Anti-IgE monoclonal antibodies directed at the Fcϵ receptor binding site

Michal Baniyash*, Marilyn Kehry, Z. Eshhar

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

25 Scopus citations

Abstract

In a search for the region in the IgE molecule, which is recognized by the Fcε{lunate} receptor (Fcε{lunate}R) on mast cells and basophils, we have generated and characterized anti-IgE monoclonal antibodies (MAbs). The novel rat anti-mouse IgE MAb described herein (denoted 84-1c) interacts with an antigenic determinant which is associated with the Fcε{lunate}R recognition site on the IgE molecule. The MAb can bind to the Fcε{lunate} of IgE and block its binding to rat basophil leukemia (RBL) cells. The epitope recognized by 84-lc MAb was completely masked by the Fcε{lunate}R either in its cellular or soluble form. This epitope was dependent on the native conformation of the IgE molecule and differed from the ones that were recognized by the anti-IgE MAbs we described before.

Original languageAmerican English
Pages (from-to)705-711
Number of pages7
JournalMolecular Immunology
Volume25
Issue number8
DOIs
StatePublished - Aug 1988
Externally publishedYes

Bibliographical note

Funding Information:
Ackno~led~ement.r--Wea re gratefult o G. Frank for tech-nical assistancea nd MS E. Gross for excellent secretarial work. This study was supported in part by the Minerva Fund. Z. Eshhar is incumbent of Marshall and Renette Ezralow Chair in Chemical and Cellular Immunology.

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