Evidence map›Paper›PMID 15919887›Full record

ArticleJournal of virology2005

A single amino acid change in the L-polymerase protein of vesicular stomatitis virus completely abolishes viral mRNA cap methylation.

Valery Z Grdzelishvili, Sherin Smallwood, Dallas Tower, Richard L Hall, D Margaret Hunt, Sue A Moyer

Abstract read
In one paragraph

Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.6field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
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  5. Article
  6. Locations and in situ structure of the polymerase complex inside the virion of vesicular stomatitis virus.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  7. Article
  8. Article
  9. Article
  10. Structures of theJournal of virology · 2020
    Review
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  13. Review
  14. Article
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  16. Review
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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 3 institutions in 1 country.

Valery Z GrdzelishviliUniversity of Florida College of Medicine, Department of Molecular Genetics and Microbiology, 1600 S.W. Archer Road, P.O. Box 100266, Gainesville, FL 32610-0266, USA.
Sherin Smallwood
Dallas Tower
Richard L Hall
D Margaret Hunt
Sue A Moyer
Florida College · USUniversity of Florida · USUniversity of South Carolina · US

Funding

TRANSCRIPTION/REPLICATION OF NEGATIVE STRAND RNA VIRUSESR01AI014594 · NIAID · VANDERBILT UNIVERSITY · PI MOYER, SUE A. · 1985 to 2005
$1.7M
NIAID NIH HHS AI14594NIAID NIH HHS R01 AI014594
6 · The paper itself

Abstract

The vesicular stomatitis virus (VSV) RNA polymerase synthesizes viral mRNAs with 5'-cap structures methylated at the guanine-N7 and 2'-O-adenosine positions (7mGpppA(m)). Previously, our laboratory showed that a VSV host range (hr) and temperature-sensitive (ts) mutant, hr1, had a complete defect in mRNA cap methylation and that the wild-type L protein could complement the hr1 defect in vitro. Here, we sequenced the L, P, and N genes of mutant hr1 and found only two amino acid substitutions, both residing in the L-polymerase protein, which differentiate hr1 from its wild-type parent. These mutations (N505D and D1671V) were introduced separately and together into the L gene, and their effects on VSV in vitro transcription and in vivo chloramphenicol acetyltransferase minigenome replication were studied under conditions that are permissive and nonpermissive for hr1. Neither L mutation significantly affected viral RNA synthesis at 34 degrees C in permissive (BHK) and nonpermissive (HEp-2) cells, but D1671V reduced in vitro transcription and genome replication by about 50% at 40 degrees C in both cell lines. Recombinant VSV bearing each mutation were isolated, and the hr and ts phenotypes in infected cells were the result of a single D1671V substitution in the L protein. While the mutations did not significantly affect mRNA synthesis by purified viruses, 5'-cap analyses of product mRNAs clearly demonstrated that the D1671V mutation abrogated all methyltransferase activity. Sequence analysis suggests that an aspartic acid at amino acid 1671 is a critical residue within a putative conserved S-adenosyl-l-methionine-binding domain of the L protein.

Indexed as

Amino Acid SubstitutionAmino Acid SequenceAnimalsCell LineCricetinaeHumansMethylationMolecular Sequence DataMutationRecombination, GeneticRNA CapsRNA-Dependent RNA PolymeraseRNA, MessengerRNA, ViralTemperatureVesicular stomatitis Indiana virusL protein, vesicular stomatitis virusRNA CapsRNA-Dependent RNA PolymeraseRNA, MessengerRNA, ViralViral Proteins

Identifiers

PMID15919887
PMCPMC1143665
OpenAlexW2041593979

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.