Evidence map›Paper›PMID 24899153›Full record

ArticleThe Journal of general virology2014

Newly isolated mAbs broaden the neutralizing epitope in murine norovirus.

Abimbola O Kolawole, Chunsheng Xia, Ming Li, Monica Gamez, Chenchen Yu, Christine M Rippinger, Ryan E Yucha, Thomas J Smith, Christiane E Wobus

Open access · greenAbstract read
In one paragraph

Article in The Journal of general virology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.4field-weighted citation impact, top 40% 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

23 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
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  4. Impaired K48-polyubiquitination downmodulates mouse norovirus propagation.Frontiers in cellular and infection microbiology · 2025
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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 at 2 institutions in 1 country.

Abimbola O KolawoleDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, USA.
Chunsheng XiaDonald Danforth Plant Science Center, St Louis, MO, USA.
Ming LiDonald Danforth Plant Science Center, St Louis, MO, USA.
Monica GamezDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, USA.
Chenchen YuDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, USA.
Christine M RippingerDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, USA.
Ryan E YuchaDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, USA.
Thomas J SmithDonald Danforth Plant Science Center, St Louis, MO, USA.
Christiane E WobusDepartment of Microbiology and Immunology, University of Michigan Medical School, Ann Arbor, MI, USA.
University of Michigan–Ann Arbor · USDonald Danforth Plant Science Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Here, we report the isolation and functional characterization of mAbs against two murine norovirus (MNV) strains, MNV-1 and WU20, which were isolated following oral infection of mice. The mAbs were screened for reactivity against the respective homologous and heterologous MNV strain by ELISA. Selected mAbs were of IgA, IgG1, IgG2a or IgG2b isotype and showed a range of Western blot reactivities from non-binding to strong binding, suggesting recognition of conformational and linear epitopes. Some of the anti-MNV-1 antibodies neutralized both MNV-1 and WU20 infections in culture and in mice, but none of the anti-WU20 mAbs neutralized either virus. The non-neutralizing anti-MNV-1 IgG2b antibody 5C4.10 was mapped to the S domain of the MNV-1 capsid, whilst the epitopes of the neutralizing anti-MNV-1 IgA antibodies 2D3.7 and 4F9.4 were mapped to the P domain. Generation of neutralization escape viruses showed that two mutations (V339I and D348E) in the C'D' loop of the MNV-1 P domain mediated escape from mAb 2D3.7 and 4F9.4 neutralization. These findings broaden the known neutralizing epitopes of MNV to the main surface-exposed loops of the P domain. In addition, the current panel of antibodies provides valuable reagents for studying norovirus biology and development of diagnostic tools.

Indexed as

Amino Acid SequenceAnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralAntibody SpecificityCaliciviridae InfectionsCapsidCapsid ProteinsCell LineEpitopesHEK293 CellsHumansImmunoglobulin AImmunoglobulin GMacrophagesAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralCapsid ProteinsEpitopesImmunoglobulin AImmunoglobulin G

Identifiers

PMID24899153
PMCPMC4135088
OpenAlexW1996865848

What OpenQuestion holds

Textmetadata
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.