Evidence map›Paper›PMID 23426355›Full record

ArticleThe Journal of general virology2013

Mutations in the rotavirus spike protein VP4 reduce trypsin sensitivity but not viral spread.

Shane D Trask, J Denise Wetzel, Terence S Dermody, John T Patton

Open access · greenAbstract read
In one paragraph

Article in The Journal of general virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. 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

4 authors at 2 institutions in 1 country.

Shane D TraskLaboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-8026, USA.
J Denise WetzelDepartment of Pediatrics and the Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-2581, USA.
Terence S DermodyDepartments of Pediatrics and Pathology, Microbiology and Immunology and the Elizabeth B. Lamb Center for Pediatric Research, Vanderbilt University School of Medicine, Nashville, Tennessee 37232-2581, USA.
John T PattonLaboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland 20892-8026, USA.
National Institute of Allergy and Infectious Diseases · USVanderbilt University · US

Funding

CELL ENTRY OF REOVIRUSR01AI032539 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI TERENCE S. DERMODY · 1998 to 2026
$12.3M
Mechanism Of Rotavirus Genome Replication And PackagingZIAAI000754 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI PATTON, JOHN · 2009 to 2015
$3.4M
MODIFICATION OF THE ANTIGENICITY &VIRULENCE OF ROTAVIRUSES BY REVERSE GENETICSZ01AI000788 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI PATTON, JOHN · 1997 to 2008
$1.1M
Intramural NIH HHSNIAID NIH HHS R01 AI032539NIAID NIH HHS R01 AI32539NIAID NIH HHS Z01 AI000788
6 · The paper itself

Abstract

Infectious entry of the nonenveloped rotavirus virion requires proteolysis of the spike protein VP4 to mediate conformational changes associated with membrane penetration. We sequenced and characterized an isolate that was cultured in the absence of trypsin and found that it is more resistant to proteolysis than WT virus. A substitution mutation abrogates one of the defined trypsin-cleavage sites, suggesting that blocking proteolysis at this site reduces the overall kinetics of proteolysis. Kinetic analysis of the membrane penetration-associated conformational change indicated that the 'fold-back' of the mutant spike protein is slower than that of WT. Despite these apparent biochemical defects, the mutant virus replicates in an identical manner to the WT virus. These findings enhance an understanding of VP4 functions and establish new strategies to interrogate rotavirus cell entry.

Indexed as

MutationAmino Acid SequenceAnimalsCapsid ProteinsHost-Pathogen InteractionsHumansMacaca mulattaMolecular Sequence DataProtein Processing, Post-TranslationalRotavirusRotavirus InfectionsSequence AlignmentTrypsinVirus InternalizationVirus ReplicationCapsid ProteinsTrypsinVP4 protein, Rotavirus

Identifiers

PMID23426355
PMCPMC3709623
OpenAlexW2067700983

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.