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Structural Basis for Antibody Neutralization of Pertussis Toxin
Jory A Goldsmith1, Annalee W Nguyen2, Rebecca E Wilen2
1Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA 78712.
Biorxiv : the Preprint Server for Biology
|October 10, 2024
Summary
Structural analysis of pertussis toxin (PT) reveals key neutralizing epitopes. This research defines how antibodies block toxin adhesion and activity, crucial for developing improved vaccines against Bordetella pertussis.
Area of Science:
- Immunology
- Structural Biology
- Microbiology
Background:
- Pertussis toxin (PT) is a critical antigen for immunity against Bordetella pertussis.
- Understanding PT-neutralizing epitopes is vital for vaccine development, but none have been structurally characterized.
- No previous studies have structurally defined PT-neutralizing epitopes.
Purpose of the Study:
- To structurally define neutralizing epitopes on PT.
- To identify key structural elements for PT antigen design.
- To elucidate the mechanisms of PT neutralization by antibodies.
Main Methods:
- Determined cryo-electron microscopy structure of detoxified PT (PTg) bound to neutralizing antibodies hu11E6 and hu1B7.
- Utilized high-throughput glycan array analysis to assess antibody-mediated inhibition of PT binding.
- Performed T cell activation assays to evaluate antibody effects on PT mitogenic activities.
Main Results:
- Structurally defined neutralizing epitopes for hu11E6 and hu1B7 antibodies.
- Hu11E6 binds conserved epitopes on S2 and S3 subunits, preventing PTg binding to sialylated N-glycans and blocking mitogenic activity.
- Hu1B7 binds a quaternary epitope on S1 and S5 subunits, though S5 binding is not essential for neutralization.
Conclusions:
- First structural characterization of PT-neutralizing epitopes.
- Provides molecular insights into immune protection against B. pertussis.
- Offers critical information for designing future PT-based immunogens.
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