From c80a12f9c0cf0d7b449a2ce220c1bf4b1230a639 Mon Sep 17 00:00:00 2001 From: ftesson <florian.tesson@cri-paris.org> Date: Wed, 17 Jan 2024 10:28:02 +0100 Subject: [PATCH] Update thoeris.md --- content/3.defense-systems/thoeris.md | 11 +++++------ 1 file changed, 5 insertions(+), 6 deletions(-) diff --git a/content/3.defense-systems/thoeris.md b/content/3.defense-systems/thoeris.md index a7511d05..43e92a29 100644 --- a/content/3.defense-systems/thoeris.md +++ b/content/3.defense-systems/thoeris.md @@ -21,18 +21,17 @@ relevantAbstracts: # Thoeris ## Description -Thoeris is a two-gene defense system identified in more than 2000 bacterial genomes. It consists of the genes thsA and thsB. Its anti-phage function was experimentally validated in _Bacillus subtilis_. In response to phage infection, it produces an isomer of cyclic ADP-ribose, which leads to depletion of NAD+ and results in abortive infection. +Thoeris is a two-gene defense system identified in more than 2000 bacterial genomes. It consists of the genes ThsA and thsB. Its anti-phage function was experimentally validated in *Bacillus subtilis* :ref{doi=10.1126/science.aar4120}. In response to phage infection, it produces an isomer of cyclic ADP-ribose, which leads to depletion of NAD+ and results in abortive infection. -ThsA contains the sirtuin-like domain which binds to nicotinamide adenine dinucleotide (NAD) metabolites. The N112A point mutation neutralizes the Thoeris defense system and abolishes the NAD+ hydrolase activity of thsA. It lacks a N-terminal transmembrane domain, and is predicted to be cytoplasmic. - -ThsB is proposed to participate in the recognition of phage infection, as various thsB proteins sense different phage components.ThsB is found in more than 50% of Thoeris systems in multiple diverse copies. +ThsA contains the sirtuin-like domain which binds to nicotinamide adenine dinucleotide (NAD) metabolites. The N112A point mutation neutralizes the Thoeris defense system and abolishes the NAD+ hydrolase activity of thsA :ref{doi=10.1126/science.aar4120}. It lacks a N-terminal transmembrane domain, and is predicted to be cytoplasmic. +ThsB contains a TIR domain :ref{doi=10.1126/science.aar4120} is proposed to participate in the recognition of phage infection, as various thsB proteins sense different phage components.ThsB is found in more than 50% of Thoeris systems in multiple diverse copies :ref{doi=10.1126/science.aar4120}. ## Molecular mechanism -The Thoeris system is believed to function by degrading NAD+ (a cofactor of central metabolism) to stop the growth of phage-infected cells and prevent the transmission of the phage to neighboring bacteria. +The Thoeris system functions by degrading NAD+ (a cofactor of central metabolism) to stop the growth of phage-infected cells and prevent the transmission of the phage to neighboring bacteria :ref{doi=10.1038/s41467-020-16703-w}. -The protein ThsB, featuring the TIR domain, plays a cruial role in identifying phage invasion. Upon detecting the infection, the TIR domain becomes enzymatically active, initiating the synthesis of a cADPR isomer molecule. This molecule acts as a signal, binding to the ThsA effector, likely through its C-terminal SLOG domain, thereby activating its NADase activity. Consequently, the NADase effector reduces NAD+ cellular levels, creating an environment unsuitable for phage replication. +The protein ThsB, featuring the TIR domain, plays a cruial role in identifying phage invasion. Upon detecting the infection, the TIR domain becomes enzymatically active, initiating the synthesis of a cADPR isomer molecule :ref{doi=10.1038/s41586-021-04098-7}. This molecule acts as a signal, binding to the ThsA effector, likely through its C-terminal SLOG domain, thereby activating its NADase activity :ref{doi=10.1038/s41586-021-04098-7}. Consequently, the NADase effector reduces NAD+ cellular levels, creating an environment unsuitable for phage replication :ref{doi=10.1038/s41586-021-04098-7,10.1038/s41467-020-16703-w}. ## Example of genomic structure -- GitLab