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Human IgE against the major allergen Bet v 1--defining an epitope with limited cross-reactivity between different PR-10 family proteins.

Levin M, Davies AM, Liljekvist M, Carlsson F, Gould HJ, Sutton BJ, Ohlin M - Clin. Exp. Allergy (2014)

Bottom Line: The interaction between IgE and allergen is a key event at the initiation of an allergic response, and its characteristics have substantial effects on the clinical manifestation.We here display the usefulness of allergen-specific human monoclonal IgE as a tool in studies of the crucial molecular interaction taking place at the initiation of an allergic response.Such studies may aid us in development of better diagnostic tools and guide us in the development of new therapeutic compounds.

View Article: PubMed Central - PubMed

Affiliation: Department of Immunotechnology, Lund University, Lund, Sweden.

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Binding specificity of novel scFv selected on Bet v 1 as determined by phage-ELISA on a panel of different allergens and BSA. All scFv are highly Bet v 1-specific and show no detectable cross-reactivity. All samples were run in duplicate.
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fig01: Binding specificity of novel scFv selected on Bet v 1 as determined by phage-ELISA on a panel of different allergens and BSA. All scFv are highly Bet v 1-specific and show no detectable cross-reactivity. All samples were run in duplicate.

Mentions: To enable characterization of molecular interactions between antibody fragments with origin in the human IgE repertoire and the major birch pollen Bet v 1, we performed phage display selections on the three Bet v 1 isoforms Bet v 1.0101, Bet v 1.0102 and Bet v 1.0112 from an antibody fragment library created from atopic donors. The library was created from transcripts encoding the VH domain of IgE isolated from nasal tissue of two allergic subjects known to have an IgE repertoire overrepresented by antibodies derived from the IGHV5 gene subgroup 4. These selections generated four novel-specific binders (B10, B13, B14 and M0418). Three binders, B10, B13 and B14, were isolated by selection on the major isoform Bet v 1.0101, while selection on isoform Bet v 1.0102 generated one additional binder (M0418) together with re-isolation of binder B14. Selections performed on isoform Bet v 1.0112 failed to generate any binders. All isolated scFv were highly Bet v 1-specific, showing no cross-reactivity to a panel of unrelated allergens (Fig.1).


Human IgE against the major allergen Bet v 1--defining an epitope with limited cross-reactivity between different PR-10 family proteins.

Levin M, Davies AM, Liljekvist M, Carlsson F, Gould HJ, Sutton BJ, Ohlin M - Clin. Exp. Allergy (2014)

Binding specificity of novel scFv selected on Bet v 1 as determined by phage-ELISA on a panel of different allergens and BSA. All scFv are highly Bet v 1-specific and show no detectable cross-reactivity. All samples were run in duplicate.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4215112&req=5

fig01: Binding specificity of novel scFv selected on Bet v 1 as determined by phage-ELISA on a panel of different allergens and BSA. All scFv are highly Bet v 1-specific and show no detectable cross-reactivity. All samples were run in duplicate.
Mentions: To enable characterization of molecular interactions between antibody fragments with origin in the human IgE repertoire and the major birch pollen Bet v 1, we performed phage display selections on the three Bet v 1 isoforms Bet v 1.0101, Bet v 1.0102 and Bet v 1.0112 from an antibody fragment library created from atopic donors. The library was created from transcripts encoding the VH domain of IgE isolated from nasal tissue of two allergic subjects known to have an IgE repertoire overrepresented by antibodies derived from the IGHV5 gene subgroup 4. These selections generated four novel-specific binders (B10, B13, B14 and M0418). Three binders, B10, B13 and B14, were isolated by selection on the major isoform Bet v 1.0101, while selection on isoform Bet v 1.0102 generated one additional binder (M0418) together with re-isolation of binder B14. Selections performed on isoform Bet v 1.0112 failed to generate any binders. All isolated scFv were highly Bet v 1-specific, showing no cross-reactivity to a panel of unrelated allergens (Fig.1).

Bottom Line: The interaction between IgE and allergen is a key event at the initiation of an allergic response, and its characteristics have substantial effects on the clinical manifestation.We here display the usefulness of allergen-specific human monoclonal IgE as a tool in studies of the crucial molecular interaction taking place at the initiation of an allergic response.Such studies may aid us in development of better diagnostic tools and guide us in the development of new therapeutic compounds.

View Article: PubMed Central - PubMed

Affiliation: Department of Immunotechnology, Lund University, Lund, Sweden.

Show MeSH