Protein Antigens: The Molecular Bases of Antigenicity and Immunogenicity
The Antigens, Page: 1-78
1974
- 44Citations
- 16Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations44
- Citation Indexes44
- CrossRef44
- Captures16
- Readers16
- 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.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/B9780126355024500084; http://dx.doi.org/10.1016/b978-0-12-635502-4.50008-4; https://linkinghub.elsevier.com/retrieve/pii/B9780126355024500084; http://linkinghub.elsevier.com/retrieve/pii/B9780126355024500084; http://api.elsevier.com/content/article/PII:B9780126355024500084?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:B9780126355024500084?httpAccept=text/plain; https://dx.doi.org/10.1016/b978-0-12-635502-4.50008-4
Elsevier BV
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