Evidence map›Paper›PMID 30635077›Full record

ReviewAdvances in virus research2019

Phage Lysis: Multiple Genes for Multiple Barriers.

Jesse Cahill, Ry Young

Abstract readReview
In one paragraph

Review in Advances in virus research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 207 papers.

0numbers the graph read from it
0cells of the map it votes in
207citing papers in PubMed
42.6field-weighted citation impact, top 1% 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

207 citing papers in PubMed, 319 citations in OpenAlex.

  1. Review
  2. How bacterial immune systems sense phage infection.Nature reviews. Microbiology · 2026
    Review
  3. Article
  4. Prophage-Derived Molecules as Anti-Antibiotics (Basel, Switzerland) · 2026
    Review
  5. Bacteriophages AgainstViruses · 2026
    Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

147 more citing papers are in PubMed but not listed here.

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 1 institution in 1 country.

Jesse CahillDepartment of Biochemistry & Biophysics, Center of Phage Technology, Texas A&M University, College Station, TX, United States. Electronic address: jesse.cahill@tamu.edu.
Ry YoungDepartment of Biochemistry & Biophysics, Center of Phage Technology, Texas A&M University, College Station, TX, United States.
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

The first steps in phage lysis involve a temporally controlled permeabilization of the cytoplasmic membrane followed by enzymatic degradation of the peptidoglycan. For Caudovirales of Gram-negative hosts, there are two different systems: the holin-endolysin and pinholin-SAR endolysin pathways. In the former, lysis is initiated when the holin forms micron-scale holes in the inner membrane, releasing active endolysin into the periplasm to degrade the peptidoglycan. In the latter, lysis begins when the pinholin causes depolarization of the membrane, which activates the secreted SAR endolysin. Historically, the disruption of the first two barriers of the cell envelope was thought to be necessary and sufficient for lysis of Gram-negative hosts. However, recently a third functional class of lysis proteins, the spanins, has been shown to be required for outer membrane disruption. Spanins are so named because they form a protein bridge that connects both membranes. Most phages produce a two-component spanin complex, composed of an outer membrane lipoprotein (o-spanin) and an inner membrane protein (i-spanin) with a predominantly coiled-coil periplasmic domain. Some phages have a different type of spanin which spans the periplasm as a single molecule, by virtue of an N-terminal lipoprotein signal and a C-terminal transmembrane domain. Evidence is reviewed supporting a model in which the spanins function by fusing the inner membrane and outer membrane. Moreover, it is proposed that spanin function is inhibited by the meshwork of the peptidoglycan, thus coupling the spanin step to the first two steps mediated by the holin and endolysin.

Indexed as

BacteriolysisBacteriophagesCell WallDNAEvolution, MolecularGene Expression Regulation, BacterialGene Expression Regulation, ViralGram-Negative BacteriaMembrane FusionN-Acetylmuramoyl-L-alanine AmidaseSignal TransductionViral Proteinsbacteriophage lambda lysis effector protein S105DNAN-Acetylmuramoyl-L-alanine AmidaseViral Proteinsantiholinendolysinevolutionholinlysismultigene lysispinholinsingle gene lysisspanin

Identifiers

PMID30635077
PMCPMC6733033
OpenAlexW2903176883

What OpenQuestion holds

Textmetadata
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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.