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Updated: Jan 17, 2026

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
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Structure and function of the nairovirus cap-snatching endonuclease

Wenhua Kuang1, Zhenhua Tian1,2, Gan Zhang3

  • 1State Key Laboratory of Virology and Biosafety, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan 430207, Hubei, China.

Nucleic Acids Research
|January 14, 2026
PubMed

Insights

Structural and biochemical studies reveal a unique two-metal-ion mechanism in nairovirus endonuclease (EN) activity, crucial for viral transcription. These findings pave the way for developing novel antivirals targeting Crimean-Congo hemorrhagic fever virus (CCHFV).

Area of Science:

  • Virology
  • Structural Biology
  • Biochemistry

Background:

  • Nairoviruses, including CCHFV and KASV, are significant human pathogens.
  • The viral endonuclease (EN) domain is vital for transcription and a key antiviral target.
  • Structural and functional insights into nairovirus ENs are limited.

Purpose of the Study:

  • To elucidate the biochemical and structural mechanisms of CCHFV and KASV ENs.
  • To identify potential antiviral strategies targeting nairovirus replication.

Main Methods:

  • Biochemical assays to characterize RNA endonuclease activity.
  • Determination of crystal structures of CCHFV and KASV ENs in various states.
  • Functional assays to assess the role of the metal-ion binding mechanism.

Main Results:

  • Nairovirus EN activity is manganese-dependent and prefers uridine-rich RNA.
  • Three inhibitors (DPBA, L-742,001, BXA) were identified, with BXA showing highest potency.
  • Nine crystal structures revealed a unique two-metal-ion binding mode essential for transcription.

Conclusions:

  • The two-metal-ion binding mechanism is critical for nairovirus transcription.
  • Structural data provides a foundation for designing targeted antivirals against CCHFV and related viruses.

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