Evidence map›Paper›PMID 25870259›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Membrane fusion during phage lysis.

Manoj Rajaure, Joel Berry, Rohit Kongari, Jesse Cahill, Ry Young

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
5.0field-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

57 citing papers in PubMed, 93 citations in OpenAlex.

  1. Whole-proteome structure/function prediction in UropathogenicbioRxiv : the preprint server for biology · 2026
    Article
  2. Prophage: agent provocateur?Archives of microbiology · 2026
    Review
  3. Review
  4. Article
  5. A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  6. Phage N4 uses a SAR endolysin-holin system for host cell lysis.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Identifying components of theJournal of bacteriology · 2024
    Article
  15. Review
  16. Review
  17. Article
  18. Genome characterization of a multi-drug resistantFrontiers in microbiology · 2024
    Article
  19. Article
  20. 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

5 authors at 2 institutions in 2 countries.

Manoj RajaureCenter for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128; and.ORCID http://orcid.org/0000-0002-0440-6222
Joel BerryDepartment of Microbiology, Pasteur Institute, 75724 Paris, France.
Rohit KongariCenter for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128; and.
Jesse CahillCenter for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128; and.
Ry YoungCenter for Phage Technology, Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843-2128; and ryland@tamu.edu.
Texas A&M University · USInstitut Pasteur · FR

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 GM27099NIGMS NIH HHS R01 GM027099NIGMS NIH HHS R37 GM027099
6 · The paper itself

Abstract

In general, phages cause lysis of the bacterial host to effect release of the progeny virions. Until recently, it was thought that degradation of the peptidoglycan (PG) was necessary and sufficient for osmotic bursting of the cell. Recently, we have shown that in Gram-negative hosts, phage lysis also requires the disruption of the outer membrane (OM). This is accomplished by spanins, which are phage-encoded proteins that connect the cytoplasmic membrane (inner membrane, IM) and the OM. The mechanism by which the spanins destroy the OM is unknown. Here we show that the spanins of the paradigm coliphage lambda mediate efficient membrane fusion. This supports the notion that the last step of lysis is the fusion of the IM and OM. Moreover, data are provided indicating that spanin-mediated fusion is regulated by the meshwork of the PG, thus coupling fusion to murein degradation by the phage endolysin. Because endolysin function requires the formation of μm-scale holes by the phage holin, the lysis pathway is seen to require dramatic dynamics on the part of the OM and IM, as well as destruction of the PG.

Indexed as

Membrane FusionBacteriophage lambdaCell MembraneEndopeptidasesEscherichia coliPeptidoglycanViral ProteinsVirus ReleaseendolysinEndopeptidasesPeptidoglycanViral Proteinsendolysinholinmembrane fusionspaninspheroplast

Identifiers

PMID25870259
PMCPMC4418876
OpenAlexW2024166349

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.