Terradot lab

One-shot design of functional protein binders with BindCraft - Nature BindCraft, an open-source, automated pipeline for de novo protein binder design with experimental success rates of 10–100%, leverages AlphaFold2 weights to generate binders with nanomolar affinity without the need for high-throughput screening.

BindCraft: an AlphaFold2-powered de novo protein binder design tool 🧬✨
Tested in some bacterial systems too! Designs so far are short peptides or mini-domains. Looking forward to long/full protein design ahead! 🧪 #microsky
www.nature.com/articles/s41...

Still Time to read this new study form Mathilde Guzzo’s Lab post doc @cjresearch.bsky.social with our structural contribution !

We will have soon an Open position for a PhD thesis position to work on bacterial secretion systems !

Stay tuned !!

Open position !!
Either at the Engineer or post-doctoral level, to work on filamentous phages. Collaboration between Laetitia Houot's group and Thierry Doan @thicoz.bsky.social.
To apply at the E level:
emploi.cnrs.fr/Offres/CDD/U...
To apply at the post-doc level:
emploi.cnrs.fr/Offres/CDD/U...

Widespread deployment of the human CD38 ADP-ribosyl cyclase fold in antibacterial and anti-eukaryotic polymorphic toxins Bacterial polymorphic toxins are modular weapons that mediate inter-microbial competition and host interactions by delivering diverse cytotoxic domains through specialized secretion systems. Here, we ...

Happy to share our work on a T6SS effector with ADP ribose cyclase activity, published in JBC @asbmbjournals.bsky.social
Great work of Julius Martinkus @jmartinkus.bsky.social and (always) great collaboration with @dukasju.bsky.social and @laurentterradot.bsky.social
www.jbc.org/article/S002...

Congratulation to all ! Fantastic work

🌿Congrats to the Equipe Projet VERT: Marine Blanc, Sandrine Magnard, Lauriane Lecoq (MMSB UMR 5086), Sandrine Vadon-Le Goff (LBTI UMR 5305), Nicolas Grimault (IBCP UAR 3760) and Virginie Gueguen-Chaignon (SFR Biosciences UAR 3444) for their Cristal Collectif Medal!
✨Towards more sustainable science!

We have an open engineer position to work on type IX secretion (T9SS), under the supervision of @doan_thierry (collab with HP Fierobe & A. Tolonen). 1-year contract, renewable up to 3.5 years. Please apply here or forward to anyone potentially interested:

emploi.cnrs.fr/Offres/CDD/U...

The 4th edition of the Integrative Structural Biology Meeting (BSI) will take place in Bordeaux, from December 15th to 19th, 2025

#CryoEM #XmasBSI

bsi4.org

Einenkel et al 𝘕𝘢𝘵 𝘔𝘪𝘤𝘳𝘰 🦠

Cryo-EM structures of the complete 𝘚𝘢𝘭𝘮𝘰𝘯𝘦𝘭𝘭𝘢 extracellular flagellum—including the FliD cap complex and hook–filament junction. Flagellin subunits assemble while the junction buffers mechanical stress → stable motility and colonization.

www.nature.com/articles/s41...

Structural dynamics of DNA unwinding by a replicative helicase | Nature Hexameric helicases are nucleotide-driven molecular machines that unwind DNA to initiate replication across all domains of life. Despite decades of intensive study, several critical aspects of their function remain unresolved1: the site and mechanism of DNA strand separation, the mechanics of unwinding propagation, and the dynamic relationship between nucleotide hydrolysis and DNA movement. Here, using cryo-electron microscopy (cryo-EM), we show that the simian virus 40 large tumour antigen (LTag) helicase assembles in the form of head-to-head hexamers at replication origins, melting DNA at two symmetrically positioned sites to establish bidirectional replication forks. Through continuous heterogeneity analysis2, we characterize the conformational landscape of LTag on forked DNA under catalytic conditions, demonstrating coordinated motions that drive DNA translocation and unwinding. We show that the helicase pulls the tracking strand through DNA-binding loops lining the central channel

New insights! Cryo-EM reveals structural dynamics of simian virus 40 helicase: DNA strand separation and unwinding mechanics detailed after decades—must explore! PMID:40108462, Nature 2025, @Nature https://doi.org/10.1038/s41586-025-08766-w #Medsky #Pharmsky #RNA #ASHG #ESHG 🧪

Zoom into a human cell infected by Shigella, the bacteria behind dysentery. Using cryo-EM, @leaswistak.bsky.social and team revealed how it pierces cells with molecular syringes. Stunning science at the nanoscale.

@enningalab.bsky.social @jytinevez.bsky.social @nanoimaging.bsky.social

#CryoEM

This is completely mad.
We must, as a community, do something about this #cryoem

Huge shoutout to 3 amazing woman scientists at MMSB recently recognized with major research awards!
🌟 Dr Anja Böckmann–Impulscience® grant
🌟 Dr Mathilde Guzzo–FEBS Excellence Award
🌟 Dr Anne Chevallereau–FSER Dotation
Brilliant science, strong leadership, powered by women!💪🔬#WomenInScience #CNRS

Beautiful work ! Congratulations Nathan et al.

Congratulations to all !

Structural Basis of Lipopolysaccharide Assembly by the Outer Membrane Translocon Holo-Complex Lipopolysaccharide (LPS) assembly at the surfaces-exposed leaflet of the bacterial outer membrane (OM) is mediated by the OM LPS translocon. An essential transmembrane beta-barrel protein, LptD, and a...

