Review article with Omer Dushek @tcell.bsky.social on tethered signaling proteins, out now! Tethered bio-molecular reactions can do at least 7 cool things that freely-diffusing reactions do not. Read more here! #IDR #TCells #cytoskeleton
www.annualreviews.org/content/jour...
A new study from the @tcell.bsky.social lab demonstrates a novel strategy to reduce dangerous off-target effects in engineered T cell therapies.
Find out more: www.path.ox.ac.uk/news-article...
#Immunotherapy #TCells #CancerResearch #BiomedicalEngineering #OpenAccess #NatureBiomedicalEngineering
The work was led by our talented student Jose Cabezas Caballero (now a postdoc with Mala Maini) and huge thanks to all the co-authors and collaborators who made this work possible, and to Springer Nature Biomedical Engineering for an efficient review process.
This approach offers a universal method to generate highly selective therapeutic T cells for any TCR, potentially improving both the safety and effectiveness of adoptive immunotherapy for a wide range of targets.
Our work shows that by modulating co-signalling receptors on T cells (such as switching CD8 for CD4), we can significantly and selectively reduce lower-affinity off-target activation while keeping higher-affinity antitumor target efficacy intact.
In this study, we explore a novel strategy to enhance the safety of T cell immunotherapies. Traditional engineered T cell receptors (TCR-T) can sometimes cross-react with unintended lower-affinity targets, leading to harmful side effects.
🚀 Our new Publication in Nature Biomedical Engineering!🎉
📄 Title: Generation of T cells with reduced off-target cross-reactivities by engineering co-signalling receptors
🔗 Read the full paper here: www.nature.com/articles/s41...
The work was lead by Anna H. with support from many lab members, a fantastic collaboration with Audrey Gerard with support from Wellcome Trust and BBSRC. Thank you to EMBO Journal for a constructive and efficient review process.
We suggest that T cells 'force-shield' their TCR/pMHC interactions at interfaces to faithfully measure their affinities.
We show that despite the enormous molecular complexity at T cell interfaces (with target cells), the 3D affinity measured with purified TCR and pMHC in SPR can accurately predict the OT-I T cell response.
With a News & Views by Pierre Bongrand and Philippe Robert
Unraveling T-cell decoding strategy: a step forward
www.embopress.org/doi/full/10....
Our work accurately measuring the 3D affinity between the OT-I TCR and a large number of foreign and self antigen ligands is now published at EMBO Journal.
Murine T-cell receptor OT-I exhibits imperfect discrimination between foreign and self-antigens
www.embopress.org/doi/full/10....
Murine T-cell receptor OT-I exhibits imperfect discrimination between foreign and self-antigens
Omer Dushek @tcell.bsky.social and colleagues show that 3D solution affinities of the OT-I TCR for foreign and self-antigens predict functional T-cell responses
www.embopress.org/doi/full/10....
UK NK 2026 in Cardiff.
January 9th. Be there.
eventbrite.co.uk/e/uk-nk-confer…
Hosted by Rich Stanton, Ceri Fielding & Eddie Wang
I was Chair of @biologists.bsky.social when we started this initiative, the brainwave of the @stevenkelly.bsky.social
It was an imaginative idea and I am thrilled to see this landmark
Remember: @biologists.bsky.social are the goodies in scientific publishing!
We can make the flexibility of a model match the hypothesis being tested -- more flexibility is not always better, if it prohibits rejection of the hypothesis. Here is one simple case involving T cells where it made a difference!
www.biorxiv.org/content/10.1...
If you're a postdoc interested in starting your own group, please consider the Dunn School at Oxford, UK.
It's a fantastic department and university for molecular immunology and all aspects of immune research!
Temporal control of cytokine production is lost in 2nd-gen CAR-T cells, says Patel et al. This could be key to understanding their efficacy and toxicity in cancer immunotherapy. 🧬
🔗 https://bit.ly/4lOLicw
#CancerImmunotherapy
Thanks to our funding, collaborators, constructive reviewers, and for the very efficient process at Immunology & Cell Biology!
By comparing the advantages and limitations of each platform, we provide a framework to choose the most suitable system to study signal integration in both basic and translational contexts.
A recently developed CombiCell system enables easy manipulation of ligands while conserving key biophysical properties.
In contrast, solid surfaces or supported lipid bilayers allow easy manipulation of ligands but lack the biophysical properties of cells, such as softness, a glycocalyx, and/or ligand mobility.
Although genetically modified antigen-presenting cells (APCs) offer the most physiological system, manipulating their ligands is difficult and slow.
We review and compare the available platforms, focusing on T-cell recognition.
Since they encounter a huge variety of normal and abnormal cells, they experience many different combinations and concentrations of ligands.
Understanding immune responses therefore requires platforms that enable ligands to be easily manipulated.
Immune cells interact directly with other cells and make decisions by integrating information from many different receptor–ligand interactions at these cell–cell interfaces.
Our new review article led by Jordan Kramer:
Platforms for studying cell–cell recognition by immune cells
onlinelibrary.wiley.com/doi/10.1111/...
biomembrane-days-2025.mpikg.mpg.de
📢 Registration is open for the Biomembrane Days 2025!
🔗 biomembrane-days-2025.mpikg.mpg.de
A top-notch lineup of speakers, 120 posters, 200 scientists.
📜Submit an abstract by July 14
🏆3 Poster prizes
⚠️Limited spots-previous events were fully booked!
#BiomembraneDays2025 #Biophysics #CellMembranes
The original manuscript was published in @embojournal.org EMBO Journal last year
Using CombiCells, a platform for titration and combinatorial display of cell surface ligands, to study T-cell antigen sensitivity modulation by accessory receptors
www.embopress.org/doi/full/10....
