GasderMIN system

traitmech:000336 · CLASS · PROPOSED

A phage defense system in which an organism possesses a bacterial gasdermin locus represented by the DefenseFinder GasderMIN__bGSDM profile, whose bGSDM effectors are associated with bacteriophage defense and can be proteolytically activated in characterized bGSDM-protease systems to assemble membrane pores, disrupt membrane integrity, and execute cell death.

Trait evidence (10)

DOI:10.1126/science.abj8432
We discovered gasdermin homologs encoded in bacteria that defended against phages and executed cell death.

Johnson et al. support bacterial gasdermin homologs as phage-defense proteins that execute cell death.
https://pmc.ncbi.nlm.nih.gov/articles/PMC9134750/
bGSDM-protease systems are found in diverse bacteria and archaea, as well as in metagenomic samples of prokaryotic origin

Johnson et al. report bGSDM-protease systems across bacteria, archaea, and prokaryotic metagenomic samples, supporting curation above one engineered locus.
https://pmc.ncbi.nlm.nih.gov/articles/PMC9134750/
a four gene operon from Lysobacter enzymogenes exhibited robust defense against coliphages T4, T5, and T6

Johnson et al. experimentally tested a Lysobacter enzymogenes bGSDM-containing operon that defended against coliphages T4, T5, and T6.
https://pmc.ncbi.nlm.nih.gov/articles/PMC9134750/
Deletion of the bGSDM gene from the Lysobacter operon abolished protection

Deletion of the bGSDM gene from the Lysobacter operon abolished the observed phage protection.
DOI:10.1126/science.abj8432
Bacterial gasdermins were activated by dedicated caspase-like proteases that catalyzed site-specific cleavage and the removal of an inhibitory C-terminal peptide.

Johnson et al. connect bacterial gasdermin activation to dedicated caspase-like proteases that remove an inhibitory C-terminal peptide.
DOI:10.1126/science.abj8432
Release of autoinhibition induced the assembly of large and heterogeneous pores that disrupted membrane integrity.

Johnson et al. support pore assembly and membrane disruption as outputs of bacterial gasdermin autoinhibition release.
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/List_system_article.md
GasderMIN | 10\.1101/2021\.06\.07\.447441 | Bacterial gasdermins reveal an ancient mechanism of cell death

The DefenseFinder article registry maps the GasderMIN model namespace to the Johnson et al. bacterial gasdermin preprint, later published under DOI:10.1126/science.abj8432.
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/Liste_hmm_system.md
| GasderMIN__bGSDM | GasderMIN__bGSDM___bGSDM | GasderMIN | Custom | 50 |

The DefenseFinder HMM inventory records the bGSDM profile under the GasderMIN model namespace.
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsv
GasderMIN GasderMIN 1 1 GasderMIN__bGSDM

The DefenseFinder rules table models GasderMIN as a one-mandatory-profile system requiring GasderMIN__bGSDM.
https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsv
CARD_NLR CARD_NLR_GasderMIN 1 3 GasderMIN__bGSDM CARD_NLR__CARD_Protease, CARD_NLR__NLR_new, CARD_NLR__Trypsin CARD_NLR__Endonuclease, CARD_NLR__Endonuclease_new, CARD_NLR__Phospho, CARD_NLR__Phospho_Trypsin, CARD_NLR__Subtilase, CARD_NLR__Subtilase_long_new, CARD_NLR__Subtilase_small_new, CARD_NLR__Trypsin_Phospho, CARD_NLR__Trypsine_Endonuclease_new

The DefenseFinder rules table also models a CARD_NLR_GasderMIN subtype with GasderMIN__bGSDM as its mandatory profile.

GasderMIN activation forms lethal membrane pores

System-level sketch linking a bacterial gasdermin locus to phage defense-system possession and linking characterized bGSDM-protease systems to caspase-like proteolytic activation, gasdermin pore assembly, membrane disruption, and cell death.

NONMECHANISTIC · The graph captures GasderMIN as a named DefenseFinder single-mandatory-profile system supported by Johnson et al. bacterial gasdermin experiments while leaving the natural phage trigger, the universality of adjacent protease activation, the full family breadth, and CARD-NLR-associated gasdermin variants unresolved.

