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The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects
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| Zeitschriftentitel: | Allergy |
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| Personen und Körperschaften: | , , , , , , , |
| In: | Allergy, 55, 2000, 3, S. 246-250 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Assunta Costa, M. Duro, G. Izzo, V. Colombo, P. Mirisola, M. G. Locorotondo, G. Cocchiara, R. Geraci, D. Assunta Costa, M. Duro, G. Izzo, V. Colombo, P. Mirisola, M. G. Locorotondo, G. Cocchiara, R. Geraci, D. |
|---|---|
| author |
Assunta Costa, M. Duro, G. Izzo, V. Colombo, P. Mirisola, M. G. Locorotondo, G. Cocchiara, R. Geraci, D. |
| spellingShingle |
Assunta Costa, M. Duro, G. Izzo, V. Colombo, P. Mirisola, M. G. Locorotondo, G. Cocchiara, R. Geraci, D. Allergy The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects Immunology Immunology and Allergy |
| author_sort |
assunta costa, m. |
| spelling |
Assunta Costa, M. Duro, G. Izzo, V. Colombo, P. Mirisola, M. G. Locorotondo, G. Cocchiara, R. Geraci, D. 0105-4538 1398-9995 Wiley Immunology Immunology and Allergy http://dx.doi.org/10.1034/j.1398-9995.2000.00265.x <jats:p>Pollen allergens are multivalent proteins that cross‐link IgE antibodies on mast or basophil cells, inducing secretion of biologic mediators, and resulting in various allergic symptoms. The IgE‐binding regions of the <jats:italic>Parietaria judaica </jats:italic>(<jats:italic>Pj</jats:italic>) pollen major allergen rPar j 2 were investigated. Twenty‐nine single sera from <jats:italic>Pj</jats:italic>‐allergic subjects were tested by Western blot against five recombinant peptides. At least four putative IgE‐binding epitopes were identified. The analysis of their diffusion suggested a heterogeneous IgE‐binding response. In fact, 75% of the sera reacted with peptide 1–54, 48% with peptide 48–101, 24% with peptide 1–30, 7% with peptide 29–54, and none with peptide 48–76. These five peptides were analyzed with the histamine‐release assay. Only peptide 48–101 was capable of inducing degranulation and release of histamine. These results suggest that the recombinant rPar j 2 allergen contains IgE epitopes that are heterogeneously recognized by sensitive patients, and that therefore the therapeutic approach based on the use of haptenic peptides needs a careful evaluation.</jats:p> The IgE‐binding epitopes of rPar j 2, a major allergen of <i>Parietaria judaica</i> pollen, are heterogeneously recognized among allergic subjects Allergy |
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| title |
The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_unstemmed |
The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_full |
The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_fullStr |
The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_full_unstemmed |
The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_short |
The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_sort |
the ige‐binding epitopes of rpar j 2, a major allergen of <i>parietaria judaica</i> pollen, are heterogeneously recognized among allergic subjects |
| topic |
Immunology Immunology and Allergy |
| url |
http://dx.doi.org/10.1034/j.1398-9995.2000.00265.x |
| publishDate |
2000 |
| physical |
246-250 |
| description |
<jats:p>Pollen allergens are multivalent proteins that cross‐link IgE antibodies on mast or basophil cells, inducing secretion of biologic mediators, and resulting in various allergic symptoms. The IgE‐binding regions of the <jats:italic>Parietaria judaica </jats:italic>(<jats:italic>Pj</jats:italic>) pollen major allergen rPar j 2 were investigated. Twenty‐nine single sera from <jats:italic>Pj</jats:italic>‐allergic subjects were tested by Western blot against five recombinant peptides. At least four putative IgE‐binding epitopes were identified. The analysis of their diffusion suggested a heterogeneous IgE‐binding response. In fact, 75% of the sera reacted with peptide 1–54, 48% with peptide 48–101, 24% with peptide 1–30, 7% with peptide 29–54, and none with peptide 48–76. These five peptides were analyzed with the histamine‐release assay. Only peptide 48–101 was capable of inducing degranulation and release of histamine. These results suggest that the recombinant rPar j 2 allergen contains IgE epitopes that are heterogeneously recognized by sensitive patients, and that therefore the therapeutic approach based on the use of haptenic peptides needs a careful evaluation.</jats:p> |
