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At least 1,117 records · Page 62Linked to original sources
PubMed1982

The immune response to bee venom. Comparison of the antibody response to phospholipase A2 with the response to inhalant antigens.

The antibody response to phospholipase A2 (PLA2) was studied by using radiolabelled antigen-binding techniques for both IgG and IgE antibodies. The results are compared with results for antigen P1 from Dermatophagoides pteronyssinus and for rye I from rye grass pollen. The response to PLA2 differs from the response to the inhalant allergens in several ways: almost all exposed bee keepers produce IgG antibodies to PLA2; among the allergic bee keepers there was no quantitative correlation between IgG and IgE antibodies; and the antibodies to PLA2 are not produced locally in the nose. Bee keepers with hay fever did not appear to have an increased incidence of allergic reactions to bee venom. In addition, the bee keepers with hay fever and the same levels of IgG and IgE antibodies to rye I as other individuals with hay fever. However, the bee keepers who had no history of hay fever were found to have high levels of IgG antibodies to rye I. These antibodies did not cross-react with PLA2 or bee venom, and the results suggest that bee stings may act as an adjuvant for IgG antibodies to pollen antigens.

Allergens↗
PubMed1982

Antibody response profiles to components of rye grass pollen extract in various strains of mice.

Using a combination of immunoprecipitation and polyacrylamide gel electrophoresis techniques, patterns of antibody responses to a number of components in rye pollen extract have been studied in hyperimmune mouse sera. Common laboratory strains of mice were investigated, including AKR, C3H/He, SwR, Ist, Asn, Balb/c, C57BL10, DBA2 and BD1:F1 hybrids. All strains responded vigorously to the immunisation protocol used (rye pollen extract/alum followed by a booster dose in aqueous media) when tested with non-discriminating assay procedures such as haemagglutination or passive cutaneous anaphylaxis directed against the whole rye pollen extract. However, markedly variable antibody responses were observed between strains and between murine and human sera when considered in relation to individual rye extract components. Particularly noteworthy was the relatively poor response of all mice to the low molecular weight rye antigen component (11,000 daltons). This material was readily detected by human sera derived from pollenosis patients. Notable also was the fact that no single rye component was detected by all mice sera. These results illustrate the complex serological response induced by heterogeneous antigen mixtures, such as grass pollen extracts.

Animals↗
PubMed1984

Proliferation of mouse lymphocytes to rye grass pollen extract: effect of inflammatory exudate cells.

The ability of inflammatory peritoneal exudate cells to modify a murine lymphoproliferative response to rye grass pollen extract was investigated. Popliteal and mesenteric lymph node cells from Balb/c mice immunised with either aqueous rye or rye grass emulsified in complete Freund's adjuvant were co-cultured with 2 X 10(3)-10(5) macrophage or polymorphonuclear neutrophil (PMN)-enriched exudate cells. There was a dose-dependent increase in the response to rye grass antigen with increasing numbers of PMN. A similar enhancement was seen with up to 10(4) macrophages per culture; higher numbers were inhibitory. Lymph node cells from rye grass or ovalbumin-immune mice that had been challenged with a combination of sensitising antigen plus 10(7) PMN gave an increased antigen-specific response in vitro. Neither antigen alone, PMN nor a mixture of PMN plus heterologous antigen was active. Adoptive transfer of a similar number of peritoneal macrophages plus antigen was also without effect. These results are in accord with the suggestion that cells obtained from acute inflammatory lesions can directly influence the activity of immunocompetent lymphocytes.

Animals↗
PubMed1987

Seasonal variations in in vitro synthesis of rye pollen-specific IgE by human peripheral mononuclear cells. Functional heterogeneity within the IgE-B pool.

Peripheral blood mononuclear B cells from 6 rye pollen-allergic patients, with no consistent perennial symptoms, were isolated before (July), during (October) and after (February and May) the pollen season. The T-depleted cells were fractionated on a discontinuous percoll density gradient and the B cell fractions, together with unfractionated B cells, incubated in vitro for quantitation of spontaneous synthesis of rye pollen-specific IgE. Markedly higher levels of IgE were synthesised by the fractions, as opposed to unfractionated B cells. The low-density fraction (B5) contributed most towards synthesis in the pollen season and the denser B6 cells in the pre- and post-pollen season. All low-density B cell fractions (B1-3-B5) and some high-density fractions contained large but variable amounts of preformed specific IgE which was retained, even in the absence of de novo synthesis in vitro, during the post- and pre-pollen season. Since only a fraction of this preformed IgE escaped into culture supernatants the contribution of preformed IgE to in vitro IgE synthesis in general may require reappraisal.

