Time for a thread!🧵 How different is the molecular organization of thylakoids in “higher” plants🌱? To find out, we teamed up with @profmattjohnson.bsky.social to dive into spinach chloroplasts with #CryoET ❄️🔬. Curious? ..Read on!

#TeamTomo #PlantScience 🧪 🧶🧬 🌾
elifesciences.org/articles/105...
1/🧵

I am excited to share our new preprint on the CAGE complex, a mysterious hollow protein complex that I first saw years ago while surveying Tetrahymena ciliary lysate www.biorxiv.org/content/10.1... #cilia #protistsonsky 🧬🧪

Was lucky to see this presented at the NYC cryoEM meeting earlier this year - super cool stuff!

NEW Review from @soreklab.bsky.social @dinahoch.bsky.social explains how immune pathways manipulate the availability of nucleotides, chemically modify nucleotides to generate immune signalling molecules, and produce altered nucleotides that poison viral replication
#immunosky #microsky #phagesky

Excited this paper is finally published! We focused on the inner concave surface of LRR RKs to expand bacterial flagellin perception in plants. Selection indicates expanded perception is more common than previously thought. Experiments led by @jerrytli.bsky.social www.nature.com/articles/s41...

Thank you, JC! 😊

Thank you, Sam!😊

And a special shout-out to @kamounlab.bsky.social for his unwavering support on this journey exploring AVRcap1b from Phytophthora infestans – the infamous Irish potato famine pathogen. 🥔🦠
10/10

Huge thanks to Ben and all our fantastic co-authors (‪@adelineharant.bsky.social @mpcontreras.bsky.social @Liang-Yu Hou @Chih-Hang Wu ‪@kamounlab.bsky.social‬) who made this story possible.
Here’s that amazing movie by Ben again!
9/10

Our model: Once activated, dissociated NRC protomers assemble in a stepwise manner to form a full hexameric resistosome. AVRcap1b blocks this process, capturing NRC assembly intermediates and relocating them via the TOL-ESCRT pathway.
Effector biology rocks! #EffectorWisdom
8/10

Remember TOL? How does it bind to AVRcap1b compared to SlNRC3? Turns out, they bind to opposite interfaces on AVRcap1b! This supports a dual-targeting mechanism, with the effector linking ‘immune suppression’ to ‘membrane trafficking’
🧊 SlNRC3–AVRcap1b (cryoEM)
🧬 AVRcap1b–TOL (PDB:9RDC)
7/10

It turns out we could use AVRcap1b as a molecular trap to capture other NRC assembly intermediates. One AVRcap1b truncation captured an SlNRC3 assembly intermediate with four protomers.
Cool! NRC resistosomes assemble in a stepwise process!
6/10

Through its L-shaped structure, AVRcap1b sterically blocks the SlNRC3 resistosome by forming contacts with three protomers (half the hexameric resistosome)!
5/10

What’s this intriguing complex? Together with Ben, we purified the AVRcap1b-SlNRC3 complex from our favourite plant—the Aussie wonder Nicotiana benthamiana aka benthi—and resolved this beautiful cryo-EM structure and see how AVRcap1b wraps around three SlNRC3 protomers!
4/10

What sort of complex does AVRcap1b form with activated NRCs? Blue Native-PAGE assays revealed an intermediate complex. Instead of the expected NRC hexamer, we saw an intriguing smaller band that contains both tomato NRC3 and Phytophthora AVRcap1b 🤔
3/10

It turned out AVRcap1b associates only with the activated NRCs, but not their resting state. Check this super co-IP experiment from our previous paper:
bsky.app/profile/kamo...
2/10

We’re building on the recent structure of L-shaped AVRcap1b effector in complex with a host TOL9 protein. This effector bridges TOL9 and NRC helpers to suppress immunity 👇
bsky.app/profile/mpco...
2/10

🚨 New @biorxivpreprint alert! 🚨
We are thrilled to share our latest findings—building on our earlier work on suppressors of helper NLRs of the NRC family—a Phytophthora infestans L-shaped effector captures resistosome assembly intermediates of tomato NRC3!
www.biorxiv.org/content/10.1...
1/10

A co-IP masterclass. Courtesy of Madhu
@jmadhuprakash.bsky.social

A plant pathogen effector blocks stepwise assembly of a helper NLR resistosome https://www.biorxiv.org/content/10.1101/2025.07.14.664264v1