Evidence map›Paper›PMID 28691656›Full record

ArticleMicrobiology (Reading, England)2017

Mutational analysis of the MS2 lysis protein L.

Karthik R Chamakura, Garrett B Edwards, Ry Young

Abstract read
In one paragraph

Article in Microbiology (Reading, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Measuring the selective packaging of RNA molecules by viral coat proteins in cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Physiological characterization of single gene lysis proteins.bioRxiv : the preprint server for biology · 2023
    Article
  8. Review
  9. Article
  10. Microbiome research reports · 2023
    Article
  11. Article
  12. Single-gene lysis in the metagenomic era.Current opinion in microbiology · 2020
    Review
  13. Article
  14. Review
  15. Review
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

3 authors at 1 institution in 1 country.

Karthik R ChamakuraCenter for Phage Technology, Texas A&M AgriLife, Texas A&M University, College Station, TX, USA.
Garrett B EdwardsCenter for Phage Technology, Texas A&M AgriLife, Texas A&M University, College Station, TX, USA.
Ry YoungDepartment of Biochemistry and Biophysics, Texas A&M University, College Station, TX, USA.
Texas A&M University · US

Funding

CONTROL OF VIRUS-INDUCED LYSISR01GM027099 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI YOUNG, RYLAND FLETCHER · 1985 to 2019
$4.6M
CONTROL OF VIRUS INDUCED LYSISR37GM027099 · NIGMS · TEXAS A&M UNIVERSITY SYSTEM · PI YOUNG, RYLAND F. · 1996 to 2005
$2.4M
NIGMS NIH HHS R01 GM027099NIGMS NIH HHS R37 GM027099
6 · The paper itself

Abstract

Small single-stranded nucleic acid phages effect lysis by expressing a single protein, the amurin, lacking muralytic enzymatic activity. Three amurins have been shown to act like 'protein antibiotics' by inhibiting cell-wall biosynthesis. However, the L lysis protein of the canonical ssRNA phage MS2, a 75 aa polypeptide, causes lysis by an unknown mechanism without affecting net peptidoglycan synthesis. To identify residues important for lytic function, randomly mutagenized alleles of L were generated, cloned into an inducible plasmid and the transformants were selected on agar containing the inducer. From a total of 396 clones, 67 were unique single base-pair changes that rendered L non-functional, of which 44 were missense mutants and 23 were nonsense mutants. Most of the non-functional missense alleles that accumulated in levels comparable to the wild-type allele are localized in the C-terminal half of L, clustered in and around an LS dipeptide sequence. The LS motif was used to align L genes from ssRNA phages lacking any sequence similarity to MS2 or to each other. This alignment revealed a conserved domain structure, in terms of charge, hydrophobic character and predicted helical content. None of the missense mutants affected membrane-association of L. Several of the L mutations in the central domains were highly conservative and recessive, suggesting a defect in a heterotypic protein-protein interaction, rather than in direct disruption of the bilayer structure, as had been previously proposed for L.

Indexed as

Amino Acid MotifsAmino Acid SequenceBase SequenceDNA Mutational AnalysisLevivirusMolecular Sequence DataSequence AlignmentViral Structural ProteinsViral Structural Proteins

Identifiers

PMID28691656
PMCPMC5775895
OpenAlexW2731516456

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.