The regulatory mechanisms of SARS-CoV-2 N protein helicase and its annealing activity

The nucleocapsid (N) protein of SARS-CoV-2 performs multiple functions essential for viral replication and host adaptation. Here, we identify ionic strength as a critical determinant of its dual nucleic acid-manipulating activities. Under low-salt conditions (≤100 mM NaCl), SARS-CoV-2 N primarily promotes strand annealing, whereas at high ionic strength (≥300 mM NaCl), its helicase activity is additively enhanced. SARS-CoV-2 N also preferentially acts on DNA rather than RNA substrates and modulates the helicase activity of Nsp13 in an ion-dependent manner-inhibiting it under low-salt conditions but enhancing it under high-salt conditions. These findings reveal an ion concentration-dependent regulatory mechanism that enables SARS-CoV-2 N to dynamically switch between distinct biochemical states, thereby supporting viral adaptability and providing new insights into antiviral development.

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Publication Details

Journal
iScience
Published
2025-11-17
DOI
https://doi.org/10.1016/j.isci.2025.113983
Primary Topic
RNA Research and Splicing
Type
article
Field-Weighted Citation Impact
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article

The regulatory mechanisms of SARS-CoV-2 N protein helicase and its annealing activity

Zhaoling Lan, Meng Cai, Shuo Wei, Chuanping Yang et al.
iScience
RNA Research and Splicing
article

The regulatory mechanisms of SARS-CoV-2 N protein helicase and its annealing activity

Zhaoling Lan, Meng Cai, Shuo Wei, Chuanping Yang, Yin Dai, Yan Xie, Jing Yang, Peng Zhou, Jida Li, Can‐Jun Ruan, Bo Zhang, Yi Zhang, Hongyi Wang, Long Gao
article en

Abstract

The nucleocapsid (N) protein of SARS-CoV-2 performs multiple functions essential for viral replication and host adaptation. Here, we identify ionic strength as a critical determinant of its dual nucleic acid-manipulating activities. Under low-salt conditions (≤100 mM NaCl), SARS-CoV-2 N primarily promotes strand annealing, whereas at high ionic strength (≥300 mM NaCl), its helicase activity is additively enhanced. SARS-CoV-2 N also preferentially acts on DNA rather than RNA substrates and modulates the helicase activity of Nsp13 in an ion-dependent manner-inhibiting it under low-salt conditions but enhancing it under high-salt conditions. These findings reveal an ion concentration-dependent regulatory mechanism that enables SARS-CoV-2 N to dynamically switch between distinct biochemical states, thereby supporting viral adaptability and providing new insights into antiviral development.

iScienceVol. 28(12)
Zunyi Medical University (CN)
Openalex Percentile: Top 69%
RNA Research and Splicing
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