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2017 ; 7
(ä): 46418
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Distorted Immunodominance by Linker Sequences or other Epitopes from a Second
Protein Antigen During Antigen-Processing
#MMPMID28422163
Kim A
; Boronina TN
; Cole RN
; Darrah E
; Sadegh-Nasseri S
Sci Rep
2017[Apr]; 7
(ä): 46418
PMID28422163
show ga
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.