Antigen Interaction and Heat Inactivation Expose New Epitopes on Human IgE Journal Articles

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abstract

It is well established that heat–denatured IgE is no longer capable of binding to FcεRI. We have found an antibody that interacts with heat–denatured IgE. Interestingly, this antibody can also be used to detect some serum IgE, but not IgE synthesized de novo in vitro. However, native IgE can be transformed into an IgE that is recognized by this antibody, if antigen is added. Our data indicate that physiological mechanisms exist that biologically inactivate IgE which might still be mistaken for 'functional' IgE by assays based on polyclonal antibodies.

authors

Stampfli, Martin R
Pachlopnik, Jana M
Stämpfli, Martin R
Rudolf, Michael P
Aebischer, Iwan
Kricek, Franz
Miescher, Sylvia
Stadler, Beda M

status

published

publication date

1998

has subject area

1107 Immunology (FoR)
Allergy (Science Metrix)
Animals (MeSH)
Antibodies (MeSH)
Antibodies, Monoclonal (MeSH)
Antibody Specificity (MeSH)
Antigen-Antibody Reactions (MeSH)
Enzyme-Linked Immunosorbent Assay (MeSH)
Epitopes (MeSH)
Hot Temperature (MeSH)
Humans (MeSH)
Immunoassay (MeSH)
Immunodominant Epitopes (MeSH)
Immunoglobulin E (MeSH)
Leukocytes, Mononuclear (MeSH)
Mice (MeSH)
Multiple Myeloma (MeSH)
Protein Denaturation (MeSH)
Protein Structure, Tertiary (MeSH)
Receptors, IgE (MeSH)
Recombinant Fusion Proteins (MeSH)

published in

International Archives of Allergy and Immunology Journal