Evidence map›Paper›PMID 17417822›Full record

ArticleBiochemistry2007

Membrane topography of the hydrophobic anchor sequence of poliovirus 3A and 3AB proteins and the functional effect of 3A/3AB membrane association upon RNA replication.

Kentaro Fujita, Shyam S Krishnakumar, David Franco, Aniko V Paul, Erwin London, Eckard Wimmer

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.0field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 69 citations in OpenAlex.

  1. Review
  2. Article
  3. Serial passagingFrontiers in cellular and infection microbiology · 2026
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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

6 authors at 1 institution in 1 country.

Kentaro FujitaDepartment of Molecular Genetics and Microbiology, Stony Brook University, Stony Brook, New York 11794-5222, USA.
Shyam S Krishnakumar
David Franco
Aniko V Paul
Erwin London
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
DIPHTHERIA TOXIN STRUCTURE AND MEMBRANE INTERACTIONR01GM031986 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI LONDON, ERWIN · 1985 to 2006
$2.0M
POLIOVIRUS MOLECULAR BIOLOGY AND SURFACE STRUCTURER01AI015122 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI WIMMER, ECKARD · 1985 to 2013
$1.9M
NIAID NIH HHS AI015122NIAID NIH HHS R01 AI015122NIAID NIH HHS R37 AI015122NIGMS NIH HHS GM31986NIGMS NIH HHS R01 GM031986
6 · The paper itself

Abstract

Replication of poliovirus RNA takes place on the cytoplasmic surface of membranous vesicles that form after infection of the host cell. It is generally accepted that RNA polymerase 3D(pol) interacts with membranes in a complex with viral protein 3AB, which binds to membranes by means of a hydrophobic anchor sequence that is located near the C-terminus of the 3A domain. In this study, we used fluorescence and fluorescence quenching methods to define the topography of the anchor sequence in the context of 3A and 3AB proteins inserted in model membranes. Mutants with a single tryptophan near the center of the anchor sequence but lacking Trp elsewhere in 3A/3AB were constructed which, after the emergence of suppressor mutations, replicated well in HeLa cells. When a peptide containing the mutant anchor sequence was incorporated in model membrane vesicles, measurements of Trp depth within the lipid bilayer indicated formation of a transmembrane topography. However, rather than the 22-residue length predicted from hydrophobicity considerations, the transmembrane segment had an effective length of 16 residues, such that Gln64 likely formed the N-terminal boundary. Analogous experiments using full-length proteins bound to preformed model membrane vesicles showed that the anchor sequence formed a mixture of transmembrane and nontransmembrane topographies in the 3A protein but adopted only the nontransmembrane configuration in the context of 3AB protein. Studies of the function of 3A/3AB inserted into model membrane vesicles showed that membrane-bound 3AB is highly efficient in stimulating the activity of 3D(pol) in vitro while membrane-bound 3A totally lacks this activity. Moreover, in vitro uridylylation reactions showed that membrane-bound 3AB is not a substrate for 3D(pol), but free VPg released by cleavage of 3AB with proteinase 3CD(pro) could be uridylylated.

Indexed as

AcrylamideAmino Acid SequenceBase SequenceBinding SitesDNA PrimersMolecular Sequence DataMutagenesisPoliovirusProtein BindingRNA, ViralSpectrometry, FluorescenceTranscription, GeneticViral ProteinsAcrylamideDNA PrimersRNA, ViralViral Proteins

Identifiers

PMID17417822
PMCPMC2519882
OpenAlexW2058988384

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.