Edge evidence

bacterial gasdermin locus contributes to caspase-like bGSDM cleavage RO:0002326
Characterized bacterial gasdermin-protease loci can encode dedicated caspase-like proteases that cleave bGSDM effectors and remove their inhibitory C-terminal peptide.
- https://pmc.ncbi.nlm.nih.gov/articles/PMC9134750/ bGSDM-protease systems are found in diverse bacteria and archaea, as well as in metagenomic samples of prokaryotic origin Johnson et al. describe bGSDM-protease systems across prokaryotic genomes and metagenomes.
- DOI:10.1126/science.abj8432 Bacterial gasdermins were activated by dedicated caspase-like proteases that catalyzed site-specific cleavage and the removal of an inhibitory C-terminal peptide. Johnson et al. support caspase-like proteases as direct activators of bacterial gasdermins.
caspase-like bGSDM cleavage contributes to bacterial gasdermin pore assembly RO:0002326
Proteolytic release of the inhibitory bacterial gasdermin peptide induces large pore assembly.
- DOI:10.1126/science.abj8432 Release of autoinhibition induced the assembly of large and heterogeneous pores that disrupted membrane integrity. Johnson et al. connect release of autoinhibition to gasdermin pore assembly.
- https://pmc.ncbi.nlm.nih.gov/articles/PMC9134750/ The Runella bGSDM and protease only induced cellular toxicity when expressed together The Runella bGSDM system required both bGSDM and its protease to trigger cellular toxicity.
bacterial gasdermin pore assembly contributes to membrane integrity disruption RO:0002326
Activated bacterial gasdermins assemble pores that disrupt membrane integrity.
- DOI:10.1126/science.abj8432 Release of autoinhibition induced the assembly of large and heterogeneous pores that disrupted membrane integrity. Johnson et al. link bacterial gasdermin pore assembly to disrupted membrane integrity.
membrane integrity disruption contributes to gasdermin-dependent cell death RO:0002326
Bacterial gasdermin activation can execute cell death through loss of membrane integrity.
- DOI:10.1126/science.abj8432 We discovered gasdermin homologs encoded in bacteria that defended against phages and executed cell death. Johnson et al. identify bacterial gasdermins as phage-defense homologs that execute cell death.
bacterial gasdermin locus contributes to GasderMIN system RO:0002326
The GasderMIN DefenseFinder model identifies a GasderMIN__bGSDM profile, and Johnson et al. show that deleting a bGSDM gene can abolish phage protection by a gasdermin operon.
- https://pmc.ncbi.nlm.nih.gov/articles/PMC9134750/ a four gene operon from Lysobacter enzymogenes exhibited robust defense against coliphages T4, T5, and T6 The tested Lysobacter enzymogenes bGSDM-containing operon protected cells from coliphage challenge.
- https://pmc.ncbi.nlm.nih.gov/articles/PMC9134750/ Deletion of the bGSDM gene from the Lysobacter operon abolished protection The bGSDM gene was essential for the Lysobacter operon's observed phage protection.
- https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/Liste_hmm_system.md | GasderMIN__bGSDM | GasderMIN__bGSDM___bGSDM | GasderMIN | Custom | 50 | The DefenseFinder HMM inventory records the bGSDM profile under the GasderMIN model namespace.
- https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsv GasderMIN GasderMIN 1 1 GasderMIN__bGSDM The DefenseFinder rules table models GasderMIN as a one-mandatory-profile system requiring GasderMIN__bGSDM.
gasdermin-dependent cell death contributes to GasderMIN system RO:0002326
Bacterial gasdermin-mediated cell death realizes the GasderMIN phage-defense-system output in tested bGSDM-protease systems.
- DOI:10.1126/science.abj8432 We discovered gasdermin homologs encoded in bacteria that defended against phages and executed cell death. Johnson et al. connect bacterial gasdermin phage defense with cell death.
GasderMIN system is a phage defense system rdfs:subClassOf
GasderMIN system possession is a bacterial gasdermin phage-defense-system trait.
- https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/List_system_article.md GasderMIN | 10\.1101/2021\.06\.07\.447441 | Bacterial gasdermins reveal an ancient mechanism of cell death The DefenseFinder article registry maps the GasderMIN model namespace to the Johnson et al. bacterial gasdermin preprint, later published under DOI:10.1126/science.abj8432.
- https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/DefenseFinder_rules.tsv GasderMIN GasderMIN 1 1 GasderMIN__bGSDM The DefenseFinder rules table models GasderMIN as a one-mandatory-profile system requiring GasderMIN__bGSDM.

Provenance

Identifier source: TraitMech local identifier
Definition source: DOI:10.1126/science.abj8432

Parent traits (1)

phage defense system traitmech:000209

Synonyms (2)

GasderMIN RELATED_SYNONYM · https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/List_system_article.md
GasderMIN__bGSDM RELATED_SYNONYM · https://raw.githubusercontent.com/mdmparis/defense-finder-models/afb0e5a8b466be53586b13266f5d38d98c3ac268/Liste_hmm_system.md

kg-microbe context

No kg-microbe node embedding matched this record in the 2026-04-25 deepwalk.

Canonical examples (1)

Organisms cited as exemplars of this trait. Taxon ids are NCBITaxon and link out to the NCBI record.

Lysobacter enzymogenes NCBITaxon:69 DOI:10.1126/science.abj8432 Johnson et al. showed that a Lysobacter enzymogenes bGSDM-containing operon provided robust defense against coliphages T4, T5, and T6 in an Escherichia coli heterologous assay, and that deleting the bGSDM gene abolished protection.

Discussions and Knowledge Gaps (1)

Open questions attached to this trait. Seeded by just knowledge-gap-scan and curated; see the corpus-wide index.

Resolve natural GasderMIN family breadth and CARD-NLR gasdermin context before minting narrower gasdermin subfamily traits.

KNOWLEDGE GAP OPEN gasdermin-family-breadth-and-card-nlr-scope-gap · raised by codex · 2026-09-21

Attached to causal_graphs#gasdermin_proteolysis_triggers_pore_cell_death

Johnson et al. experimentally tested a Lysobacter bGSDM-containing operon and mechanistically dissected Runella bGSDM protease-triggered toxicity, while some bacterial gasdermins showed no discernible phage restriction in Escherichia coli and the GasderMIN__bGSDM profile is also used in CARD-NLR detector contexts in the pinned DefenseFinder rules table. This record captures the standalone GasderMIN detector namespace and leaves CARD-NLR-associated gasdermins, natural phage triggers, and broader family boundaries unresolved.

Curation history

2026-09-21T13:10:00Z · MINTED_TRAITMECH_ID · codex
Minted GasderMIN system as a DOI-backed GENOMICS TraitRecord under the phage defense system parent after an ignored-and-hidden duplicate review found no exact live TraitMech, METPO, history, or prior proposal record; the replacement placeholder is reserved in proposals/metpo_traitmech_v213.