Evidence map›Paper›PMID 17804495›Full record

ArticleJournal of virology2007

A single-amino-acid substitution in the P2 domain of VP1 of murine norovirus is sufficient for escape from antibody neutralization.

Vance P Lochridge, Michele E Hardy

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 13% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 60 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Structural basis for murine norovirus engagement of bile acids and the CD300lf receptor.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Norovirus.Clinical microbiology reviews · 2015
    Review
  18. Article
  19. Article
  20. Pathology caused by persistent murine norovirus infection.The Journal of general virology · 2014
    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

2 authors at 1 institution in 1 country.

Vance P LochridgeVeterinary Molecular Biology, Montana State University, Bozeman, MT 59717-3610, USA.
Michele E Hardy
Montana State University · US

Funding

VIRUSES: FROM PARTICLES TO PROTEOMICSP20RR020185 · NCRR · MONTANA STATE UNIVERSITY - BOZEMAN · PI VOYICH, JOVANKA M · 2004 to 2011
$17.0M
The role of beta-endorphin in cutaneous inflammationF31ES027301 · NIEHS · HARVARD MEDICAL SCHOOL · PI SILKWORTH, WHITNEY · 2016 to 2017
$63k
NCRR NIH HHS P20 RR020185NIEHS NIH HHS 27301C0040
6 · The paper itself

Abstract

Noroviruses cause epidemic outbreaks of acute viral gastroenteritis worldwide, and the number of reported outbreaks is increasing. Human norovirus strains do not grow in cell culture. However, murine norovirus (MNV) replicates in the RAW 264.7 macrophage cell line and thus provides a tractable model to investigate norovirus interactions with host cells. Epitopes recognized by monoclonal antibodies (MAbs) against the human norovirus strains Norwalk virus and Snow Mountain virus (SMV) identified regions in the P domain of major capsid protein VP1 important for interactions with putative cellular receptors. To determine if there was a relationship between domains of MNV VP1 and VP1 of human norovirus strains involved in cell binding, epitope mapping by phage display was performed with an MNV-1-neutralizing MAb, A6.2.1. A consensus peptide, GWWEDHGQL, was derived from 20 third-round phage clones. A synthetic peptide containing this sequence and constrained through a disulfide linkage reacted strongly with the A6.2.1 MAb, whereas the linear sequence did not. Four residues in the A6.2.1-selected peptide, G327, G333, Q334, and L335, aligned with amino acid residues in the P2 domain of MNV-1 VP1. This sequence is immediately adjacent to the epitope recognized by anti-SMV MAb 61.21. Neutralization escape mutants selected with MAb A6.2.1 contained a leucine-to-phenylalanine substitution at position 386 in the P2 domain. The predicted location of these residues on VP1 suggests that the phage peptide and the mutation in the neutralization-resistant viruses may be in close proximity to each other and to residues reported to be important for carbohydrate binding to VP1 of human norovirus strains.

Indexed as

Amino Acid MotifsAmino Acid SequenceAmino Acid SubstitutionAnimalsAntibodies, MonoclonalAntibodies, ViralEpitope MappingEpitopesHumansMiceMolecular Sequence DataMutationNeutralization TestsNorovirusNorwalk virusPeptide LibraryAntibodies, MonoclonalAntibodies, ViralEpitopesPeptide LibraryViral Core Proteins

Identifiers

PMID17804495
PMCPMC2168968
OpenAlexW2079005064

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.