Scholarlink

<p>Crimean–Congo haemorrhagic fever virus (CCHFV) is a highly pathogenic member of the <i>Nairoviridae</i> 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.</p>

错误：搜索内容不能为空，请输入英文关键词
错误：关键词超出字数限制，请精简
高级检索

Structure of Crimean–Congo haemorrhagic fever virus RNA polymerase

  • 期刊论文

  • 发表日期：

    2026年4月16日

查看全文
  • Dong Wang,
  • Ge Yang,
  • Bin Liu

摘要

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.