Adult↗
PubMed1987

T cell reactivity of conjugates of N-formyl-methionyl-leucyl-phenylalanine and rye-grass pollen allergens.

Conjugates of rye-grass pollen extract and N-formyl-methionyl-leucyl-phenylalanine were prepared using an activated form of the tripeptide. Introduction of the peptide into the extract brought about an extensive reduction of reactivity with grass-pollen-specific IgE, as measured by RAST inhibition. Despite this loss, guinea pig alveolar macrophages and murine splenic macrophages readily presented the conjugates to T lymphocytes specific for grass pollen allergens and caused their proliferation in vitro.

Animals↗
PubMed1988

Induction of allergen-specific T cells by conjugates of N-formyl-methionyl-leucyl-phenylalanine and rye grass pollen extract.

A conjugate of the biologically active peptide N-formyl-methionyl-leucyl-phenylalanine and rye grass pollen extract (F-MLP/rye), previously shown to react with rye grass pollen extract-specific T cells, induced the formation of allergen-specific T cells in mice. Lymph node cells prepared from mice immunized with either native extract or F-MLP/rye gave an enhanced response to unmodified rye grass pollen allergens in vitro. Syngeneic spleen macrophages were able to present the unmodified allergens to T cells obtained from both groups of mice causing their proliferation in vitro. Conjugation of the peptide into the extract brought about an extensive reduction in its reactivity with grass pollen-specific human IgE, and a loss of its ability to induce specific IgG antibody in guinea-pigs. A state of delayed hypersensitivity specific for rye grass pollen extract was produced in guinea-pigs by immunization with either the F-MLP/rye or unmodified extract. It is concluded that conjugates such as F-MLP/rye or other T' allergoids could be used as probes to investigate whether changes in T cell activity are important in immunotherapy.

Allergens↗
PubMed1988

Short-term sensitizing antibodies in bakers' asthma.

In a prospective study the occurrence of rye-specific IgG4 was investigated. We compared 17 bakers with clinical symptoms of bakers' asthma and a more than 100% increase in specific airway resistance following rye dust provocation to 16 bakers who showed neither symptoms of asthma nor an increase in specific airway resistance following rye dust provocation. In the group of patients with allergic type I responses, specific IgG4 was found in 15 cases by an indirect immunofluorescent test on rye grains. In none of the asymptomatic bakers was rye-specific IgG4 detected. In 15 symptomatic subjects rye-specific IgE alone or together with rye-specific IgG4 was found. In 2 cases only rye-specific IgG4--the so-called short-term sensitizing antibody--was demonstrated to explain the allergic bronchial response.

Allergens↗
PubMed1989

Molecular genetics of human immune responsiveness to Lolium perenne (rye) allergen, Lol p III.

Lol p II and III are each about 11-kD protein allergens from the pollen of Lolium perenne (rye grass). We have found that human immune responses (IgE and IgG antibodies) to both proteins are significantly associated with HLA-DR3. In addition, the two proteins are cross-reactive with the antibodies in many human sera (about 84% human sera showed the cross-reactivity). We have determined greater than 90% of the amino acid sequences of the two proteins and found that they are at least 54% homologous. Berzofsky found that 75% of the 23 known T cell sites in various proteins had an amphipathic structure. Our analysis by the same method showed that both Lol p II and III have a major region of amphipathicity (at residues 61-67, Lol p III numbering) which might contain sites for binding to an Ia molecule and a T cell receptor. This region is identical between Lol p II and III, except for an Arg-Lys substitution, and could account, in part, for the DR3 association with responsiveness to both molecules. An interesting difference between the two proteins is that immune response to Lol p III is associated with DR5 (in addition to DR3), whereas no DR5 association is found in the case of Lol p II. One possibility is that Lol p III has an additional site which binds to the DR5 Ia molecule. Lol p III indeed has a second highly amphiphathic peptide, 24-30 (Lol p III 24 R P G D T L A 30), which is different and not amphipathic in Lol p II.(ABSTRACT TRUNCATED AT 250 WORDS)

Age Factors↗
PubMed1989

Allergenic fragments of ryegrass (Lolium perenne) pollen allergen Lol p IV.

