1), Gouyon B, Huet A, Baron-Bodo V, Nony E, Hrabina M, Fenaille F,
Lautrette A, Bonvalet M, Maillère B, Bordas-Le Floch V, Van Overtvelt L, Jain K,
Ezan E, Batard T, Moingeon P.