Evidence map›Paper›PMID 2656650›Full record

ArticleJournal of bacteriology1989

Specific localization of the lysis protein of bacteriophage MS2 in membrane adhesion sites of Escherichia coli.

B Walderich, J V Höltje

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 1989. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
5.2field-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

17 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Physiological characterization of single gene lysis proteins.bioRxiv : the preprint server for biology · 2023
    Article
  3. Microbiome research reports · 2023
    Article
  4. Review
  5. Review
  6. Review
  7. Mutational analysis of the MS2 lysis protein L.Microbiology (Reading, England) · 2017
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Review
  14. Article
  15. Article
  16. Bacteriophage lysis: mechanism and regulation.Microbiological reviews · 1992
    Review
  17. 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

2 authors at 2 institutions in 1 country.

B WalderichMax-Planck-Institut für Entwicklungsbiologie, Abteilung Biochemie, Tübingen, Federal Republic of Germany.
J V Höltje
Max Planck Institute for Developmental Biology · DEMax Planck Society · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specific localization of the lysis (L) protein of bacteriophage MS2 in the cell wall of Escherichia coli was determined by immunoelectron microscopy. After induction of the cloned lysis gene, the cells were plasmolyzed, fixed, and embedded in either Epon or Lowicryl K4M. Polyclonal L-protein-specific antiserum was purified by preabsorption to membranes from cells harboring a control plasmid. Protein A-gold was used to label the protein-antibody complexes. Between 42.8% (Lowicryl) and 33.8% (Epon) of the label was found in inner and outer membranes, but 30.3% (Lowicryl) and 32.8% (Epon) was present mostly in clusters in the adhesion sites visible after plasmolysis. The remaining label (26.9 and 33.4%, respectively) appeared to be present in the periplasmic space but may also have been part of membrane junctions not visible because of poor contrast of the specimen. In contrast, a quite different distribution of the L protein was found in cells grown under conditions of penicillin tolerance, i.e., at pH 5, a condition that had previously been shown to protect cells from L-protein-induced lysis. At tolerant conditions, only 21.0% of the L protein was in the adhesion sites; most of the protein (68.2%) was found in inner and outer membranes. It is concluded that lysis of the host, E. coli, was a result of the formation of specific L-protein-mediated membrane adhesion sites.

Indexed as

Cell MembraneCell WallColiphagesEscherichia coliImmunohistochemistryMicroscopy, ElectronViral Proteinslysis protein, Enterobacterio phage MS2Viral Proteins

Identifiers

PMID2656650
PMCPMC210054
OpenAlexW2136345418

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.