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Polyclonal antisera elicited bý lysozymes: insights into antigenic structure and evolution
1Division of Biochemistry and Molecular Biology, University of California, Berkeley 94720-3202, USA.
EXS
|January 1, 1996
Summary
Polyclonal antisera revealed that most of a protein's surface is antigenic. Immunological distances correlate with amino acid changes, aiding evolutionary relationship and time scale inferences.
Area of Science:
- Immunology
- Molecular Evolution
- Protein Biochemistry
Background:
- The multideterminant-regulatory model explains the antigenic structure of globular proteins.
- Evolutionary studies of bird lysozymes c provided key insights into protein antigenicity.
Purpose of the Study:
- To review evidence supporting the multideterminant-regulatory model.
- To demonstrate the correlation between immunological differences and amino acid sequence differences.
- To highlight the utility of immunological distances in inferring evolutionary relationships.
Main Methods:
- Analysis of polyclonal antisera elicited by evolutionary variants of bird lysozymes c.
- Examination of antigenic properties of lysozyme c and other globular proteins.
- Calculation of immunological distances and comparison with amino acid sequence data.
Main Results:
- The entire surface of globular proteins is largely antigenic.
- Nearly all evolutionary substitutions impact immunological cross-reactivity.
- Immunological distances provide a reliable method for inferring genealogical relationships and evolutionary timescales.
Conclusions:
- Polyclonal antisera are valuable tools for understanding protein evolution and antigenicity.
- Immunological data strongly correlate with molecular evolutionary changes.
- Immunological distances offer a robust approach for reconstructing evolutionary histories.
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