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Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
Epitope mapping of a function-blocking beta 1 integrin antibody by phage display
S T Ryan1, G Chi-Rosso, L L Bonnycastle
1Biogen, Inc., Cambridge, MA 02142, USA.
Cell Adhesion and Communication
|June 25, 1998
Summary
The anti-beta 1 integrin antibody Ha2/11 blocks integrin function by binding near the I domain. This antibody cross-reacts with multiple species, aiding research into beta 1 integrin roles.
Area of Science:
- Cell Biology
- Immunology
- Biochemistry
Background:
- Integrins are crucial cell surface receptors mediating cell-cell and cell-matrix interactions.
- Understanding integrin function is vital for various biological processes.
- Beta 1 integrins play significant roles in adhesion and signaling pathways.
Purpose of the Study:
- To characterize the function-blocking anti-rat beta 1 integrin antibody Ha2/11.
- To determine the cross-reactivity and epitope of Ha2/11.
- To elucidate the mechanism by which Ha2/11 inhibits beta 1 integrin function.
Main Methods:
- Phage display for epitope mapping.
- Monoclonal antibody mapping experiments.
- Mutational analyses and direct binding assays.
Main Results:
- Ha2/11 antibody cross-reacts with human, Xenopus, and Drosophila beta 1 integrins.
- The epitope for Ha2/11 was mapped to the sequence LRSGEPQTF, near the I domain.
- Ha2/11 interferes with I domain-mediated ligand binding, blocking beta 1 integrin function.
Conclusions:
- Ha2/11 is a versatile reagent for studying beta 1 integrin function across species.
- The antibody's mechanism of action involves inhibiting ligand binding via the I domain.
- These findings provide insights into integrin-ligand interactions and antibody-based functional blocking.
