Effect of cysteine mutagenesis on human IgE reactivity of recombinant forms of the major rye grass pollen allergen Lol p 1
Background: Hypersensitivity to the group 1 grass pollen allergens is a significant causative factor in the onset of symptoms for hay fever sufferers. To better understand the IgE reactivity of the group 1 allergen from rye grass pollen, we sought to disrupt potential conformational IgE epitopes on...
| Main Authors: | , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2003-01-01
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| Series: | Allergology International |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S1323893015311655 |
| _version_ | 1828741411211575296 |
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| author | Nicole de Weerd Prem L. Bhalla Mohan B. Singh |
| author_facet | Nicole de Weerd Prem L. Bhalla Mohan B. Singh |
| author_sort | Nicole de Weerd |
| collection | DOAJ |
| description | Background: Hypersensitivity to the group 1 grass pollen allergens is a significant causative factor in the onset of symptoms for hay fever sufferers. To better understand the IgE reactivity of the group 1 allergen from rye grass pollen, we sought to disrupt potential conformational IgE epitopes on recombinant (r) Lol p 1 by the specific replacement of the seven cysteine residues in the protein sequence.
Methods: Site-directed mutagenesis on the Lol p 1 coding sequence was used to replace all seven cysteine residues with serine residues. rLol p 1 and the seven cysteine variants generated by this method were tested for comparative human IgE reactivity via western blot immunoscreening and densitometry.
Results: Alteration of the cysteine residues at amino acid positions 72, 77, 83 and 139 of rLol p 1 was found to reduce the human IgE binding potential of the molecule. However, the most consistent reduction in human IgE reactivity was demonstrated by replacement of C77; human IgE antibodies showed an average 62.7% reduction in reactivity to this molecule.
Conclusions: The present investigation has shown that at least one of the cysteine residues within the Lol p 1 protein contributes to the IgE binding properties of this allergen. |
| first_indexed | 2024-04-13T00:59:19Z |
| format | Article |
| id | doaj.art-fdeebc78f7ab40fcaf54a9d1bba2b8f9 |
| institution | Directory Open Access Journal |
| issn | 1323-8930 |
| language | English |
| last_indexed | 2024-04-13T00:59:19Z |
| publishDate | 2003-01-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Allergology International |
| spelling | doaj.art-fdeebc78f7ab40fcaf54a9d1bba2b8f92022-12-22T03:09:33ZengElsevierAllergology International1323-89302003-01-0152418319010.1046/j.1323-8930.2003.00300.xEffect of cysteine mutagenesis on human IgE reactivity of recombinant forms of the major rye grass pollen allergen Lol p 1Nicole de WeerdPrem L. BhallaMohan B. SinghBackground: Hypersensitivity to the group 1 grass pollen allergens is a significant causative factor in the onset of symptoms for hay fever sufferers. To better understand the IgE reactivity of the group 1 allergen from rye grass pollen, we sought to disrupt potential conformational IgE epitopes on recombinant (r) Lol p 1 by the specific replacement of the seven cysteine residues in the protein sequence. Methods: Site-directed mutagenesis on the Lol p 1 coding sequence was used to replace all seven cysteine residues with serine residues. rLol p 1 and the seven cysteine variants generated by this method were tested for comparative human IgE reactivity via western blot immunoscreening and densitometry. Results: Alteration of the cysteine residues at amino acid positions 72, 77, 83 and 139 of rLol p 1 was found to reduce the human IgE binding potential of the molecule. However, the most consistent reduction in human IgE reactivity was demonstrated by replacement of C77; human IgE antibodies showed an average 62.7% reduction in reactivity to this molecule. Conclusions: The present investigation has shown that at least one of the cysteine residues within the Lol p 1 protein contributes to the IgE binding properties of this allergen.http://www.sciencedirect.com/science/article/pii/S1323893015311655allergygrass pollenLol p 1mutage- nesisrye grass |
| spellingShingle | Nicole de Weerd Prem L. Bhalla Mohan B. Singh Effect of cysteine mutagenesis on human IgE reactivity of recombinant forms of the major rye grass pollen allergen Lol p 1 Allergology International allergy grass pollen Lol p 1 mutage- nesis rye grass |
| title | Effect of cysteine mutagenesis on human IgE reactivity of recombinant forms of the major rye grass pollen allergen Lol p 1 |
| title_full | Effect of cysteine mutagenesis on human IgE reactivity of recombinant forms of the major rye grass pollen allergen Lol p 1 |
| title_fullStr | Effect of cysteine mutagenesis on human IgE reactivity of recombinant forms of the major rye grass pollen allergen Lol p 1 |
| title_full_unstemmed | Effect of cysteine mutagenesis on human IgE reactivity of recombinant forms of the major rye grass pollen allergen Lol p 1 |
| title_short | Effect of cysteine mutagenesis on human IgE reactivity of recombinant forms of the major rye grass pollen allergen Lol p 1 |
| title_sort | effect of cysteine mutagenesis on human ige reactivity of recombinant forms of the major rye grass pollen allergen lol p 1 |
| topic | allergy grass pollen Lol p 1 mutage- nesis rye grass |
| url | http://www.sciencedirect.com/science/article/pii/S1323893015311655 |
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