S. Vrtala et al., PROPERTIES OF TREE AND GRASS-POLLEN ALLERGENS - REINVESTIGATION OF THE LINKAGE BETWEEN SOLUBILITY AND ALLERGENICITY, International archives of allergy and immunology, 102(2), 1993, pp. 160-169
In this study we reinvestigated the kinetics of allergen release from
birch pollen (Betula verrucosa) and timothy grass pollen (Phleum prate
nse) using different protein extraction procedures, immunoblotting wit
h specific antibodies and immune electron microscopy. Pollen allergens
such as the major birch pollen allergen, Bet v I, the major timothy g
rass pollen allergens, Phl p I and Phl p V, group-II/III allergens fro
m timothy grass and profilins were released rapidly and in large amoun
ts from hydrated pollen. Within a few minutes pollen allergens could b
e detected in aqueous supernatants prepared from birch and grass polle
n with serum IgE or specific antibodies. In parallel the allergen cont
ent in the pollen pellet fractions decreased. A nonallergenic protein
such as heat shock protein 70 can be extracted in sufficient amounts o
nly with harsh extraction procedures. Immune electron microscopy of dr
y and rehydrated birch pollens showed that after short hydration, the
major birch pollen allergen, Bet v I, migrated into the exine and to t
he surface of intact pollen grains, whereas profilin, against which a
lower percentage of patients is sensitized, was retained in the pollen
grain. Comparing the amino acid composition and hydrophilicity of the
tested allergens with a nonallergenic protein such as heat shock prot
ein 70, no significant difference was noted. In agreement with earlier
observations we conclude that the allergenic properties of proteins a
re rather linked to the amount and speed of solubility from airborne p
articles than to intrinsic properties.