IgE-Binding Proteins from Pine (<i>Pinus radiata</i> D. Don) Pollen: Evidence for Cross-Reactivity with Ryegrass <i>(Lolium perenne)</i>

Abstract

A complex mixture of pine (Pinus radiata D. Don) pollen proteins are rapidly released into aqueous solutions. IgE-binding proteins have been identified in these extracts using combined SDS-PAGE immunoblotting techniques. These IgE-binding proteins were detected using atopic patient and commerical pooled human sera known to be high in ryegrass-specific IgE. Enzyme-immunoassay inhibition studies revealed that leached P. radiata pollen proteins could partially inhibit serum IgE binding to ryegrass RAST discs thus providing preliminary evidence for allergen cross-reactivity between these two unrelated species.

Patterns of pollen cross-allergenicity

“…Some rapidly eluted proteins from Monterey pine (Pinus radiata) are able to modestly inhibit solid phase perennial ryegrass (Lolium perenne) RAST discs. 14 While initially perplexing, this cross-reactivity, however modest, probably reflects panallergens such as the profilins.…”

Pinus pollen in the atmosphere of Vigo and its relationship to meteorological factors

“…The presence of allergenic proteins in pine pollen, and their possible cross-reactivity with Lolium perenne allergens, have been cited by Fountain and Cornford (1990) and Cornford et al (1990), who demonstrated a slower release of such proteins on the part of pine pollen grains. Recently, Pettyjhon and Levetin (1997) found that the quantity of protein in Pinus echinata pollen is higher than that of pollens such as Juniperus ashei, considered to be highly allergenic, linking the low allergenicity of Pinus to its high quantity of lipids and the slow release of allergens, since the quick release of allergens is a highly important factor in allergic reactions.…”

“…Despite its elevated pollen production, calculated to be between 20.9×10 6 and 32.3×10 6 pollen grains per tree for Pinus pinaster (Tormo et al 1996), and its anemophilous nature, it is not generally considered to be an important allergen. Different reasons are given to explain the causes of its scarce or null allergenicity: the large size of its pollen grains, which inhibits its penetration of the respiratory tract (Armentia et al 1990), its low protein content (Cornford et al 1990) or its hydrophobic nature due to its high lipid content (Harris and German 1985). However, pine pollen has been found in the respiratory tract: Dankaart et al (1991) highlighted its presence in the lower respiratory tract and Accorsi et al (1991) identified pine pollen in nasal and conjunctival secretions and, to a lesser degree, in the bronchi.…”

Urban green zones and related pollen allergy: A review. Some guidelines for designing spaces with low allergy impact

“…display cross-reactivity with ryegrass (Lolium perenne, Poaceae) proteins (Conford, Fountain, & Burr, 1990). A number of studies on grasses, which are species that produce pollen that is a major cause of allergies, have revealed strong cross-reactivity between members of a particular subfamily (Martin, Mansfield, & Nelson, 1985), as well as between members of different subfamilies (Smith, Xu, Swoboda, & Singh, 1997).…”