Evidence map›Paper›PMID 41532757›Full record

ArticleJournal of virology2026

Key residues in SARS-CoV-2 NSP3 hypervariable region are necessary to modulate early stress granule activity.

R Elias Alvarado, Kumari G Lokugamage, Dimitriya Garvanska, Leah K Estes, Yani Ahearn, Alyssa M McLeland, Arian Moayyed, Jennifer Chen, Blanca Lopez Mendez, Jessica A Plante and 4 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of virology, 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

5 · Who and what money

Authors and funding

14 authors.

R Elias AlvaradoDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Kumari G LokugamageDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Dimitriya GarvanskaNovo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Leah K EstesDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Yani AhearnDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Alyssa M McLelandDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Arian MoayyedDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Jennifer ChenDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Blanca Lopez MendezNovo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Jessica A PlanteDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Kenneth S PlanteDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.
Bryan A JohnsonDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.ORCID 0000-0002-8999-1255
Jakob NilssonNovo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Copenhagen, Denmark.
Vineet D MenacheryDepartment of Microbiology and Immunology, University of Texas Medical Branch, Galveston, Texas, USA.ORCID 0000-0001-8803-7606

Funding

Burroughs Wellcome Fund Investigators In PathogenesisIndependent Research Fund Denmark 3101-00358BNational Institute of Allergy and Infectious Diseases AI153602, AI145400, AI171413National Institute of Allergy and Infectious Diseases T32AI007526Novo Nordisk Fonden NNF14CC0001Sygeforsikring Danmark
6 · The paper itself

Abstract

Antagonism of the host responses that limits viral replication is critical to the success of infection. Recently, we identified that the hypervariable region (HVR) of SARS-CoV-2 NSP3 binds to FXR1 and disrupts stress granule formation during the early stages of infection. Despite variation across the rest of the HVR, a 20-amino acid region, highly conserved in the Sarbecovirus family, is required for NSP3-FXR1 binding, but the critical residues remained unresolved. In this study, we explore the individual residues in NSP3 driving FXR1 binding and determine their impact on viral replication, pathogenesis, and stress granule formation. Our results indicate that the tyrosine at position 138 (Y138) and a phenylalanine at position 145 (F145) are required for FXR1 binding and affinity. Using reverse genetics, we showed that mutating NSP3 Y138A/F145A (YF mutant) reduced viral replication

Indexed as

COVID-19SARS-CoV-2Stress GranulesViral Nonstructural ProteinsAnimalsChlorocebus aethiopsHumansMutationProtein BindingRNA-Binding ProteinsVero CellsVirus ReplicationRNA-Binding ProteinsViral Nonstructural ProteinscoronavirusFXR1NSP3nucleocapsidSARS-CoV-2stress granules

Identifiers

PMID41532757
PMCPMC12911859

What OpenQuestion holds

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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.