ArticleiScience2025
The regulatory mechanisms of SARS-CoV-2 N protein helicase and its annealing activity.
Article in iScience, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Authors and funding
14 authors.
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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.
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