Congratulations to everyone involved: @IBaudrexel, @l_masu, @SusanneReinhar3, Jisoo Kwon, Ondřej Skořepa, Maite Llop, Sylvia Herter, Marina Bacac and Christian Klein. (6/6).Read the full story here:

The shift from Type II to Type I function reveals a structure–function continuum for anti-CD20 antibodies, showing that receptor arrangements dictate mechanism of action. RESI provides a platform for structure-guided antibody development, applicable far beyond CD20. (5/6)

We showed a direct link between CD20 oligomerization and function by investigating OBZ-based T-cell engagers (TCEs). An increased IgG flexibility in the 2+1 TCE format lead to increased CD20 tetramerization, without higher-order clustering, reducing direct cytotoxicity. (4/6)

In contrast, Type II antibodies like Obinutuzumab and H299 induced limited oligomerization to dimers, trimers and tetramers, consistent with their role in promoting direct tumor cell death rather than complement activation. (3/6)

By imaging intact cells, we could see these therapeutic antibodies in action: Type I antibodies like Rituximab and Ofatumumab formed extended chains of CD20 hexamers or larger, creating platforms compatible with complement protein binding, mediating cancer cell killing. (2/6)

Ever wondered what happens when therapeutic antibodies bind to cancer cells? In our latest study, we used multiplexed 3D-RESI to directly visualize how anti-CD20 antibodies interact with their receptors, revealing their precise arrangement at single-protein resolution. (1/6)

We're excited that the study is now out in Nature Nanotechnology @NatureNano

RT @LMoeckl: Very happy to see this one out - the first molecular-resolution imaging of glycocalyx components in their native environment!….

RT @MPI_Biochem: Congratulations to Ralf on your election as a new EMBO member:. ❕Original press release from @EMBO: .

@MoniqueHonsa, @PhilippSteen, Larissa Heinze, Shuhan Xu, @heerpa, @IBaudrexel, @SusanneReinhar3, Ana Perovic, Jisoo Kwon, Ethan Oxley, Ross Dickins, @IkbenMaartje, @IanParish_AU.

Big congrats to @l_masu and @rafalkowalew who led the project as well as other co-authors that contributed to this work!!.

To facilitate SPINNA’s widespread use in the scientific community, we offer an open-source Python implementation and a GUI available in the latest version of Picasso (. 7/7

Finally, we investigate the dimerization of CD80 and PD-L1, key surface ligands involved in immune cell signaling. 6/7

We further quantitatively evaluate the oligomerization of the Epidermal Growth Factor Receptor (EGFR) upon binding of its ligand, EGF. 5/7

We demonstrate SPINNA in DNA-origami, showing that it can infer not only the stoichiometry of the oligomers but also different spatial conformations. 4/7

Here, we present SPINNA (Single-Protein Investigation via Nearest Neighbor Analysis): an analysis framework that compares nearest neighbor distances from experimental single-protein data with those from realistic simulations based on a model of protein oligomerization states. 3/7

Latest advances in super-resolution microscopy (DNA-PAINT, MINFLUX, RESI) allow the study of molecular arrangements at the level of single proteins, but extracting quantitative information on the 1–20 nm scale through rigorous image analysis remains a significant challenge. 2/7

Understanding how proteins assemble into complexes (oligomerize) within their native cellular environments is crucial for deciphering cellular signaling pathways 1/7.

Spatial and stoichiometric in situ analysis of biomolecular oligomerization at single-protein resolution. We are excited to present our latest work published in @NatureComms .

A huge thank you to all authors and collaborators whose dedication and teamwork made this protocol possible! @EduardUnterauer @EvaSchentarra @jekriste @MarrCarsten @FelipeOpaz_o @euforna.Let us know if you’re ready to generate your own single-cell spatial proteomics atlases! 🚀.