# STRUCTURE/FUNCTION OF RAGWEED POLLEN ALLERGEN ANTIGEN E

> **NIH NIH R01** · UNIV OF NORTH CAROLINA CHAPEL HILL · 1990 · $120,902

## Abstract

Major projects in this laboratory are all designed to further our
understanding of allergens and to approach questions of
fundamental interest in immunology using well defined allergens
as a particularly relevant model.  Using selected ragweed and
grass pollen allergens isolated in this laboratory and elsewhere,
the proteins are being characterized structurally (amino acid
sequence analysis) and antigenically (by defining epitopes reactive
with human IgE).  The allergens currently under study include
short ragweed Ra5, Ra6, and antigen E.  From a series of grass
pollens, the Group I allergen is the model system chosen for
development.  In addition to these molecules which are isolated
from pollen in this laboratory, Western ragweed Ra5 (isolated
elsewhere) will be sequenced in order to compare it with short and
giant ragweed Ra5's whose structures have already been
established.

Monoclonal antibodies continue to be generated against allergens.
Many of these have potential use in standardizing allergen
extracts and many are useful in immunoassays for identifying
epitopes recognized by human IgE and IgG antibodies.  Currently,
the monoclonal antibodies in use in the laboratory are of murine
origin, but recent progress in using the Epstein Barr virus to
"immortalize" human antibody producing lymphocytes is
encouraging and will be pursued.

Acquisition of peptide synthesis capability adds a new dimension
to studies of allergen epitopes.  It is now possible to synthesize
particular peptides, immunize experimental animals with these,
and ascertain whether the immune serum reacts with the intact
allergen.

Finally, the ability to probe for and isolate the genes which code
for allergens will enable this laboratory to begin to use powerful
molecular biology approaches in the study of allergy and
allergens.  Enough is known about the structure of a number of
allergens to allow the design of oligonucleotide probes which will
anneal to genomic and cDNA libraries under construction.  The
family of monoclonal antibodies to these allergen allow isolation
of polysomes actively synthesizing particular allergens in in vitro
translation systems.  "Western" and "dot" blotting procedures
ensure that a particular message is present prior to synthesizing a
cDNA library for sequence analysis and placement into expression
vectors.

## Key facts

- **NIH application ID:** 3125915
- **Project number:** 5R01AI014908-12
- **Recipient organization:** UNIV OF NORTH CAROLINA CHAPEL HILL
- **SAM.gov UEI:** D3LHU66KBLD5
- **Principal Investigator:** DAVID G KLAPPER
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1990
- **Award amount:** $120,902
- **Award type:** 5
- **Project period:** 1978-08-01 → 1993-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3125915

## Citation

> US National Institutes of Health, RePORTER application 3125915, STRUCTURE/FUNCTION OF RAGWEED POLLEN ALLERGEN ANTIGEN E (5R01AI014908-12). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3125915. Licensed CC0.

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