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Receptor phage
Author(s) -
Scarselli Elisa,
Esposito Gloria,
Traboni Cinzia
Publication year - 1993
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(93)80226-k
Subject(s) - chemistry , computational biology , microbiology and biotechnology , biology
In this paper we demonstrate that phage display technology is a suitable system for studying the interaction between the high‐affinity receptor for IgE (FcϵRI) and IgE. The α subunit extracellular domains of the human receptor were expressed on the surface of filamentous phage M 13 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 α 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 α 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 α receptor is sufficient for the interaction with IgE although with a binding affinity lower than that of the two‐domain receptor.