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At least 19 recordsLinked to original sources
PubMed1992

Monoclonal antibodies against Olea europaea major allergen: allergenic activity of affinity-purified allergen and depleted extract and development of a radioimmunoassay for the quantitation of the allergen.

Several monoclonal antibodies (MAbs) were raised against Olea europaea pollen-extract components. Two of these antibodies, named OL 2 and OL 7, recognize two nonoverlapping, nonrepeating epitopes on the olive-allergen Ole e I, as demonstrated by different techniques. The allergen was purified in a single step by MAb-based affinity chromatography, and the allergen revealed a band at molecular weight 20 kd as well as a minor band at 18 kd on sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The contribution of allergen Ole e I to the allergenic activity of O. europaea pollen extracts was determined from the effect of allergen depletion by affinity chromatography on skin reactivity and a histamine-release test. The removal of allergen caused a large reduction in the activity of the preparation in 25 monospecific olive-allergic patients. In agreement, the affinity-purified allergen demonstrated a similar response when it was compared with the whole extract in these assays. The results indicated that Ole e I is by far the most important olive-pollen allergen. A two-site solid-phase radioimmunoassay was developed for the quantitation of the allergen Ole e I in mass units. The assay was based on the MAbs, OL 2 and OL 7, and had a detection limit in the nanogram range. A good correlation was found between allergenic activity, as determined by RAST inhibition, and allergen content in 18 olive-pollen extracts. This result indicates that the assay can be a good alternative to RAST inhibition for the standardization of O. europaea extracts.

Allergens↗
PubMed1977

Allergenic structure of allergen M from cod. II. Allergenicity of the limited tryptic hydrolysis peptides of fragment TM 2.

The peptides P1B3 (amino acid residues No. 88-113) and LT3N1 (residues No. 88-108), obtained from the limited tryptic hydrolysis of fragment TM 2 from codfish allergen M inhibited the interaction between allergen M and reaginic IgE antibodies both in vitro (87 and 62% RAST inhibition, respectively) and in vivo (total PK test inhibition). The peptide A7B1 (residues No. 97-113) overlapping the former at the COOH-terminus, was inactive in PK test inhibition experiments and produced only a minor inhibition of RAST (15%). The findings suggest that the nonapeptide residue No. 88-96 is partially indispensible for the allergenic activity of fragment TM 2, and is likely to incorporate allergenic determinant(s).

Allergens↗
PubMed1978

Effect of reagins and allergen extracts on radioallergosorbent assays for mite allergen.

The reproducibility of the radioallergosorbent (RAST) inhibition and direct binding assys with mite allergen were investigated in the presence of heterogeneous extracts and non-mite-sensitive atopic sera. Both contain components similar to potential contaminants which would occur in the assay of mite allergen and dust allergen and dust allergen extracts. The standardized inhibition and direct binding assays employed had a day to day (n = 4) coefficient of variation [(s.d. x 100)/mean] of 15% and 24% respectively. The inhibition assay for mite allergen was reproducible in the presence of protein concentrations of added plant, fungal, arthropod and animal extracts in excess of the protein concentrations that occur under the operational mite assay conditions. The mite inhibition assay was also reproducible in the presence of non-mite allergen extracts, with and without additional sera containing IgE specific for the non-mite allergens. The binding of a additional sera containing IgE specific for the non-mite allergens. The binding of a constant quantity of mite allergen to the activated solid phase in the direct binding assay was reproducible in the presence of added bovine serum albumin, and of a fungal or arthropod extract, representing the heterogeneous components of an allergen extract at the concentrations of total protein known to occur in the direct binding assay of mite extracts.

Allergens↗
PubMed1977

Allergens in bee venom II. Two new high molecular weight allergenic specificities.

Two new allergenic specificites were detected in honeybee venom and the two corresponding protein substances isolated by gel filtration, immunoadsorption, and ion exchange chromatography. The first of these, allergen B, has a molecular weight ranging from 49,000 to more than 200,00 d and can be recognized by rabbit and guinea pig antisera as well as by human reaginic sera using the radioallergosorbent test (RAST). Allergen B gives a single line in immunodiffusion distinct from hyaluronidase, phospholipase A, melittin, and the other high molecular weight substances described and gives a single band at 49,000 d in sodium dodecyl sulfate (SDS) polyacrylamide gel. The second substance, allergen C, has a molecular weight of 105,000 d and was separated from allergen B by immunoadsorption with insoluble antibody. Allergen C was shown to be distinct from the other sustances in bee venom by immunodiffusion with animal antisera. One human reaginic serum was monospecific for allergen C. Two other minor components of 86,000 and 71,000 d are present in bee venom; their allergenic activities are unknown. The two specifities, B and C, comprise most of the reactivity of the previously described Sephadex G-75 fraction 1 and clearly are important allergens, reacting with 98% of sera from bee venom-allergic individuals.

