GasderMIN
Description
Gasdermin proteins were initially discovered in humans. Recently they were shown to be present in multiple bacteria, where they are almost always encoded in an operon together with a protease. The experimental validation of the antiphage activity of bacterial gasdermins was demonstrated through the heterologous expression of a 4-genes operon from Lysobacter in E. coli (N/A, N/A) .
Molecular Mechanism
Akin to their human counterparts, bacterial gasdermins encode a C-terminal inhibitory domain. Following phage infection, proteases associated with bacterial gasdermin cleave this domain triggering oligomerization of gasdermins into large, membrane-breaching pores (N/A) leading to cell death:ref{doi=10.1101/2023.05.28.542683}. As such gasdermins containing systems are abortive infection systems. rIIB, a protein allowing T6 to overcome the RexAB system was shown to activate gasdermin. It was further shown that CARD domains are also essential in bacterial gasdermins defense (N/A) .
Example of genomic structure
The GasderMIN is composed of 1 protein: bGSDM.
Here is an example found in the RefSeq database:
The GasderMIN system in Flavobacterium johnsoniae (GCF_000016645.1, NC_009441) is composed of 1 protein: bGSDM (WP_012023900.1)