Evidence map›Paper›PMID 42008678›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2026

Bacteriophages target membrane-anchored glycopolymers to promote host cell lysis and progeny release.

Amelia C McKitterick, Evan W Lyerly, Thomas G Bernhardt

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Article
  2. Article
  3. Phage N4 uses a SAR endolysin-holin system for host cell lysis.bioRxiv : the preprint server for biology · 2025
    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

3 authors.

Amelia C McKitterickDepartment of Microbiology, Harvard Medical School, Boston, MA 02115.
Evan W LyerlyDepartment of Microbiology, Harvard Medical School, Boston, MA 02115.ORCID 0009-0001-2273-1707
Thomas G BernhardtDepartment of Microbiology, Harvard Medical School, Boston, MA 02115.ORCID 0000-0003-3566-7756

Funding

HHMI (HHMI) NA
6 · The paper itself

Abstract

Most bacteriophages lyse their host cell to release progeny virions. Double-stranded DNA phages typically promote host lysis using a holin-endolysin system. Holins form pores in the cytoplasmic membrane allowing endolysins access to the peptidoglycan (PG) cell wall, which they degrade to weaken the cell envelope and promote osmotic lysis. Phages that infect Proteobacteria also encode a spanin in their lysis cassette that functions to disrupt the host outer membrane (OM). The spanin-requirement for cell lysis provided the first clue that the proteobacterial OM confers mechanical rigidity to the cell envelope. Corynebacteria and mycobacteria also build an OM, but it is made of mycolic acids instead of lipopolysaccharides. Here, we investigated whether the mycomembrane presents a mechanical barrier to phage-induced lysis of corynebacteria. In addition to annotated holin and endolysin genes, mycobacteriophages and corynephages were found to encode a membrane protein we call LysZ in their lysis cassettes. Deletion of

Indexed as

BacteriolysisBacteriophagesMycobacteriophagesVirus ReleaseCell MembraneCell WallCorynebacteriumCorynebacterium glutamicumEndopeptidasesLipopolysaccharidesPeptidoglycanViral ProteinsendolysinEndopeptidasesLipopolysaccharidesPeptidoglycanViral Proteinscorynebacteriaglycopolymersmycobacteriaphage

Identifiers

PMID42008678
PMCPMC13123898

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.