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Protein Antigens: The Molecular Bases of Antigenicity and Immunogenicity

The Antigens, Page: 1-78
1974
  • 44
    Citations
  • 0
    Usage
  • 16
    Captures
  • 0
    Mentions
  • 0
    Social Media
Metric Options:   Counts1 Year3 Year

Metrics Details

  • Citations
    44
    • Citation Indexes
      44
      • CrossRef
        44
  • Captures
    16

Book Chapter Description

This chapter discusses the relationships between the molecular structures of proteins and their capacities to induce cellular and humoral immune responses—immunogenicity, and to interact with the antibodies formed—antigenicity. The role of phylogeny—degree of foreignness—in determining immunogenicity and, thereby, antigenicity has been emphasized, as also has the role played by the conformation of the protein. In general antibodies are formed only against those areas of the surface of the protein immunogen that differ from that of the homologous protein of the immunized animal. It appears that an inverse relationship exists between proteins' capacities to induce cellular and humoral responses, and that unfolded—denatured—proteins, for example, myelin and acetoacetylated flagellin induce cellular immunity preferentially. These effects are most probably mediated by the less stringent structural requirements—size and/ or conformation of the antigenic determinants—for interaction with cell-bound antibodies compared with circulating antibodies. Thus, whereas the native and denatured states of a protein cross-react with cell-bound antibodies, no cross-reaction is usually detected with humoral antibodies.

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