Evidence map›Paper›PMID 22761387›Full record

ArticleJournal of virology2012

Alanine scanning of poliovirus 2CATPase reveals new genetic evidence that capsid protein/2CATPase interactions are essential for morphogenesis.

Chunling Wang, Ping Jiang, Claire Sand, Aniko V Paul, Eckard Wimmer

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

36 citing papers in PubMed, 51 citations in OpenAlex.

  1. Review
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  9. Article
  10. Microorganisms · 2021
    Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Seneca Valley Virus 2C and 3CFrontiers in microbiology · 2019
    Article
  17. Article
  18. Article
  19. Emergency Services of Viral RNAs: Repair and Remodeling.Microbiology and molecular biology reviews : MMBR · 2018
    Review
  20. 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

5 authors at 1 institution in 1 country.

Chunling WangDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York, USA.
Ping Jiang
Claire Sand
Aniko V Paul
Eckard Wimmer
Stony Brook University · US

Funding

POLIOVIRUS--MOLECULAR BIOLOGY AND SURFACE STRUCTURER37AI015122 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI WIMMER, ECKARD · 1988 to 2007
$3.8M
POLIOVIRUS MOLECULAR BIOLOGY AND SURFACE STRUCTURER01AI015122 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI WIMMER, ECKARD · 1985 to 2013
$1.9M
NIAID NIH HHS R01 AI015122NIAID NIH HHS R37 AI015122NIAID NIH HHS R37AI015122
6 · The paper itself

Abstract

Polypeptide 2C(ATPase) is one of the most thoroughly studied but least understood proteins in the life cycle of poliovirus. Within the protein, multiple functional domains important for uncoating, host cell membrane alterations, and RNA replication and encapsidation have previously been identified. In this study, charged to alanine-scanning mutagenesis was used to generate conditional-lethal mutations in hitherto-uncharacterized domains of the 2C(ATPase) polypeptide, particularly those involved in morphogenesis. Adjacent or clustered charged amino acids (2 to 4), scattered along the 2C(ATPase) coding sequence, were replaced with alanines. RNA transcripts of mutant poliovirus cDNA clones were transfected into HeLa cells. Subsequently, 10 lethal, 1 severely temperature-sensitive, 2 quasi-infectious, and 3 wild type-like mutants were identified. Using a luciferase-containing reporter virus, we demonstrated RNA replication defects in all lethal and quasi-infectious mutants. Temperature-sensitive mutants were defective in RNA replication only at the restricted temperatures. Furthermore, we characterized a quasi-infectious mutant (K(6)A/K(7)A) that produced a suppressor mutation (G(1)R) and a novel 2B^2C(ATPase) cleavage site (Q^R). Surprisingly, this cleavage site mutation did not interfere with normal processing of the polyprotein. These mutants have led to the identification of several new sites within the 2C(ATPase) polypeptide that are required for RNA replication. In addition, analysis of the suppressor mutants has revealed a new domain near the C terminus of 2C(ATPase) that is involved in encapsidation, possibly achieved through interaction with an amino acid sequence between NTP binding motifs A and B of 2C(ATPase). Most importantly, the identification of suppressor mutations in both 2C(ATPase) and the capsid domains (VP1 and VP3) of poliovirus has confirmed that an interaction between 2C(ATPase) and capsid proteins is involved in viral morphogenesis.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceAmino Acid SubstitutionCapsid ProteinsCarrier ProteinsConserved SequenceHeLa CellsHumansMolecular Sequence DataMorphogenesisMutagenesis, Site-DirectedPhenotypePoliovirusProtein Structure, TertiaryViral Nonstructural ProteinsVirus Assembly2C protein, viralAdenosine TriphosphatasesCapsid ProteinsCarrier ProteinsViral Nonstructural Proteins

Identifiers

PMID22761387
PMCPMC3446611
OpenAlexW1978460998

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.