# STRUCTURE-FUNCTION RELATIONSHIPS OF THE IGE RECEPTOR

> **NIH NIH R01** · CORNELL UNIVERSITY · 1990 · $168,259

## Abstract

The work proposed continues the systematic analysis of the three-
dimensional structure of the immunoglobulin E (IgE) -receptor
complex, its interactions with other cellular components, and the
mechanism by which it transmits a signal across the plasma
membrane of mast cells and basophils to trigger degranulation in
allergic responses.  The structural map will be extended by
measurements of resonance energy transfer between well defined
sites on receptor-bound IgE and cytoplasmically exposed portions
of the receptor that are labeled by monoclonal antibodies.
Regions of IgE that are critical for its interaction with receptor
will be examined by genetic manipulation of the polypeptide
chains.  Genetic methods will also be used to introduce specific
cysteine residues for fluorescent labeling such that energy
transfer measurements may be carried out to test the model that
IgE undergoes a conformation change upon binding.  In addition to
providing basic information knowledge of the IgE-receptor
interaction may be valuable in clinical treatments of allergies.

The interactions between receptors and other cellular components
that occur after lgE-receptor complexes have clustered in a
triggering configuration will be investigated by fluorescence
photobleaching recovery and electrodiffusion measurements of
the lateral mobility of fluorescently labeled monoclonal
antibodies that dimerize the receptors or are specific for a
partially characterized component that appears to associate with
receptors.  A procedure for measuring rotational mobility by
steady-state phosphorescence anisotropy will be developed such
that time-dependent changes in the receptor interactions may be
monitored under conditions where cell triggering occurs.  The
particular components that interact with the clustered receptors
will be characterized with the use of differential chemical
crosslinking, radioactive labeling and purification schemes.  The
participation of the cytoplasmically exposed parts of the receptor
in interactions with other cellular components during signal
transduction will be investigated by testing the competence of
lgE-receptor complexes with proteolyzed cytoplasmic portions
after reconstitution into intact cells and also by microinjection
into cells of the monoclonal antibodies specific for cytoplasmic
portions.  These studies should contribute new insights to
understanding the chain-of-events between antigen bridging of
lgE-receptor complexes on the cell surface and the degranulation
signal.

## Key facts

- **NIH application ID:** 3127829
- **Project number:** 5R01AI018306-10
- **Recipient organization:** CORNELL UNIVERSITY
- **SAM.gov UEI:** G56PUALJ3KT5
- **Principal Investigator:** Barbara A Baird
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1990
- **Award amount:** $168,259
- **Award type:** 5
- **Project period:** 1981-08-01 → 1992-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3127829

## Citation

> US National Institutes of Health, RePORTER application 3127829, STRUCTURE-FUNCTION RELATIONSHIPS OF THE IGE RECEPTOR (5R01AI018306-10). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3127829. Licensed CC0.

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