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Immunological activity of the peptidoglycan
Zeitschrift Fur Immunitatsforschung, Experimentelle Und Klinische Immunologie
|July 1, 1975
Summary
Rabbit antisera against Group A-variant streptococci are rich in peptidoglycan antibodies. The C-terminal D-Ala-D-Ala of pentapeptides is the main immunodominant site, with bacterial peptidoglycans showing immunological cross-reactivity.
Area of Science:
- Immunology
- Microbial Biochemistry
Background:
- Peptidoglycan (PG) antibody studies were advanced by high concentrations found in rabbit Group A-variant streptococcal antisera.
- Purified PG from streptococcal cell walls was previously a poor antigen, though both its polymer and peptide components are antigenic.
Purpose of the Study:
- To determine the immunodominant site of peptidoglycan.
- To investigate the immunological cross-reactivity of bacterial peptidoglycans.
Main Methods:
- Quantitative precipitin studies using rabbit antisera.
- Solid-phase synthesis of pentapeptides for fine structure analysis of the immunodominant site.
Main Results:
- Group A-variant streptococcal immunization yielded significantly higher PG antibody concentrations compared to Group A or C streptococci.
- The C-terminal D-Ala-D-Ala sequence of synthesized pentapeptides was identified as the immunodominant determinant.
- Immunological cross-reactivity was confirmed among peptidoglycans from various bacterial species.
Conclusions:
- The immunochemistry of peptidoglycans is well-established, providing a foundation for further research.
- The constant exposure to ubiquitous bacterial peptidoglycans suggests continuous immune system stimulation.
- The medical and biological significance of peptidoglycan antibodies warrants further investigation.