AI Article Synopsis
- The immune system primarily targets a few specific epitopes from pathogens, but determining what makes these epitopes immunodominant is complex.
- Researchers used a cell-free system to identify factors influencing immunodominance among dominant epitopes and tested their findings in both mice and humans.
- They discovered that introducing spacer/tag sequences during protein purification can interfere with the recognition of important epitopes, advising against their use in vaccine candidates or recommending their removal before vaccination.
Article Abstract
The immune system focuses on and responds to very few representative immunodominant epitopes from pathogenic insults. However, due to the complexity of the antigen processing, understanding the parameters that lead to immunodominance has proved difficult. In an attempt to uncover the determinants of immunodominance among several dominant epitopes, we utilized a cell free antigen processing system and allowed the system to identify the hierarchies among potential determinants. We then tested the results in vivo; in mice and in human. We report here, that immunodominance of known sequences in a given protein can change if two or more proteins are being processed and presented simultaneously. Surprisingly, we find that new spacer/tag sequences commonly added to proteins for purification purposes can distort the capture of the physiological immunodominant epitopes. We warn against adding tags and spacers to candidate vaccines, or recommend cleaving it off before using for vaccination.
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|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5396073 | PMC |
| http://dx.doi.org/10.1038/srep46418 | DOI Listing |
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