Structure of Crimean–Congo haemorrhagic fever virus RNA polymerase

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Abstract
Crimean–Congo haemorrhagic fever virus (CCHFV) is a highly pathogenic member of the Nairoviridae and causes severe disease with high fatality rates. Currently, there are no approved antivirals for CCHFV, but resolving the structure of its RNA-dependent RNA polymerase, termed L protein, could help drug development. Here we report cryogenic electron microscopy structures of the CCHFV L protein in both apo and RNA-bound states at 2.62 Å and 2.53 Å, respectively. These structures define the molecular architecture of the PA-, PB1- and PB2-like domains within the polymerase core, elucidate the mechanism of promoter recognition and reveal RNA-induced conformational changes that stabilize catalytic elements. Together, these insights provide a structural framework for understanding nairovirus replication and enable structure-based development of polymerase inhibitors.
Funding Information
  • The Hormel Institute, University of Minnesota

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