Abstract:
:In this paper we demonstrate that phage display technology is a suitable system for studying the interaction between the high-affinity receptor for IgE (Fc epsilon RI) and IgE. The alpha subunit extracellular domains of the human receptor were expressed on the surface of filamentous phage M13 fused to the carboxyl-terminal part of the gene III protein (pIII). Two constructs were made, the first with both the Ig-like domains of the receptor alpha chain and the second with only the C-terminal domain. The fusion genes were cloned in a phagemid vector to display monovalently the receptor on the phage surface. Our results indicate that the alpha receptor expressed on the phage is able to interact with IgE as demonstrated by an ELISA assay. In addition, by using the same system, we show that a single domain of the alpha receptor is sufficient for the interaction with IgE although with a binding affinity lower than that of the two-domain receptor.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Scarselli E,Esposito G,Traboni Cdoi
10.1016/0014-5793(93)80226-ksubject
Has Abstractpub_date
1993-08-23 00:00:00pages
223-6issue
1-2eissn
0014-5793issn
1873-3468pii
0014-5793(93)80226-Kjournal_volume
329pub_type
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