To facilitate studies on establishing the nature of structure/function relationships of allergens, ryegrass pollen allergen, Lol p IV, was cleaved into smaller fragments by cyanogen bromide (CNBr) and the resulting peptides were further digested with trypsin. The resulting peptides were then fractionated by high performance liquid chromatography (HPLC) on a C-18 reverse phase column. The allergenic activity of the HPLC fractions was evaluated in terms of their ability to inhibit the binding of 125I-Lol p IV to serum IgE antibodies of a grass-allergic patient. Many of these fractions inhibited the binding between the native allergen and IgE antibodies in a dose-dependent manner. The inhibitions were specific, i.e., the fractions did not inhibit the binding between 125I-Lol p I (a group-I ryegrass pollen allergen) and the IgE antibodies present in the allergic human serum. The possibility that the allergenic peptide fractions were contaminated by the native undegraded allergen, which might have accounted for the observed inhibition, was ruled out by the fact that the native allergen could not be detected by SDS-PAGE and the elution profiles of allergenically active peptides did not coincide with that of native allergen. One of the allergenic sites recognized by monoclonal antibody (Mab) 90, i.e., site A, was located in HPLC fractions 90-100 while another allergenic site B (recognized by Mab 12) appeared to be lost following the sequential digestion of Lol p IV with CNBr and trypsin.

Allergens↗
PubMed1989

Demonstration of human, rye grass pollen extract-specific, helper and suppressor stimulating activity of modified allergens by effects on in vitro hapten-specific antibody production.

An in vivo system is described in which penicilloyl antibody was produced from peripheral leucocytes of a grass pollen-sensitive patient who had received penicillin therapy, by challenge of the cells with penicilloyl-grass pollen extract conjugate. Incubation of these leucocytes with a number of modified preparations of grass pollen extract with various T-cell-stimulating properties was shown to affect penicilloyl antibody production. Both chymotryptically fragmented rye grass pollen extract and a conjugate of f met-leu-phe and rye grass pollen extract enhanced penicilloyl-specific antibody similarly to the enhancement induced by unmodified extract, though at high concentration some suppression was seen. A conjugate of polysarcosine and rye grass pollen extract, previously shown to cause antibody suppression in mice, was similarly suppressive for penicilloyl-specific antibody. The system therefore shows potential for the evaluation of the effects of modified allergen treatment on antibody levels via T-cell mechanisms.

Allergens↗
PubMed1990

IgE-binding proteins from pine (Pinus radiata D. Don) pollen: evidence for cross-reactivity with ryegrass (Lolium perenne).

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 commercial 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.

Antigens, Differentiation↗
PubMed1995

Antibody response against wheat, rye, barley, oats and corn: comparison between gluten-sensitive patients and monoclonal antigliadin antibodies.

The antibody response of patients with gluten-sensitive enteropathy and dermatitis herpetiformis against alcohol-soluble prolamines of wheat, rye, barley, oats and corn assessed by immunoblotting was compared to the staining patterns produced by monoclonal antigliadin antibodies. Both monoclonal antibodies (MAbs) and patient serum reacted with wheat, rye, barley and oats, the patient serum showing individual variation both in IgA and IgG stainings. A broad reactivity with polypeptides from 30 to 68 kD was, however, typical for patient serum and comparable to the reactivity of two broadly reacting antigliadin MAbs. This kind of broad reactivity of the MAb may suggest that it binds to glutamine-repeating sequences of highly homologous gliadin polypeptides. Glutamine- and proline-containing motifs Pro-Ser-Gln-Gln and Gln-Gln-Gln-Pro are also included in the peptides toxic to the celiac small intestinal mucosa. Our study indicates that the humoral response of the patients may detect similar structures, in oat prolamines as well. Patient serum and one of the MAbs also reacted with a 22-kD polypeptide of corn extract. The meaning of this reactivity is not known, and further characterization of the antigenic epitopes of different cereals will be important.

Amino Acid Sequence↗
PubMed1996

IgA and IgG binding components of wheat, rye, barley and oats recognized by immunoblotting analysis with sera from adult atopic dermatitis patients.

IgA and IgG antibody response of adult atopic dermatitis patients against neutral/ acidic fractions of wheat, rye, barley and oats was analyzed utilizing an immunoblotting method. Moreover, the antibody response against ethanol-soluble fraction of wheat was examined with serum pools of healthy donors, atopic dermatitis patients and patients with dermatitis herpetiformis or adult celiac disease. All patient sera revealed polymorphic IgA and IgG binding to cereal peptides with molecular weights of 11-97 kD. The antibody staining was essentially identical with atopic dermatitis patients and controls. Patients with dermatitis herpetiformis or celiac disease showed more intensive staining with the ethanol extract of wheat and showed more IgA-stained bands in immunoblotting. It seems that the presence of IgA and IgG antibodies to different cereal antigens is a result of natural exposure and in atopic dermatitis displays little diagnostic significance, in contrast to antigliadin antibody response in dermatitis herpetiformis and celiac disease.

Adolescent↗