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RI1
Department of Microbiology and Immunology, Virginia Commonwealth University, Richmond, VA 23298
The low affinity receptor for IgE (Fc
RII/CD23) has previously
been shown to interact with IgE with a dual affinity. Three chimeric
constructs were created containing the lectin domain (amino acids
172–188) or the "neck" and lectin domain (amino acids 157–188)
attached to subunits of oligomeric proteins. All chimeras were
incapable of interacting with IgE with either a high or low affinity,
indicating that the 
-helical stalk of CD23 is important for
orienting the lectin heads such that an interaction with IgE can occur.
This concept received further support in that a chimeric CD23 composed
of the human CD23 stalk and the mouse CD23 lectin head bound mouse IgE
with a dual affinity, but could only bind rat IgE with a low affinity.
Effort was next concentrated on a construct consisting of the entire
extracellular (EC) region of CD23. A mutation to the first cleavage
site of CD23 (C1M) resulted in a more stable molecule as determined by
a decrease of soluble CD23 release. A soluble chimeric EC-C1M was
prepared by attaching an isoleucine zipper to the amino terminus
(lzEC-C1M). The interaction with IgE by
lzEC-C1M was found to be superior to that seen with
EC-CD23. The lzEC-C1M could inhibit binding of IgE to
both CD23 and the high affinity receptor for IgE, FcRI, providing
further evidence for a strong interaction with IgE. FcRI inhibition
(
70%) was seen at equimolar concentrations of
lzEC-C1M, implying the effectiveness of this chimera and
suggesting its potential therapeutic value.
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