0573932 - ÚOCHB 2024 RIV DE eng J - Článek v odborném periodiku
Duchoslav, Vojtěch - Bouřa, Evžen
Structure of monkeypox virus poxin: implications for drug design.
Archives of Virology. Roč. 168, č. 7 (2023), č. článku 192. ISSN 0304-8608. E-ISSN 1432-8798
Grant CEP: GA MŠMT(CZ) LX22NPO5103
Grant ostatní: AV ČR(CZ) StrategieAV21/25
Program: StrategieAV
Výzkumná infrastruktura: CIISB III - 90242
Institucionální podpora: RVO:61388963
Klíčová slova: virus * poxin * nuclease * crystal structure
Obor OECD: Virology
Impakt faktor: 2.7, rok: 2022
Způsob publikování: Open access
https://doi.org/10.1007/s00705-023-05824-4

Monkeypox, or mpox, is a disease that has recently resurfaced and spread across the globe. Despite the availability of an FDA-approved vaccine (JYNNEOS) and an effective drug (tecovirimat), concerns remain over the possible recurrence of a viral pandemic. Like any other virus, mpox virus must overcome the immune system to replicate. Viruses have evolved various strategies to overcome both innate and adaptive immunity. Poxviruses possess an unusual nuclease, poxin, which cleaves 2'-3'-cGAMP, a cyclic dinucleotide, which is an important second messenger in the cGAS-STING signaling pathway. Here, we present the crystal structure of mpox poxin. The structure reveals a conserved, predominantly β-sheet fold and highlights the high conservation of the cGAMP binding site and of the catalytic residues His17, Tyr138, and Lys142. This research suggests that poxin inhibitors could be effective against multiple poxviruses.
Trvalý link: https://hdl.handle.net/11104/0344320


Vědecká data: PDB