Here our new preprint on the LPS holo-translocon doi.org/10.1101/2025... , collaboration with Yves Quentin @JulieMarcoux @fronzeslab.bsky.social @pstansfeld.bsky.social - @cbitoulouse.bsky.social

Félicitations à @annechevallereau.bsky.social lauréate 2025 de la Fondation Schlumberger ! 🏆
Ses recherches sur les interactions entre bactéries pathogènes et bactériophages ouvrent la voie à de nouvelles thérapies contre les infections.

👋 @cnrs-rhoneauvergne.bsky.social

Félicitations Anne !

Please RT. Post-doc opportunity alert! 💥 Come join our team (thelowlab.org) at Imperial, London, working on bacterial secretion systems. The position is funded by the Wellcome Trust.

For more details and to apply please see

www.imperial.ac.uk/jobs/search-...

YouTube’s play button doing the lord’s work

French scientist denied US entry after phone messages critical of Trump found France’s research minister said the scientist was traveling to Houston for a conference when his phone was searched

www.theguardian.com/us-news/2025...

Etats-Unis : un chercheur français refoulé pour avoir exprimé « une opinion personnelle sur la politique menée par l’administration Trump » Le ministre de la recherche français a dit sa « préoccupation », mercredi, après cette décision des autorités américaines. Le chercheur du CNRS aurait subi un contrôle aléatoire à son arrivée, avant q...

Effrayant

www.lemonde.fr/internationa...

ICYMI, NIH will be asking soon for each NIH-funded researcher to justify every draw they make (often several times a week) on their grants and every NIH officer and their boss will have to justify their agreeing on these draws.

This is the death of US biomedical research by a thousand cuts

Left: WHIX can carry two flanking domains for secretion via the T6SS. AlphaFold 3 structure predictions of Awe1 (top) or Awe1 in complex with AwiU and AwiD lacking their predicted N-terminal signal peptides (bottom). The first part of the Awe1 WHIX domain is colored blue (amino acids 148–301); the second part of WHIX (amino acids 500–699) is colored magenta; the N-terminal (N-ter) Awe1 domain fused to WHIX (amino acids 1–147) is colored orange; the C-terminal (C-ter) Awe1 domain fused to WHIX (amino acids 700–862) is colored beige; AwiU is colored green; AwiD is colored purple. Right: AlphaFold structure prediction of the complex assembled by an Awe1 monomer and a VgrG4 trimer, shown as a ribbon representation. The inset is a close-up view of the predicted Awe1-VgrG4 interacting region. VgrG4 and Awe1 residues predicted to interact with each other are represented in green and orange, respectively.

Secretion mechanisms of many T6SS effectors in Gram-neg #bacteria remain unclear. @drdorsalomon.bsky.social &co identify a new class of #T6SS effectors, which can harbor either 1 or 2 toxic domains and use the WHIX domain as a secretion motif🧪 @plosbiology.org plos.io/4iCxVL3

Molecular basis of ParA ATPase activation by the CTPase ParB during bacterial chromosome segregation DNA segregation by bacterial ParABS systems is mediated by transient tethering interactions between nucleoid-bound dimers of the ATPase ParA and centromere (parS)-associated complexes of the clamp-for...

Interested in the bacterial ParABS DNA segregation system? Then have a look at our latest preprint... 🧬

Thanks to the Hennig and Bange groups for the great collaboration!

doi.org/10.1101/2025...

Left: WHIX can carry two flanking domains for secretion via the T6SS. AlphaFold 3 structure predictions of Awe1 (top) or Awe1 in complex with AwiU and AwiD lacking their predicted N-terminal signal peptides (bottom). The first part of the Awe1 WHIX domain is colored blue (amino acids 148–301); the second part of WHIX (amino acids 500–699) is colored magenta; the N-terminal (N-ter) Awe1 domain fused to WHIX (amino acids 1–147) is colored orange; the C-terminal (C-ter) Awe1 domain fused to WHIX (amino acids 700–862) is colored beige; AwiU is colored green; AwiD is colored purple. Right: AlphaFold structure prediction of the complex assembled by an Awe1 monomer and a VgrG4 trimer, shown as a ribbon representation. The inset is a close-up view of the predicted Awe1-VgrG4 interacting region. VgrG4 and Awe1 residues predicted to interact with each other are represented in green and orange, respectively.

Secretion mechanisms of many T6SS effectors in Gram-neg #bacteria remain unclear. @drdorsalomon.bsky.social &co identify a new class of #T6SS effectors, which can harbor either 1 or 2 toxic domains and use the WHIX domain as a secretion motif🧪 @plosbiology.org plos.io/4iCxVL3

The Journées Sécrétion are back!

2nd and 3rd October in Marseille

Keynote lecture by: @archaellum.bsky.social

Registration is open until May 15: forms.gle/2qxHntTktoxw...

Organized by Romé Voulhoux @lcbofficiel.bsky.social, @cascaleslab.bsky.social, Thierry Doan, @juliengiraud.bsky.social

This image shows the new Cryo-electron microscope JEOL ARM 200 installed on the TEM2C platform in Rennes, France, together with Reynald Gillet (Left, Director of the Institute of Genetics and Development of Rennes), and Denis Chrétien (right, in charge of the project).

Scrat (JEOL ARM 200) is now installed in Rennes with a Direct Electron Apollo camera. Don't hesitate to get in touch if you need nice SPA or cryo-electron tomography (single and dual axis) data 😍
biosit.univ-rennes.fr/en/tem2c
#CryoEM