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Distorted Immunodominance by Linker Sequences or other Epitopes from a Second Protein Antigen During
AeRyon Kim1, Tatiana N Boronina2, Robert N Cole2
1Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Scientific Reports
|April 20, 2017
Summary
Immunodominance hierarchies can shift when multiple proteins are processed together. Tags and spacers can interfere with identifying key immune epitopes, impacting vaccine development.
Area of Science:
- Immunology
- Protein Biochemistry
- Vaccine Development
Background:
- The immune system targets a limited number of immunodominant epitopes from pathogens.
- Understanding the factors governing immunodominance is challenging due to complex antigen processing.
Purpose of the Study:
- To identify the determinants of immunodominance.
- To investigate how simultaneous processing of multiple proteins affects immunodominance hierarchies.
- To assess the impact of purification tags/spacers on epitope presentation.
Main Methods:
- Utilized a cell-free antigen processing system to determine epitope hierarchies.
- Validated findings in vivo using mouse and human models.
- Analyzed the effect of co-processed proteins and purification tags on immunodominance.
Main Results:
- Immunodominance hierarchies of known epitopes can change when proteins are processed concurrently.
- Purification tags and spacers can unexpectedly alter the presentation of physiologically relevant immunodominant epitopes.
- Co-processing of proteins influences the resulting epitope landscape.
Conclusions:
- Simultaneous protein processing significantly impacts immunodominance.
- Purification tags/spacers can be detrimental to identifying and presenting critical epitopes for vaccination.
- Recommend removing tags/spacers from candidate vaccines to ensure presentation of physiological epitopes.
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