Journal article icon

Journal article

TRIM5α restricts poxviruses and is antagonized by CypA and viral protein C6

Abstract:
Human tripartite motif protein 5a (TRIM5α) is a well-characterised restriction factor for some RNA viruses including HIV, but against DNA viruses reports are limited. Here, we demonstrate TRIM5α also restricts orthopoxviruses and, via its SPRY domain, binds the orthopoxvirus capsid protein L3 to diminish virus replication and activate innate immunity. In response, several orthopoxviruses, including vaccinia, rabbitpox, cowpox, monkeypox, camelpox and variola viruses, deploy countermeasures. First, protein C6 binds to TRIM5 via the RING domain to induce its proteasome-dependent degradation. Second, cyclophilin A (CypA) is recruited via interaction with capsid protein L3 to virus factories and virions to antagonise TRIM5α, and this interaction is prevented by cyclosporine A (CsA) and non-immunosuppressive derivatives alisporivir and NIM811. Both the proviral effect of CypA and antiviral effect of CsA are TRIM5α-dependent. CsA, alisporivir and NIM811 have antiviral activity against orthopoxviruses and since these drugs target a cellular protein, CypA, emergence of virus drug resistance is difficult. These results warrant testing of CsA derivatives against orthopoxviruses including monkeypox and variola.
Publication status:
Published
Peer review status:
Peer reviewed

Actions


Access Document


Publisher copy:
10.1038/s41586-023-06401-0

Authors


More by this author
Division:
MSD
Role:
Author


Publisher:
Springer Nature
Journal:
Nature More from this journal
Volume:
620
Pages:
873-880
Publication date:
2023-08-09
Acceptance date:
2023-07-04
DOI:
EISSN:
1476-4687
ISSN:
0028-0836


Language:
English
Keywords:
Pubs id:
1495351
Local pid:
pubs:1495351
Deposit date:
2023-07-24

Terms of use



Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP