A new method for determining the distribution of allergenic fractions in biological materials: Its application to grass pollen extracts

Marsh, David G.; Haddad, Zack H.; Campbell, Dan H.

doi:10.1016/0021-8707(70)90078-x

Cited by 75 publications

(29 citation statements)

References 18 publications

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“…Nevertheless, similarily reduced RAST inhibitory activity was apparent with authentic Rye groups I, II and III, obtained from the Bureau of Biologics. The poor skin-test response of two individuals to R14a (Table 3) could be explained by variations in the response of humans to individual allergenic components in rye-grass pollen and accords with the findings of Marsh et al (1970), who showed that only 70% of grass-pollen-sensitive individuals responded to rye group II (Rl4a).…”

Section: Results and Discussion Physical And Chemical Characterizatiosupporting

confidence: 72%

Physicochemical and immunochemical characterization of allergenic proteins from rye-grass (Lolium perenne) pollen prepared by a rapid and efficient purification method

Cottam¹,

Moran²,

Standring³

1986

Biochemical Journal

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Three fractions of rye-grass (Lolium perenne) pollen extract have been isolated by preparative isoelectric focusing (i.e.f.) and characterized in terms of physicochemical and immunochemical properties. The purified components were designated 'R7' and 'R14' on the basis of their positions in relation to other rye-grass pollen extract components on SDS/polyacrylamide-gel electrophoresis and their apparent molecular masses were assessed as 31 and 11 kDa respectively. On i.e.f., R14 split into two components, one acidic (pl 5.0) and one basic (pl 9.0), termed 'Rl4a' and 'Rl4b' respectively, and R7 focused at pl 5.8. R7 and R14a were shown to be allergenic by skin-prick test and all three components were recognized by rye-grass-pollen-specific human IgE. On SDS/polyacrylamide-gel electrophoresis and i.e.f., R7 behaved in a manner identical with that shown by an authentic sample of Rye I and gave an amino acid analysis similar to published data Immunochemistry 3, 91-100] for Rye group-I isoallergens; the amino acid sequence of the first 27 N-terminal amino acids was also determined. Physicochemical analysis revealed that R14a was equivalent to Rye II and 14b to Rye III. Preparative i.e.f. followed by gel-permeation chromatography proved to be a rapid and efficient method for purifying the allergenic components of Rye I (R7), Rye II (Rl4a) and Rye III (Rl4b) from rye-grass pollen extract.

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Section: Results and Discussion Physical And Chemical Characterizatiosupporting

confidence: 72%

Physicochemical and immunochemical characterization of allergenic proteins from rye-grass (Lolium perenne) pollen prepared by a rapid and efficient purification method

Cottam¹,

Moran²,

Standring³

1986

Biochemical Journal

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“…In addition, to elucidate mechanisms of SIT, we tested BGP-sensitive patients before and after standard immunotherapy using a tailored depot preparation containing 50% BGP and 50% 7-grass mix. This preparation was used since there is minimal cross-reactivity between pollen of grasses of the Pooideae subfamily and BGP [11, 12, 13, 14]. Therefore, the standard 7-grass mix extract (rye, cocksfoot, bent, Kentucky blue, sweet vernal, timothy and meadow fescue), frequently used for immunotherapy of grass pollen allergy, is unlikely to relieve symptoms due to BGP sensitisation.…”

Section: Introductionmentioning

confidence: 99%

Oligoclonal Analysis of the Atopic T Cell Response to the Group 1 Allergen of <i>Cynodon dactylon</i> (Bermuda Grass) Pollen: Pre- and Post-Allergen-Specific Immunotherapy

Eusebius

Papalia

Suphioglu

et al. 2002

Int Arch Allergy Immunol

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Background: Bermuda grass pollen (BGP) is an increasingly important seasonal aeroallergen in Australia and other subtropical and temperate regions. BGP shares minimal allergenic cross-reactivity with pollens of rye grass or other Pooideae grasses often used for desensitization regimens in grass pollen allergy. Current allergen immunotherapy is seldom used in asthmatic patients due to IgE-mediated side effects. Since clinically effective immunotherapy is linked with altered allergen-specific T cell response, characterisation of human T cell reactivity to Cyn d 1, the major B cell allergen of BGP, should permit the design of effective and safe immunotherapy for BGP allergy. Methods: Short-term BGP-specific CD4+ T cell lines were established from peripheral blood of 14 BGP-sensitive patients before and after conventional 50% BGP and 50% 7-grass mix subcutaneous specific allergen immunotherapy (SIT). T cell diversity of antigen specificity and function was assessed by proliferation and cytokine production to BGP, Cyn d 1 and Cyn d 1 peptides. Results: Three highly immunogenic regions of Cyn d 1 were identified in 13/14 patients pre-SIT: Cyn d 1 (109–128), (181–209) and (217–241). The SIT regimen was clinically efficacious. Following SIT, decreased proliferation to BGP, Cyn d 1 and Cyn d 1 peptides was observed with a marked decrease in the IL-5:IFN-γ ratio. Conclusions: Cyn d 1 is a major T cell allergen of BGP. Decreased Cyn d 1-specific IL-5 dominant T cell responses were observed in association with clinically effective treatment with the 50% BGP and 50% 7-grass mix. Identified dominant T cell regions of Cyn d 1 should facilitate safer vaccine development for BGP-induced asthma in addition to rhinitis.

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“…As a result, differences in the immunological reactivity of the allergens of Bermuda grass compared to other grasses have been noted in a number of The nucleotide and amino acid sequences of Cyn d 7 have been submitted to the EMBL and Genbank databases under the accession numbers X91256 and U35683, respectively. studies [3][4][5]. Moreover, individuals allergic to Bermuda grass require separate diagnosis and treatment [6].…”

Section: Introductionmentioning

confidence: 99%

Molecular cloning and immunological characterisation of Cyn d 7, a novel calcium‐binding allergen from Bermuda grass pollen¹

Suphioglu¹,

Ferreira²,

Knox³

1997

FEBS Letters

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A new method for determining the distribution of allergenic fractions in biological materials: Its application to grass pollen extracts

Cited by 75 publications

References 18 publications

Physicochemical and immunochemical characterization of allergenic proteins from rye-grass (Lolium perenne) pollen prepared by a rapid and efficient purification method

Physicochemical and immunochemical characterization of allergenic proteins from rye-grass (Lolium perenne) pollen prepared by a rapid and efficient purification method

Oligoclonal Analysis of the Atopic T Cell Response to the Group 1 Allergen of <i>Cynodon dactylon</i> (Bermuda Grass) Pollen: Pre- and Post-Allergen-Specific Immunotherapy

Molecular cloning and immunological characterisation of Cyn d 7, a novel calcium‐binding allergen from Bermuda grass pollen¹

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A new method for determining the distribution of allergenic fractions in biological materials: Its application to grass pollen extracts

Cited by 75 publications

References 18 publications

Physicochemical and immunochemical characterization of allergenic proteins from rye-grass (Lolium perenne) pollen prepared by a rapid and efficient purification method

Physicochemical and immunochemical characterization of allergenic proteins from rye-grass (Lolium perenne) pollen prepared by a rapid and efficient purification method

Oligoclonal Analysis of the Atopic T Cell Response to the Group 1 Allergen of <i>Cynodon dactylon</i> (Bermuda Grass) Pollen: Pre- and Post-Allergen-Specific Immunotherapy

Molecular cloning and immunological characterisation of Cyn d 7, a novel calcium‐binding allergen from Bermuda grass pollen1

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Molecular cloning and immunological characterisation of Cyn d 7, a novel calcium‐binding allergen from Bermuda grass pollen¹