Evidence map›Paper›PMID 10516013›Full record

ArticleJournal of virology1999

Poliovirus mutants at histidine 195 of VP2 do not cleave VP0 into VP2 and VP4.

M Hindiyeh, Q H Li, R Basavappa, J M Hogle, M Chow

Abstract read
In one paragraph

Article in Journal of virology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Trial
  2. Open questions in enterovirus uncoating.Journal of virology · 2026
    Review
  3. Article
  4. Article
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  13. Review
  14. Article
  15. Article
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  17. Article
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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

5 authors.

M HindiyehDepartment of Microbiology, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205, USA.
Q H Li
R Basavappa
J M Hogle
M Chow

Funding

Tuberculosis Co-Morbidities and ImmunopathogenesisR13AI122627 · NIAID · KEYSTONE SYMPOSIA · PI WOODLAND, DAVID L. · 2016 to 2016
$6k
NIAID NIH HHS AI122627NIAID NIH HHS R13 AI122627
6 · The paper itself

Abstract

The final stage of poliovirus assembly is characterized by a cleavage of the capsid precursor protein VP0 into VP2 and VP4. This cleavage is thought to be autocatalytic and dependent on RNA encapsidation. Analysis of the poliovirus empty capsid structure has led to a mechanistic model for VP0 cleavage involving a conserved histidine residue that is present in the surrounding environment of the VP0 cleavage site. Histidine 195 of VP2 (2195H) is hypothesized to activate local water molecules, thus initiating a nucleophilic attack at the scissile bond. To test this hypothesis, 2195H mutants were constructed and their phenotypes were characterized. Consistent with the requirement of VP0 cleavage for poliovirus infectivity, all 2195H mutants were nonviable upon introduction of the mutant genomes into HeLa cells. Replacement of 2195H with threonine or arginine resulted in the assembly of a highly unstable 150S virus particle. Further analyses showed that these particles contain genomic RNA and uncleaved VP0, criteria associated with the provirion assembly intermediate. These data support the involvement of 2195H in mediating VP0 cleavage during the final stages of virus assembly.

Indexed as

CapsidCapsid ProteinsCentrifugation, Density GradientHeLa CellsHistidineHumansMutagenesis, Site-DirectedPoliovirusPrecipitin TestsProtein PrecursorsReverse Transcriptase Polymerase Chain ReactionVirionVirus AssemblyVirus ReplicationCapsid ProteinsHistidineProtein PrecursorsVP0 protein, PoliovirusVP2 protein, PoliovirusVP4 protein, Rotavirus

Identifiers

PMID10516013
PMCPMC112939

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.