By uncovering how RipAV hijacks the regulatory mechanism PUB-CPK28, and reduces BIK1 accumulation, our work reveals a sophisticated strategy of immune suppression. I would like to thank
@albertopmacho.bsky.social
and all collaborators!
@type3lab.bsky.social

@ihsmumacsic.bsky.social

This mechanism is not just incidental: we show that RipAV is required to keep BIK1 levels low during infection. Dampening BIK1 is a common virulence strategy in R. solanacearum — RipAC also reduces BIK1 levels via PUB4.
www.embopress.org/doi/full/10....

This modification promotes the proteasome-mediated degradation of BIK1, a core immune component required for pattern-triggered immunity. In other words, RipAV accelerates the removal of one of the plant’s most important defense proteins.

RipAV promotes phosphorylation of PUBs by CPK28 on a specific Thr site. This post-translational modification boosts PUB25/26 activity, as previously shown by Wang et al. (2018).
www.sciencedirect.com/science/arti...

Ralstonia solanacearum causes bacterial wilt, a devastating disease in many crops. We found that its effector RipAV directly interacts with plant ubiquitin ligases (PUBs) and the kinase CPK28, both central regulators of immune signaling.

Thanks Suayb!

As a bonus, this one comes with an always welcomed predoc contract! We'll be looking for PhD candidates soon...

Very grateful to @ageinves.bsky.social we'll try and get the most out of those funds!