The Lysis cassette of jumbophage PhiKZ

Pseudomonas jumbophage phiKZ is prominent because of the proteinaceous nuclear structure that is formed during the infection cycle, protecting the replicating phage DNA from host nucleases. Progress has been made in deciphering the molecular basis of nucleus formation and other unique aspects of phiKZ biology, but the understanding of how it causes host lysis remains minimal. Here we present bioinformatic, physiological and molecular evidence for a "lysis cassette", the expression of which is necessary and sufficient for the temporally regulated disruption of the host envelope. This cluster contains genes for the usual components of an MGL (multigene lysis) system, including the holin, endolysin, i-spanin and o-spanin. In addition, a fifth gene in the cluster, encoding a cytoplasmic protein, was found to accelerate the timing of holin-mediated lethality when expressed in trans. Evidence is provided that suggests this lysis regulator protein interacts with the cytoplasmic domain of the phiKZ class III holin. In support of this notion, alpha-fold analysis generated a high-confidence structure of a conserved holin-lysis regulator heterodimer complex. Infections at high multiplicity resulted in slower bulk culture lysis profiles than at low multiplicity, suggesting that phiKZ might have a lysis-inhibition system.

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Publication Details

Journal
Scientific Reports
Published
2026-01-20
DOI
https://doi.org/10.1038/s41598-026-36188-9
Primary Topic
Bacteriophages and microbial interactions
Type
article
Field-Weighted Citation Impact
0.00

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article

The Lysis cassette of jumbophage PhiKZ

Gabriella Ganser, K. Sharp, Ry Young, Joshua Wan et al.
Scientific Reports
Bacteriophages and microbial interactions
article

The Lysis cassette of jumbophage PhiKZ

Gabriella Ganser, K. Sharp, Ry Young, Joshua Wan, Prasanth Manohar
article en

Abstract

Pseudomonas jumbophage phiKZ is prominent because of the proteinaceous nuclear structure that is formed during the infection cycle, protecting the replicating phage DNA from host nucleases. Progress has been made in deciphering the molecular basis of nucleus formation and other unique aspects of phiKZ biology, but the understanding of how it causes host lysis remains minimal. Here we present bioinformatic, physiological and molecular evidence for a "lysis cassette", the expression of which is necessary and sufficient for the temporally regulated disruption of the host envelope. This cluster contains genes for the usual components of an MGL (multigene lysis) system, including the holin, endolysin, i-spanin and o-spanin. In addition, a fifth gene in the cluster, encoding a cytoplasmic protein, was found to accelerate the timing of holin-mediated lethality when expressed in trans. Evidence is provided that suggests this lysis regulator protein interacts with the cytoplasmic domain of the phiKZ class III holin. In support of this notion, alpha-fold analysis generated a high-confidence structure of a conserved holin-lysis regulator heterodimer complex. Infections at high multiplicity resulted in slower bulk culture lysis profiles than at low multiplicity, suggesting that phiKZ might have a lysis-inhibition system.

Scientific ReportsVol. 16(1)
The University of Texas MD Anderson Cancer Center (US), Texas A&M University System (US), Texas A&M University (US)
Universität Basel, National Institute of General Medical Sciences
Openalex Percentile: Top 86%
Bacteriophages and microbial interactions
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