# MODULATION OF IMMUNE RESPONSE BY PROTEIN FRAGMENTS

> **NIH NIH R01** · UNIVERSITY OF CINCINNATI · 1987 · $137,299

## Abstract

This study attempts to elucidate the relationship between the structural
and immunological properties of substructures of a complex protein
molecule, Bovine Serum Albumin (BSA), and provide information on how the
immune system recognizes and responds to such molecule.  Highly purified
fragments of BSA have been isolated and have been shown to be poorly
immunogenic but highly immunomodulating.  The individual antigenic
fragments carry unique determinants not shared with other fragments.  A
single antigenic fragment, however, has the capacity to suppress immuno
response to the entire BSA molecule which seem to indicate that the
regulation of immunosuppression is not dependent on serological
determinants but on some other presently unknown property of the fragment.
To further characterize distinct epitopes monoclonal antibodies to defined
antigenic fragments using hybridoma technology will be used.  These
antibodies will be a source for investigating cross-reactivity of
idiotypes.  We shall also attempt to clarify the relationship between
idiotypic and antigenic effects and specify at which cell level epitopes or
idiotypes influence immune response to BSA molecule.

## Key facts

- **NIH application ID:** 3126225
- **Project number:** 5R01AI015520-08
- **Recipient organization:** UNIVERSITY OF CINCINNATI
- **SAM.gov UEI:** DZ4YCZ3QSPR5
- **Principal Investigator:** GABRIEL G MICHAEL
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1987
- **Award amount:** $137,299
- **Award type:** 5
- **Project period:** 1979-09-15 → 1989-04-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3126225

## Citation

> US National Institutes of Health, RePORTER application 3126225, MODULATION OF IMMUNE RESPONSE BY PROTEIN FRAGMENTS (5R01AI015520-08). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3126225. Licensed CC0.

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