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SARS-CoV-2 nucleocapsid protein-specific monoclonal antibodies as tools for studying its antigenic structure and interaction with host cells

Diagnostics and prevention of COVID-19 are essential for controlling the spread of the virus and reducing mortality rates. As SARS-CoV-2 surface proteins are susceptible to mutations, the nucleocapsid protein (NP) with its highly conserved gene sequence is an attractive target for studying virus-hos...

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Main Authors: Rimkute, Agne (Author) , Simanavičius, Martynas (Author) , Dalgėdienė, Indrė (Author) , Čiplys, Evaldas (Author) , Hoffmann, Donata (Author) , Wernike, Kerstin (Author) , Starkuviene-Erfle, Vytaute (Author) , Žvirblienė, Aurelija (Author) , Kučinskaitė-Kodzė, Indrė (Author)
Format: Article (Journal)
Language:English
Published: 28 February 2026
In: Scientific reports
Year: 2026, Volume: 16, Pages: 1-15
ISSN:2045-2322
DOI:10.1038/s41598-026-40984-8
Online Access:Verlag, kostenfrei, Volltext: https://doi.org/10.1038/s41598-026-40984-8
Verlag, kostenfrei, Volltext: https://www.nature.com/articles/s41598-026-40984-8
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Author Notes:Agnė Rimkutė, Martynas Simanavičius, Indrė Dalgėdienė, Evaldas Čiplys, Donata Hoffmann, Kerstin Wernike, Vytautė Starkuvienė-Erfle, Aurelija Žvirblienė, Indrė Kučinskaitė-Kodzė
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Summary:Diagnostics and prevention of COVID-19 are essential for controlling the spread of the virus and reducing mortality rates. As SARS-CoV-2 surface proteins are susceptible to mutations, the nucleocapsid protein (NP) with its highly conserved gene sequence is an attractive target for studying virus-host interactions. NP plays a key role in the coronavirus life cycle, modulating viral RNA packaging, transcription, and assembly. In addition, its abundant expression during infection makes it a valuable diagnostic marker. NP is involved in modulating the host’s innate immunity; however, the cellular mechanisms of its pathogenicity are not yet fully understood. This study developed and characterized murine monoclonal antibodies (MAbs) specific to the SARS-CoV-2 NP to investigate its antigenic regions and utilize the MAbs in virus-detecting systems or cellular NP blocking assays. The MAbs showed cross-reactivity with Omicron NP, recognizing epitopes within functionally active domains. They also identified NP in SARS-CoV-2-infected cells, supporting their feasibility in future immunoassays. Additionally, the ability to inhibit NP-cell interaction was assessed, with MAbs 4B3, 7F10, 16D9, and 18A8 found to reduce NP internalization. Overall, this study provides well-characterized tools for investigating SARS-CoV-2 antigenicity and pathogenicity and demonstrates the functional potential of the generated MAbs in studying NP-mediated host cell interactions.
Item Description:Gesehen am 02.06.2026
Online veröffentlicht: 28. Februar 2026
Physical Description:Online Resource
ISSN:2045-2322
DOI:10.1038/s41598-026-40984-8

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