Allergens↗
PubMed1978

Suppression of reaginic antibodies with modified allergens. I. Reduction in allergenicity of protein allergens by conjugation to polyethylene glycol.

The conjugates of ovalbumin (OA) and of the nondialysable constitutents of the aqueous extract of ragweed pollen (RAG) with polyethylene glycols of molecular weights of 6,000 or 20,000 (PEG6 or PEG20) were shown to be nonantigenic, nonallergenic and nonimmunogenic. Thus, the i.v. administration of OA-PEG and RAG-PEG conjugates into mice did not elicit antibodies to OA and RAG, respectively, and these conjugates were shown to suppress in an immunologically specific manner the capacity of these animals to mount primary as well as secondary IgE responses to sensitizing doses of dinitrophenylated OA or of RAG. Moreover, the Peg-modified antigens did not combine either in vitro or in vivo with IgE antibodies directed against the natural antigens. Hence, OA-PEG and RAG-PEG conjugates were incapable of triggering allergic reactions in animals possessing IgE antibodies to the unmodified antigens. These PEG-modified antigens were also shown to be tolerogenic.

Allergens↗
PubMed1978

Quantitation of IgE antibody specific for ragweed and grass allergens: binding of radiolabeled allergens by solid-phase bound IgE.

IgE antibody specific for multiple allergens extracted from grass and ragweed pollens was measured by radioimmunoassay. The assay depends on the interaction between IgE antibody bound to a polystyrene solid phase, , 125I-labeled grass allergens (GA), and ragweed allergens (RW). The binding of 125I RW by serum IgE antibody from 37 allergic patients ranged from 0.2 ng to 75 ng RW protein (P) bound per ml. This binding of 125I RW by patient's IgE was paralleled by their IgE binding of 125I antigen E (AgE), a purified allergen from ragweed pollen (r = 0.90, p less than 0.001). Inhibition of patient's IgE binding of 125I RW by highly purified AgE ranged from 25% to 85% indicating individual differences in patient's IgE response to inhaled ragweed pollen. The binding of 125I GA by serum IgE antibody from 7 grass-sensitive patients ranged from 0.6 ng GA P bound per ml to 15 ng. This assay should be useful in the study of IgE responses to environmental agents containing multiple allergens and has the advantage that other antibody classes cannot interfere with the interaction between IgE antibody and labeled allergens.

Allergens↗
PubMed1992

Identification of allergenic epitopes on Der f I, a major allergen of Dermatophagoides farinae, using monoclonal antibodies.

The antigenic and allergenic structure of Der f I, a major allergen of the house dust mite Dermatophagoides farinae (Df) was investigated by means of a panel of 11 selected monoclonal antibodies (mAb) obtained from BALB/c mice immunized with purified Der f I. The species specificity of these mAb, tested with Der f I and Der p I--the homologous allergen from Dermatophagoides pteronyssinus--was generally restricted to Der f I since 10 out of 11 mAb reacted only with this allergen. Epitope specificity of the mAb was determined by both competitive inhibition and sandwich ELISA experiments. The results indicated the presence of at least four non-overlapping, non-repeated antigenic sites on Der f I, which were recognized by one or several mAb (sites A, B, C and D). Comparative epitope specificity studies between human IgE antibodies and mice mAb were performed, on sera and basophils of Df sensitive patients, using different inhibition assays (ELISA and histamine release experiments). The degree of inhibition varied between the patients and upon the assay design. Most of the mAb tested were found to significantly inhibit the binding of human IgE to Der f I (p less than 0.01) when compared with Der p I specific mAb as a control. The mAb reacting with site A was found to be the most potent inhibitor, presenting a mean inhibition of up to 56% in ELISA as well as in histamine release experiments. The results show that both human IgE antibodies and mAb can be directed against identical or closely related epitopes of Der f I. Therefore anti-Der f I mAb constitute immunologic probes in further allergenic epitope and peptide analysis of this major mite allergen.

Allergens↗
PubMed1992

Distribution of allergens and allergen-coding mRNAs in various tissues of white birch.

The distribution of allergenic proteins was investigated in various tissues of white birch, Betula verrucosa (pollen, leaves and male inflorescences containing immature pollen). In addition, callus and suspension culture cells were investigated for expression of IgE-binding proteins. Furthermore, RNA was extracted from all these tissues and subjected to in vitro translation in a cell-free wheat germ system. Bet v I, the major birch pollen allergen, could be extracted easily from pollen, and in low amounts from callus and leaves. No Bet v I could be extracted from immature male inflorescences. Minor allergens were expressed in high concentrations in pollen and in low concentrations in immature male inflorescences. No minor allergens could be detected in callus and leaves. In contrast to these observations, RNA from all the tissues as well as from callus could be translated in vitro into Bet v I as well as into minor allergens, in particular birch profilin (Bet v II), an important minor allergen. These data suggest that IgE-binding proteins of B. verrucosa, especially Bet v I, under certain circumstances can readily be synthesized in tissues other than pollen. This concept is corroborated by the recent observation that Bet v I reveals high homology with disease resistance response gene products from other plants, suggesting a similar function of Bet v I for the birch.

