Rapidly released allergens from short ragweed pollen *1, *2I. Kinetics of release of known allergens in relation to biologic activity

Marsh, David G.; Belin, Lars; Bruce, C.Allen; Lichtenstein, Lawrence M.; Hussain, Rabia

doi:10.1016/0091-6749(81)90063-4

Cited by 42 publications

(13 citation statements)

References 36 publications

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“…in the present study, however, we did not observe any loss in the IgE binding activity of the released allergens even after a prolonged extraction period of 20 h. In contrast to the above reports, the optimal time of extraction of Alternaría aller gens, however, varied for individual allergens and no single best time of extraction for all allergens could be determined [25]. Unlike timothy [23] and ragweed pollen allergens [2,5] where the basic proteins were extracted more rapidly than the acidic ones, no significant differences were observ ed between protein/allergen profile of the 10-second and 20-hour extracts of Parthenium pollen.…”

Section: Discussioncontrasting

confidence: 53%

Immunochemical Characterization of Rapid and Slowly Released Allergens from the Pollen of <i>Parthenium hysterophorus</i>

Gupta¹,

Sriramarao²,

Kori³

et al. 1995

Int Arch Allergy Immunol

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Allergens from the pollen of Parthenium hysterophorus (American feverfew), responsible for high incidence of allergic rhinitis, were found by immunoprint analysis to be localized on the surface of the pollen grains. The allergens were released very rapidly when extracted in vitro. The allergenic activity of the rapid (10 s) and slowly (20 h) released pollen proteins was comparable by in vivo skin test and ELISA inhibition assay. The isoelectric focusing patterns of the rapid and slowly released proteins were also identical. SDS-PAGE and Western blot analysis revealed that all the major pollen allergens with molecular weight 14, 28, 31, 37 and 45 kDa were eluted within 10 s of extraction. Periodate-Schiff staining showed that the 28,31 and 45 kDa components of the pollen extract are glycoproteins. The pollen allergens released after different periods of extraction lost 75% of IgE binding activity when subjected to in situ sodium m-periodate oxidation under controlled conditions, while 80% of the allergenic activity was still retained after extensive proteolysis. Our results support the clinical observation of a rapid onset of symptoms of allergic rhinitis in patients sensitive to Parthenium pollen, mediated predominantly by glycoproteins.

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Section: Discussioncontrasting

confidence: 53%

Immunochemical Characterization of Rapid and Slowly Released Allergens from the Pollen of <i>Parthenium hysterophorus</i>

Gupta¹,

Sriramarao²,

Kori³

et al. 1995

Int Arch Allergy Immunol

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“…In our experiments we found that the basic allergens were extracted more rapidly than the acidic ones. Similar results have also been obtained in the extraction of allergens from short ragweed pollen [36,37]. The quickly released, basic components contributed to a major portion of the biological activity of long-term ragweed extracts.…”

Section: Extraction and Characterization Of The Allergen Extractssupporting

confidence: 70%

Glycoprotein Allergens in Pollen of Timothy

Haavik

Paulsen

Wold

1985

Int Arch Allergy Immunol

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On extraction of timothy pollen with aqueous buffer high molecular weight material (MW > 3,500) containing the sugars arabinose, fucose, xylose, mannose, galactose and glucose was rapidly released. When the allergen extract was subjected to crossed immunoaffinoelectrophoresis with lectins incorporated in the first- or second-dimension gel, some allergens were clearly retarded. A basic glycoprotein allergen, probably the one known as antigen 30, was bound to concanavalin A (Con A) and also to a lectin from Pisum sativum. This allergen was purified by a combination of Con A-Sepharose and CM-Sephadex chromatography, giving a product that contained the following sugars: arabinose (1.4%), fucose (traces), xylose (1.3%), mannose (2.0%), galactose (7.6%) and glucose (10.5%). The purified allergen appeared essentially homogeneous on isoelectric focusing and on gel permeation chromatography. The allergenic activity and acid phosphatase activity, which have been correlated by previous workers, were demonstrated to be entirely separable.

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“…The use of NaCl ⁄ P i , a buffer with a physiological pH and ionic strength, allowed a fast release of BP14. Several studies have reported differences in time release of allergens from various pollen grains [19][20][21]. The allergenicity of pollen proteins, in terms of both challenge and sensitization, has been partly suggested to be related to the speed of release from the pollen grain [22][23][24].…”

Section: Discussionmentioning

confidence: 99%

Differential IgE sensitization to cypress pollen associated to a basic allergen of 14 kDa

et al. 2012

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The common cypress (Cupressus sempervirens) (Cups) pollen represents the first cause of respiratory allergies in the Mediterranean basin. The aim of this study was to characterize a novel 14-kDa cypress pollen allergen (BP14) allowing a clear dissociation of IgE sensitization patterns among allergic patients. The biochemical and immunochemical characterization of BP14 included determination of its isoelectric point, molecular mass, extraction kinetics, IgE binding prevalence, the presence of bromelain-type cross-reactive carbohydrate determinant and its IgE reactivity under reducing conditions. The presence of potential cross-reactive homologues in closely related cypress species, i.e. Cupressus arizonica (Cupa) and Cryptomeria japonica (Cryj), as well as in several taxonomically unrelated species was also investigated. According to our results, BP14 is easily and quickly solubilized in phosphate-buffered saline and exhibits several allergenic isoforms covering a broad range of pI (6.5-10.5). This allergen displays heat-stable conformational epitopes and does not include cross-reactive carbohydrate determinants, in contrast to high molecular weight cypress allergens. BP14 is expressed at higher levels in Cups than in Cupa and Cryj. No IgE cross-reactivity was found between the 14-kDa Cups pollen protein and proteins from some other non-Cupressaceae pollen allergenic sources such as orchard, timothy, wheat, maize, birch, ash and pine. Thus, IgE reactivity to BP14 is specific to Cupressaceae and discriminates two groups of patients allergic to cypress pollen. It might correspond to a relevant marker in relation to the sensitization process and ⁄ or the symptoms observed in some cypress-pollen-allergic patients. Furthermore, the description of BP14 should improve the diagnosis of cypress pollinosis.Abbreviations AB, ammonium bicarbonate buffer; BP14, basic protein of 14 kDa relative mass; CCD, cross-reactive carbohydrate determinant; Cryj,

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Rapidly released allergens from short ragweed pollen 1, 2I. Kinetics of release of known allergens in relation to biologic activity

Cited by 42 publications

References 36 publications

Immunochemical Characterization of Rapid and Slowly Released Allergens from the Pollen of <i>Parthenium hysterophorus</i>

Immunochemical Characterization of Rapid and Slowly Released Allergens from the Pollen of <i>Parthenium hysterophorus</i>

Glycoprotein Allergens in Pollen of Timothy

Differential IgE sensitization to cypress pollen associated to a basic allergen of 14 kDa

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