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Immune response to a molecularly defined internal image idiotope
W V Williams1, S D London, D B Weiner
1Department of Pathology, University of Pennsylvania, Philadelphia 19104.
Journal of Immunology (Baltimore, Md. : 1950)
|June 15, 1989
Summary
Synthetic peptides mimicking reovirus hemagglutinin (HA3) were used to study immune responses. Antibodies targeting these peptides neutralized reovirus, revealing insights into antibody structure and immune regulation.
Area of Science:
- Immunology
- Structural Biology
- Virology
Background:
- A monoclonal antibody, 87.92.6, mimics the reovirus type 3 hemagglutinin (HA3) binding site.
- Sequence similarity exists between the antibody's variable regions and a determinant on HA3.
Purpose of the Study:
- To investigate the immunologic significance of sequence similarity between an anti-idiotope antibody and reovirus HA3.
- To explore the role of specific peptide fragments in eliciting immune responses and cross-reactivity.
Main Methods:
- Synthesis of VH, VL, and Reo peptides based on antibody and viral sequences.
- Testing antibody neutralization of reovirus infectivity using these peptides.
- Assessing immunogenicity and lymphocyte proliferation responses to peptides.
- Evaluating delayed-type hypersensitivity and cytotoxic lymphocyte activity.
Main Results:
- Antibodies against Reo or VL peptides neutralized reovirus type 3.
- VH and VL peptides required linkage (VH-VL) to elicit antibodies, while Reo peptide was immunogenic alone.
- VH peptide contained a T-helper cell determinant, and VL peptide elicited reovirus-specific delayed-type hypersensitivity.
- Cytolytic lymphocytes lysed targets coated with VH-VL peptide, but not individual VH or VL peptides.
Conclusions:
- Immune cross-reactivity between external antigens and internal image antibodies can be explained by primary structural similarities.
- These findings have implications for understanding autoantibody development, immune network interactions, and immune response regulation.