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Related Experiment Video

Updated: Jan 17, 2026

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

Published on: July 27, 2021

Structure and function of the nairovirus cap-snatching endonuclease.

Wenhua Kuang¹, Zhenhua Tian^1,2, 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

Summary

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).

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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.