diff --git a/content/3.defense-systems/gasdermin.md b/content/3.defense-systems/gasdermin.md
index 09df1a0e85735d0c3da77613c14924c731c4c66e..e2eb4fc99e384c62e3182be94d6776b1fe7d0deb 100644
--- a/content/3.defense-systems/gasdermin.md
+++ b/content/3.defense-systems/gasdermin.md
@@ -6,12 +6,27 @@ tableColumns:
       doi: 10.1126/science.abj8432
       abstract: |
         Gasdermin proteins form large membrane pores in human cells that release immune cytokines and induce lytic cell death. Gasdermin pore formation is triggered by caspase-mediated cleavage during inflammasome signaling and is critical for defense against pathogens and cancer. We discovered gasdermin homologs encoded in bacteria that defended against phages and executed cell death. Structures of bacterial gasdermins revealed a conserved pore-forming domain that was stabilized in the inactive state with a buried lipid modification. Bacterial gasdermins were activated by dedicated caspase-like proteases that catalyzed site-specific cleavage and the removal of an inhibitory C-terminal peptide. Release of autoinhibition induced the assembly of large and heterogeneous pores that disrupted membrane integrity. Thus, pyroptosis is an ancient form of regulated cell death shared between bacteria and animals.
-    Sensor: Unknown
+    Sensor: Phage protein
     Activator: Unknown
     Effector: Membrane disrupting
+contributors: 
+  - Aude Bernheim
+relevantAbstracts:
+- doi: 10.1126/science.abj8432
+- doi: 10.1101/2023.05.28.542683
 ---
 
 # GasderMIN
+
+
+## Description
+
+Gasdermin proteins were initially discovered in humans. Recently there 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 experession of a 4-genes operon from Lysobacter in E. coli :ref{doi=10.1126/science.abj8432} :ref{doi=10.1101/2023.05.28.542683}. 
+
+## Molecular Mechanism
+
+Akin to their human counterparts, bacterial gasdermins encode a C-terminal inhibotry domain. Following phage infection, proteases associated to bacterial gasdermin cleave this domain triggering oligomerization of gasdermins into large, membrane-breaching pores :ref{doi=10.1126/science.abj8432} 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 RexAB system was shown to activate gasdermin. It was further shown that CARD domain are also essential in bacterial gasdermins defense :ref{doi=10.1101/2023.05.28.542683}.
+
 ## Example of genomic structure
 
 The GasderMIN system is composed of one protein: bGSDM.
@@ -105,12 +120,4 @@ end
     style Title3 fill:none,stroke:none,stroke-width:none
     style Title4 fill:none,stroke:none,stroke-width:none
 </mermaid>
-## Relevant abstracts
-
-::relevant-abstracts
----
-items:
-    - doi: 10.1126/science.abj8432
 
----
-::