Allergens↗
PubMed1976

The allergenic structure of allergen M from cod. I. Tryptic peptides of fragment TM 1.

In attempts to locate the allergenic active sites of fragment TM 1 of allergen M from cod, the allergenicity of the tryptic hydrolysis peptides was examined both in vivo and in vitro. A duodecapeptide (residues No. 33-44) was tentatively suggested to incorporate at least one allergenic determinant. All the tryptic peptides were less active than allergen M as shown by the in vivo titration experiments. The activity of the peptides was not due to contamination of intact allergens.

Allergens↗
PubMed1975

Grass allergens : a preliminary characterization by means of RAST-based allergen assay methods.

A preliminary study of a grass pollen allergens by means of radioallergosorbent test (RAST)-based assay methods has been made. A combination of gel filtration and ion exchange chromatography has been used to separate allergens, mainly from Festuca elatior, Lolium perenne, and Phleum pratense, into groups dependent on their molecular weight and net electric charges. A RAST-based titration method was used to detect and quantitate the different allergens. The specificity towards IgE of the different allergen groups was investigated by means of a RAST-based inhibition method. The allergen groups were found to be of a quite heterogenous nature when investigated by means of polyacrylamide gel electrophoreses. Furthermore, the different groups exhibited a considerable degree of cross-reactions when tested against a pool of patient sera by means of the inhibition method. This was the case even for allergen groups which differed significantly both in regard to molecular weight and net electric charge.

Allergens↗
PubMed1978

New contact allergens and allergen sources.

In the report new contact allergens and allergen sources detected in Warsaw in the period 1975-1977 are described. They are divided into 3 groups: industrial allergens, remaining occupational allergens and cosmetics. There are given some data concerning the substances present in industrial oils, hardeners and epoxy resin solvents, drugs sensitizing nurses, several new sources of chromium allergens, essential oils and synthetic flavours. Results obtained with various star anise oil samples are described. Essential oils and synthetic flavours. Results obtained with various star anise oil samples are described. Essential oils and synthetic flavours are discussed as the main allergens in cosmetics.

Allergens↗
PubMed1975

Allergens of mammalian origin. II. Characterization of allergens extracted from rat, mouse, guinea pig, and rabbit pelts.

Aqueous extracts prepared from lyophilized, defatted rat, mouse, guinea pig, and rabbit pelts elicited intense wheal-and-flare responses in the skin of a high proportion of patients who were clinically sensitive to these animals. The major allergens in each extract were nondialyzable. Skin test reactions to rat, mouse, and guinea pig serum were common in patients allergic to these animals. The fractions of rat, mouse, and rabbit pelt extract showing maximum allergenic activity contained proteins with the electrophoretic mobility of serum albumin. Fractions of guinea pig pelt extract with maximum allergenic activity were of prealbumin mobility and contained little stainable protein. On Sephadex G-100 gel filtration, most allergen from rat, mouse, and guinea pig pelt extracts was recovered in fractions containing proteins with a molecular weight range of 10,000 to 25,000 daltons. Allergen in rabbit pelt extract had a slightly higher molecular weight range of 18,000 to 38,000 daltons.

Allergens↗
PubMed1992

A comparative study of allergenic and potentially allergenic enzymes from Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei.

The presence of the enzymatically active allergens equivalent to Der p I (cysteine protease), Der p III (serine protease) and amylase in extracts of Dermatophagoides pteronyssinus, D. farinae and Euroglyphus maynei was determined using appropriate enzymatic techniques. Biochemical equivalents of all three allergens were present in each extract studied. Studies also showed that the mite extracts contained a variety of other biochemically active enzymes including trypsin, chymotrypsin, carboxypeptidase A and B, glucoamylase and lysozyme. Marked differences in the relative concentrations of some of these enzymes in different mite extracts were observed, particularly trypsin and carboxypeptidase A. The enzymes were physicochemically similar to equivalent enzymes from vertebrate and invertebrate sources. Chromatofocusing studies of faecal extracts derived from D. pteronyssinus and D. farinae showed that several isoforms of each enzyme were present. The data indicated that there were more trypsin isoforms, with pI over a wider range, in extracts prepared from D. pteronyssinus. Proteases and carbohydrases were also found in extracts prepared from faecally enriched material suggesting that they were endoperitrophic and associated with mite digestion. The data suggest that not only are the group I, III and amylase allergens a consistent feature of most pyroglyphid dust mites but also that other proteases and carbohydrases present in mite faeces are allergenic.

