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Why is it so hard to dissociate multivalent antigens from cell-surface antibodies?
1Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, NM 87545, USA. bxg@t10.lanl.gov
Immunology Today
|February 1, 1996
Summary
Dissociating multivalent antigens bound by surface-associated immunoglobulin (sIg) is challenging. A cellular response from sIg crosslinking, potentially involving receptor desensitization, makes antigens resistant to dissociation.
Area of Science:
- Immunology
- Cellular Biology
- Biochemistry
Background:
- Surface-associated immunoglobulin (sIg) binds multivalent antigens to cell surfaces.
- Dissociating these bound antigens is often difficult, even with high concentrations of monovalent haptens.
Purpose of the Study:
- To discuss evidence explaining the difficulty in dissociating multivalent antigens bound by sIg.
- To propose a mechanism for the transition of antigens to a dissociation-resistant state.
Main Methods:
- Review of existing evidence regarding antigen-sIg interactions.
- Theoretical discussion of cellular responses and receptor dynamics.
Main Results:
- Evidence suggests a cellular response triggered by sIg crosslinking contributes to antigen binding resistance.
- Multivalent antigens may transition to a dissociation-resistant state via receptor desensitization.
Conclusions:
- Cellular responses, specifically sIg crosslinking, play a critical role in antigen-antibody interactions.
- Receptor desensitization is a proposed mechanism underlying antigen-antibody dissociation resistance.