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The latest research from our team is out in Cell @cp-cell.bsky.social! We used #cryo-EM, #imaging, #BRET, and #biosensors targeted to the lysosome to understand how the KICSTOR-GATOR1 complex turns off #mTORC1 in response to low levels of amino acids.

Enteroviruses cause over a billion infections each year, but the details of how their genomes capture host ribosomes have remained elusive. I'm pleased to share a new preprint from Miguel in our group, providing some new insights into this problem: www.biorxiv.org/content/10.1...

I'm deeply honoured & grateful to have been awarded the #CSLCentenaryFellowship at the #AAHMS dinner last week Many thanks to my mentors & colleagues for their support Congratulations to my Fellow winner @rhyswg.bsky.social #MedicalResearch #CSLCentenaryFellowships #WomenInSTEMM @mcri.bsky.social

⁉️The ARC has delayed outcomes of ALL grants 1–4 months & increased scheduled outcome windows from 2 weeks to 3 months! This reverses 4 years of progress in providing greater certainty & ability to plan for researchers, their families & unis. Their excuse? Security checks under new ARC legislation👇

Happy to finally share the amazing results of our long-term collaboration with Karin Reinisch’s lab on how bridge lipid-transfer proteins (BLTPs) cooperate with partner proteins to orchestrate lipid delivery. A quick thread (1/7) www.biorxiv.org/content/10.6...

Check out our preprint in which we determine how a class of potent protein antibiotics specifically kill P. aeruginosa without a need to enter the cell. doi.org/10.1101/2025... This is work from my PhD in the lab of @rhyswg.bsky.social and many collaborators who contributed amazing data!

💊 We are excited to share our preprint that describes an inhibitor of the widespread and highly conserved Two-Partner Secretion (TPS) system that is critical for Gram-negative pathogens to export a multitude of diverse virulence factors. (1/6) www.biorxiv.org/content/10.6...

Two-partner secretion system transporter proteins (TpsB) are widely conserved across Gram-negative pathogens. TpsB family proteins secrete exoprotein virulence factors that perform a myriad of functions such as adhesion and immune modulation. Despite their incredible importance in bacterial infectious disease, TpsB inhibitors have not yet been discovered. Here, we describe a potent inhibitor of FhaC, a TpsB protein produced by Bordetella spp . FhaC secretes the exoprotein FhaB that is essential for the establishment of whooping cough. We designed a peptide called P1 that we predicted would prevent substrate binding and lock FhaC in a secretion-inactive state. Simulations and biochemical assays supported our hypothesis and identified interactions important for P1 binding to FhaC. Strikingly, we observed that the peptide strongly inhibited FhaB secretion from clinical isolates and broadly reduced correlates of virulence. Together, this work provides a strong case for further development of a novel class of anti-TpsB anti-virulence compounds. ### Competing Interest Statement The authors have declared no competing interest. National Institute of Allergy and Infectious Diseases, R21AI180112

ARC says Discovery Projects outcomes will be tomorrow (Tuesday). Linkage Projects (2025, round 1) on Wed. Over past ~year, it's often been at about 11am (Canberra). My bot will pick up the change to RMS & post immediately. ARC should email outcomes to lead CIs, but might take an 1hr or so for DPs