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| author | Assunta Costa, M., Duro, G., Izzo, V., Colombo, P., Mirisola, M. G., Locorotondo, G., Cocchiara, R., Geraci, D. |
| author_facet | Assunta Costa, M., Duro, G., Izzo, V., Colombo, P., Mirisola, M. G., Locorotondo, G., Cocchiara, R., Geraci, D., Assunta Costa, M., Duro, G., Izzo, V., Colombo, P., Mirisola, M. G., Locorotondo, G., Cocchiara, R., Geraci, D. |
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| description | <jats:p>Pollen allergens are multivalent proteins that cross‐link IgE antibodies on mast or basophil cells, inducing secretion of biologic mediators, and resulting in various allergic symptoms. The IgE‐binding regions of the <jats:italic>Parietaria judaica </jats:italic>(<jats:italic>Pj</jats:italic>) pollen major allergen rPar j 2 were investigated. Twenty‐nine single sera from <jats:italic>Pj</jats:italic>‐allergic subjects were tested by Western blot against five recombinant peptides. At least four putative IgE‐binding epitopes were identified. The analysis of their diffusion suggested a heterogeneous IgE‐binding response. In fact, 75% of the sera reacted with peptide 1–54, 48% with peptide 48–101, 24% with peptide 1–30, 7% with peptide 29–54, and none with peptide 48–76. These five peptides were analyzed with the histamine‐release assay. Only peptide 48–101 was capable of inducing degranulation and release of histamine. These results suggest that the recombinant rPar j 2 allergen contains IgE epitopes that are heterogeneously recognized by sensitive patients, and that therefore the therapeutic approach based on the use of haptenic peptides needs a careful evaluation.</jats:p> |
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| spelling | Assunta Costa, M. Duro, G. Izzo, V. Colombo, P. Mirisola, M. G. Locorotondo, G. Cocchiara, R. Geraci, D. 0105-4538 1398-9995 Wiley Immunology Immunology and Allergy http://dx.doi.org/10.1034/j.1398-9995.2000.00265.x <jats:p>Pollen allergens are multivalent proteins that cross‐link IgE antibodies on mast or basophil cells, inducing secretion of biologic mediators, and resulting in various allergic symptoms. The IgE‐binding regions of the <jats:italic>Parietaria judaica </jats:italic>(<jats:italic>Pj</jats:italic>) pollen major allergen rPar j 2 were investigated. Twenty‐nine single sera from <jats:italic>Pj</jats:italic>‐allergic subjects were tested by Western blot against five recombinant peptides. At least four putative IgE‐binding epitopes were identified. The analysis of their diffusion suggested a heterogeneous IgE‐binding response. In fact, 75% of the sera reacted with peptide 1–54, 48% with peptide 48–101, 24% with peptide 1–30, 7% with peptide 29–54, and none with peptide 48–76. These five peptides were analyzed with the histamine‐release assay. Only peptide 48–101 was capable of inducing degranulation and release of histamine. These results suggest that the recombinant rPar j 2 allergen contains IgE epitopes that are heterogeneously recognized by sensitive patients, and that therefore the therapeutic approach based on the use of haptenic peptides needs a careful evaluation.</jats:p> The IgE‐binding epitopes of rPar j 2, a major allergen of <i>Parietaria judaica</i> pollen, are heterogeneously recognized among allergic subjects Allergy |
| spellingShingle | Assunta Costa, M., Duro, G., Izzo, V., Colombo, P., Mirisola, M. G., Locorotondo, G., Cocchiara, R., Geraci, D., Allergy, The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects, Immunology, Immunology and Allergy |
| title | The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_full | The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_fullStr | The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_full_unstemmed | The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_short | The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| title_sort | the ige‐binding epitopes of rpar j 2, a major allergen of <i>parietaria judaica</i> pollen, are heterogeneously recognized among allergic subjects |
| title_unstemmed | The IgE‐binding epitopes of rPar j 2, a major allergen of Parietaria judaica pollen, are heterogeneously recognized among allergic subjects |
| topic | Immunology, Immunology and Allergy |
| url | http://dx.doi.org/10.1034/j.1398-9995.2000.00265.x |