Evidence map›Paper›PMID 41764255›Full record

ArticleScientific reports2026

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

Agnė Rimkutė, Martynas Simanavičius, Indrė Dalgėdienė, Evaldas Čiplys, Donata Hoffmann, Kerstin Wernike, Vytautė Starkuvienė-Erfle, Aurelija Žvirblienė, Indrė Kučinskaitė-Kodzė

Abstract read
In one paragraph

Article in Scientific reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

  1. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Agnė RimkutėInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania. agne.rimkute@gmc.vu.lt.
Martynas SimanavičiusInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Indrė DalgėdienėInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Evaldas ČiplysInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Donata HoffmannInstitute of Diagnostic Virology, Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany.
Kerstin WernikeInstitute of Diagnostic Virology, Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany.
Vytautė Starkuvienė-ErfleInstitute of Biosciences, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Aurelija ŽvirblienėInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.
Indrė Kučinskaitė-KodzėInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius, Lithuania.

Funding

Lietuvos Mokslo Taryba 13.1.1-LMT-K-718-05-0031
6 · The paper itself

Abstract

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.

Indexed as

Antibodies, MonoclonalAntibodies, ViralAntigens, ViralCoronavirus Nucleocapsid ProteinsNucleocapsid ProteinsSARS-CoV-2AnimalsCOVID-19Cross ReactionsEpitopesHumansMiceMice, Inbred BALB CPhosphoproteinsAntibodies, MonoclonalAntibodies, ViralAntigens, ViralCoronavirus Nucleocapsid ProteinsEpitopesnucleocapsid phosphoprotein, SARS-CoV-2Nucleocapsid ProteinsPhosphoproteinsImmunodominant epitopesMonoclonal antibodiesNucleocapsid proteinSARS-CoV-2

Identifiers

PMID41764255
PMCPMC13057025

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.