# CHEMISTRY AND IMMUNOLOGY OF STREPTOCOCCAL M PROTEIN

> **NIH NIH R01** · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · 1990 · $235,625

## Abstract

The aim of this research is to develop a safe and effective multivalent
vaccine against strains of group A streptococci that trigger acute
rheumatic fever and rheumatic heart disease.  For this purpose, the
chemistry and immunology of the protective as opposed to heart
cross-reactive epitopes of streptococcal M protein will be studied in
detail.  Specific efforts will be directed toward:  (1) identifying the
protective M protein epitopes predominating among strains of group A
streptococci collected from populations in which attacks of rheumatic fever
remain high, (2) isolating, purifying and immunochemically analyzing M
protein polypeptide fragments for protective and heart cross-reactive
epitopes, (3) determining the covalent structure of the aminoterminal and
common protective regions of relevant M proteins, (4) synthesizing peptide
copies of the amino-terminal regions of selected M proteins, and testing
the protective and heart cross-reactive immunogenicity of the peptides
conjugated to various carriers in laboratory animals, (5) synthesizing and
analyzing tandem hybrids of peptides containing protective epitopes of
different M serotypes, and (6) carefully testing the immunogenicity of
selected pep M proteins and synthetic peptides as guided by the foregoing
studies in human volunteers.  The predominant protective epitopes will be
determined by M typing, opsonophagocytic and mouse protection tests, and
Southern hybridization of the DNA of streptococcal strains with probes
prepared from the structural genes encoding M protein under varying
conditions of stringency.  Purified peptic extracts of rheumatogenic
streptococci will be tested for protective and heart cross-reactive
immunogenicity in rabbits and mice.  The covalent structures of the
amino-terminus of the relevant M proteins will be determined by automated
sequence analysis.  Overlapping peptides will be synthesized, conjugated to
various carriers, including pepM24, which has been shown to be devoid of
heart cross-reactive epitopes, and tested for type-specific, cross
protective and tissue-cross-reactive immunogenicity.  Some of the peptides
from different M serotypes will be synthesized in tandem in an attempt to
produce multivalent hybrid peptides with protective immunogenicity against
many serotypes of streptococci.  Based on the results obtained in the
foregoing studies, the synthetic peptides will be carefully evaluated in
humans for protective immunogenicity.  These studies should provide
fundamental information on the chemistry and immunology of M protein as
they relate to protective immunity against rheumatogenic streptococci.

## Key facts

- **NIH application ID:** 3124637
- **Project number:** 5R01AI010085-27
- **Recipient organization:** UNIVERSITY OF TENNESSEE HEALTH SCI CTR
- **SAM.gov UEI:** X1M1PN3KG3E7
- **Principal Investigator:** EDWIN H. BEACHEY
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1990
- **Award amount:** $235,625
- **Award type:** 5
- **Project period:** 1976-09-01 → 1991-08-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/3124637

## Citation

> US National Institutes of Health, RePORTER application 3124637, CHEMISTRY AND IMMUNOLOGY OF STREPTOCOCCAL M PROTEIN (5R01AI010085-27). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/3124637. Licensed CC0.

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