Macrocycle-based PROTACs selectively degrade cyclophilin A and inhibit HIV-1 and HCV.

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Tác giả: Dara Annett, Riccardo Zenezini Chiozzi, Alessio Ciulli, Clara Gathmann, Morten L Govasli, Thomas W Hornsby, Clare Jolly, Kate L Morling, Lydia S Newton, Ann-Kathrin Reuschl, Sophie Ridewood, David L Selwood, Robert J Smith, Ying Ying Tan, Konstantinos Thalassinos, Lucy G Thorne, Greg J Towers, Andre J Wijaya

Ngôn ngữ: eng

Ký hiệu phân loại: 553.453 Tin

Thông tin xuất bản: England : Nature communications , 2025

Mô tả vật lý:

Bộ sưu tập: NCBI

ID: 48911

Targeting host proteins that are crucial for viral replication offers a promising antiviral strategy. We have designed and characterised antiviral PROteolysis TArgeting Chimeras (PROTACs) targeting the human protein cyclophilin A (CypA), a host cofactor for unrelated viruses including human immunodeficiency virus (HIV) and hepatitis C virus (HCV). The PROTAC warheads are based on fully synthetic macrocycles derived from sanglifehrin A, which are structurally different from the classical Cyp inhibitor, cyclosporine A. Our Cyp-PROTACs decrease CypA levels in cell lines and primary human cells and have high specificity for CypA confirmed by proteomics experiments. Critically, CypA degradation facilitates improved antiviral activity against HIV-1 in primary human CD4+ T cells compared to the non-PROTAC parental inhibitor, at limiting inhibitor concentrations. Similarly, we observe antiviral activity against HCV replicon in a hepatoma cell line. We propose that CypA-targeting PROTACs inhibit viral replication potently and anticipate reduced evolution of viral resistance and broad efficacy against unrelated viruses. Furthermore, they provide powerful tools for probing cyclophilin biology.
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