Evidence map›Paper›PMID 38032199›Full record

ArticleJournal of virology2023

Amino acid substitutions in norovirus VP1 dictate host dissemination via variations in cellular attachment.

Jake T Mills, Susanna C Minogue, Joseph S Snowden, Wynter K C Arden, David J Rowlands, Nicola J Stonehouse, Christiane E Wobus, Morgan R Herod

Open access · hybridAbstract read
In one paragraph

Article in Journal of virology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.8field-weighted citation impact, top 28% of its field
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

2 citing papers in PubMed, 4 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Jake T MillsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-4443-8296
Susanna C MinogueAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.
Joseph S SnowdenAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.
Wynter K C ArdenDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan, USA.
David J RowlandsAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-4742-9272
Nicola J StonehouseAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.ORCID 0000-0003-1146-5519
Christiane E WobusDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, Michigan, USA.ORCID 0000-0001-5286-0924
Morgan R HerodAstbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.ORCID 0000-0002-8626-6787
University of Leeds · GBUniversity of Michigan · US

Funding

The role of norovirus capsid flexibility in infection and pathogenesisR21AI154647 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WOBUS, CHRISTIANE · 2021 to 2022
$444k
Medical Research Council MR/S007229/1NIAID NIH HHS R21 AI154647Wellcome Trust
6 · The paper itself

Abstract

importanceAll viruses initiate infection by utilizing receptors to attach to target host cells. These virus-receptor interactions can therefore dictate viral replication and pathogenesis. Understanding the nature of virus-receptor interactions could also be important for the development of novel therapies. Noroviruses are non-enveloped icosahedral viruses of medical importance. They are a common cause of acute gastroenteritis with no approved vaccine or therapy and are a tractable model for studying fundamental virus biology. In this study, we utilized the murine norovirus model system to show that variation in a single amino acid of the major capsid protein alone can affect viral infectivity through improved attachment to suspension cells. Modulating plasma membrane mobility reduced infectivity, suggesting an importance of membrane mobility for receptor recruitment and/or receptor conformation. Furthermore, different substitutions at this site altered viral tissue distribution in a murine model, illustrating how in-host capsid evolution could influence viral infectivity and/or immune evasion.

Indexed as

Caliciviridae InfectionsCapsid ProteinsNorovirusAmino Acid SubstitutionAnimalsCapsidImmune EvasionMiceViral Core ProteinsCapsid ProteinsViral Core ProteinsCD300lfmembrane fluidityMNVmurine norovirusreceptorvirus evolution

Identifiers

PMID38032199
PMCPMC10734460
OpenAlexW4389179542

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.