Allergens↗
PubMed1977

A new well-characterized, purified allergen preparation from timothy pollen. II. Allergenic in vivo and vitro properties.

A purified allergen preparation, Timothy N, from timothy pollen and a crude commercial extract, Timothy O, prepared from the same pollen material, were tested in tenfold dilutions on 59 adults with allergic rhinitis and on 29 children with bronchial asthma. All patients were allergic to grass pollen. Using the prick and intracutaneous methods, dose-response tablets were established for the two preparations showing a good correlation. Nasal provocation tests on the adult patients and bronchial provocation tests on the children gave positive reactions in all cases when using Timothy N. No irritant effect resulting in non specific reactions were elicited. The availability of stable, freeze-dried and purified allergen preparations supplied in different vials with defined allergenic activities fulfils the clinical demands for a modern diagnostic allergen preparation.

Adolescent↗
PubMed1976

[Allergenic fractions of bacteria belonging to the enteric family. VII. Characteristics of the intracellular proteins comprising the allergenic substrate of Escherichia coli using ion exchange chromatography].

A method of successive chromatography on Sephadex G-50 and G-100 and DEAE-Sephadex A-50 was applied for separation of the allergenic complex of E. coli intracellular proteins into a number of immunochemically different or significantly differing fractions with a definite set of antigens. Results of analysis of the fractions obtained in the tests of increased sensitivity of delayed type (ISDT) in vivo and in vitro corresponded to the view of the immunological polyvalency of the allergenic substrate of enterobacteria. Four groups of antigens were distinguished by the ratio of the activity indices in the skin reactions of ISDT and in the tests of specific inhibition of macrophage migration. Singificance of individual antigens in the formation of the allergenic profile of bacterial cells is determined by their quantitative content and the extent of the allergenic activity.

Allergens↗
PubMed1975

[Allergenic fractions of Enterobacteriaceae. VI. Gel-chromatographic profile of intracellular protein antigens, forming the allergen-active substrate of enterobacteria].

Allergeno-active protein substrate of enterobacteria (E. coli and R. rettgeri strains) was divided into 7 fractions with a different molecular weight with the aid of many-stage gel-filtration through Sephadex (G-50, G-75, G-100, G-150, G-200). A study was made of their biochemical composition, antigenic and protein spectrum, allergenic properties in the reactions of hypersensitivity of delayed type in vivo (skin tests) and in vitro (inhibition of macrophage migration). The principal part of allergenic activity was determined by components with a molecular weight of 30-150 and over 800 thousand. The majority of the antigens had a molecular weight of 30-150 thousand. A physico-chemical heterogeneity of immunologically affiliated components was noted. The allergenic substrate of the bacterial cell included a complex of molecular-nonhomogenous "strong" and "weak" protein allergens.

Allergens↗
PubMed1976

Allergens of mammalian origin. IV. Evidence for common allergens in cat and dog serum.

IgE antibodies present in serum from 3 patients clinically sensitive to cat and dog were shown to combine with whole cat and dog sera linked to cellulose particles. Employing a modified radioallergosorbent technique (RAST), it was shown that cat and dog sera inhibited the binding of IgE antibodies to insolubilized cat serum and to insolubilized dog serum. These findings suggest that cat and dog sera have common allergens. Other mammalian sera were also tested and found to have little inhibitory activity. Cat and dog sera did not inhibit the binding of IgE antiragweed antibodies to an insolubilized ragweed fraction. Following separation of cat serum by gel filtration on Sephadex G-200 or electrophoresis in acrylamide gel, several fractions were found to inhibit the binding of IgE antibodies to insolubilized cat and dog sera. Whether the heterogeneity observed reflects the presence of single allergens with diverse size and charge properties or multiple allergens remains to be determined.

Allergens↗
PubMed1976

Studies on Alternaria allergens. I. Establishment of the radioallergosorbent test for measurement of Alternaria allergens.

The ability to covalently couple Alternaria allergens to microcrystalline cellulose particles has permitted not only the measurement of IgE antibodies to Alternaria in patient serums but also the identification of allergenic fractions from crude Alternaria extracts. Crude aqueous Alternaria extracts from 3 commerical suppliers were coupled to cellulose but failed to bind more than 5% of total radioactive counts (TRC) when reacted with serums from highly sensitive patients. Fractionation of a commercial extract through Sephadex G-25 showed that almost all allergenic activity was located in a protein- and carbohydrate-containing peak eluting at the column void volume. These fractions were pooled and coupled to cellulose to yield a RAST polymer which produced up to 20% TRC binding when tested with serums from over 100 Alternaria-sensitive patients, and only up to 1% TRC binding with 17 nonallergic serums. The study of commercial Alternaria extracts by chromatographic and Rast inhibition techniques showed that present extracts are neither qualitatively or quantitatively comparable.

Allergens↗