Journal
EMBO JOURNAL
Volume 40, Issue 5, Pages -Publisher
WILEY
DOI: 10.15252/embj.2020106228
Keywords
antibody; non‐ neutralising; nucleoprotein; TRIM21; virus
Categories
Funding
- MRC (UK) [U105181010]
- Wellcome Trust Investigator Award [200594/Z/16/Z]
- Wellcome Trust Clinical Research Career Development Fellowship
- Research Council of Norway through its Centre of Excellence funding scheme [179573]
- South-Eastern Norway project [40018]
- [230526/F20]
- [251037/F20]
- Wellcome Trust [200594/Z/16/Z] Funding Source: Wellcome Trust
- MRC [MC_U105181010] Funding Source: UKRI
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The study revealed a new mechanism of immune protection mediated by anti-N antibodies through cytosolic Fc receptor and TRIM21. These antibodies target N for degradation and generate CTLs, facilitating efficient viral clearance. This highlights the importance of N as a vaccine target and the synergy between antibodies and T cells in immunity.
Nucleoprotein (N) is an immunodominant antigen in many enveloped virus infections. While the diagnostic value of anti-N antibodies is clear, their role in immunity is not. This is because while they are non-neutralising, they somehow clear infection by coronavirus, influenza and LCMV in vivo. Here, we show that anti-N immune protection is mediated by the cytosolic Fc receptor and E3 ubiquitin ligase TRIM21. Exploiting LCMV as a model system, we demonstrate that TRIM21 uses anti-N antibodies to target N for cytosolic degradation and generate cytotoxic T cells (CTLs) against N peptide. These CTLs rapidly eliminate N-peptide-displaying cells and drive efficient viral clearance. These results reveal a new mechanism of immune synergy between antibodies and T cells and highlights N as an important vaccine target.
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