Search bioRxiv⌕ Search

bioRxiv · 10.1101/2025.09.16.676641

Correlative MS Imaging for cellular identification and analysis of in situ cryo-ET

Abstract

In situ cryo-electron tomography (cryo-ET) offers direct access to protein structures in their native state and environment. A central challenge for this technique is the identification and classification of imaged cells, as sample heterogeneity with respect to cell type and functional state can significantly impact the data. Currently, cells can be classified using subtomogram averaging or fluorescent labeling, which require sufficiently distinguishable macromolecules, genetic modifications, or the availability of suitable labels. In MALDI-MS Imaging (MSI) individual cells can be identified and classified reliably, making use of the distributions of phospholipid species, metabolites and small proteins with characteristic profiles for specific cell types. Here we present an integrated pipeline combining MSI and in situ cryo-ET for single-cell identification and classification. Our approach enables MSI data acquisition directly from EM grids and can be used on any eukaryotic single-cell cryo-ET sample without prior modification in less than 36 h. We apply this workflow to describe cell-to-cell heterogeneity in cultured HeLa cells, to distinguish between distantly related HeLa and Polytomella cells, and between primary cultured rat neurons and glial cells. Finally we present a data integration workflow combining cryo-ET, light microscopy and MSI aligned in the same coordinate system to facilitate efficient data visualization and interpretation. We anticipate that this approach will change the way that structural biologists can approach cellular heterogeneity in cryo-ET, as cells can be identified and classified reliably post acquisition.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

Schwarz, A., Meier-Credo, J., Behrens, A., Reichert, J., Dietrich, L., Schuman, E. M., Langer, J. D.. 2025-09-18. Correlative MS Imaging for cellular identification and analysis of in situ cryo-ET. https://doi.org/10.1101/2025.09.16.676641

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related preprints

Design of colipids with controlled lateral distance of head group moieties for targeting strategies in the field of lipid-based nanoparticles

Lipid nanoparticles and liposomes are nanoparticle drug formulations which are firmly established in clinics. In order to expand their application and improve efficacy, surface modifications can be a key strategy, especially for cell specific targeting. Targeting can be achieved by integrating ligand functionalized lipids or lipidoids on the nanoparticle surface. In this case, not solely the targeting ligand itself, but also the structure of the whole targeting lipid/lipidoid can affect the interaction of the targeting ligand with the binding motive on cells. Especially, distal spacer structures between lipid anchor and ligand unit, often composed of polyethylene glycol chains, provide a certain distance of the ligand from the nanoparticle surface. A concept which is currently neglected is the control of the lateral distance between ligand structures on the nanoparticle. Herein we investigated the possibility to design lipidoids with a lateral spacer composed of polyethylene glycol units. We synthesized and characterized different lipidoids which provide a primary amine in the head group for possible ligand coupling. In our model lipidoids the head groups were functionalized with a paramagnetic probe to apply electron paramagnetic resonance (EPR) methods for the characterization of the lipidoid interaction with model nanoparticles, in our case liposomes. Continuous wave EPR was used to study the efficiency of the novel lipidoids to integrate into lipid bilayers of model liposomes, which was shown to depend on lipidoid structure and liposome composition. Furthermore, using double electron-electron resonance (DEER), we observed lipidoid conformational changes occurring upon integration into liposomes.

biophysics↗

Binding mechanisms of therapeutic antibodies to human claudin-18.2

Claudin-18.2 (CLDN18.2) is a tight junction component with highly restricted expression in the paracellular space of nonmalignant gastric epithelial cells. It becomes accessible on tumor cell surface during malignant transformation, making CLDN18.2 an attractive target for targeted therapies against gastric cancer. Recently, zolbetuximab has become the first FDA-approved monoclonal antibody that targets CLDN18.2 in advanced gastric cancer, and others like osemitamab have entered phase 3 clinical trials. However, the high-resolution structure of CLDN18.2 is lacking, and how CLDN18.2 is recognized by therapeutic antibodies remains undefined. Here, we report cryo-EM structures of human claudin-18.2 (hCLDN18.2) in complex with the Fab fragments of zolbetuximab and osemitamab, revealing the structure of hCLDN18.2 and its binding mechanism to the therapeutic antibodies. Further analyses reveal that three residues in the first extracellular loop of hCLDN18.2 that are different from human claudin-18.1 (hCLDN18.1) play a critical role in antibody binding. Our data elucidate the structural basis for selective binding of therapeutic antibodies to hCLDN18.2, which should aid rational design of next-generation immunotherapies targeting hCLDN18.2.

biophysics↗

Structural relationships between the SLC12 cotransporter C-terminal domain, universal stress proteins and adenylating enzymes

Several SLC12 cotransporters bind ATP in a cytoplasmic C-terminal domain (CTD). We analysed 16,192 CTD-containing SLC12 sequences and compared 42,845 representative structures to examine the relationship between this nucleotide site, universal stress proteins (USPs) and adenylating enzymes. In phosphorylated NKCC1, D891 and D927 lie near the ATP phosphate chain, while R801 and K889 form a basic phosphate-binding clamp. NKCC1 retains this arrangement, whereas KCC paralogs replace or lose several corresponding groups. In structural comparisons with USP and adenylating-enzyme references, both CTD lobes score between universal stress proteins and EC-annotated domains, and the two lobes form separate lineages that include bacterial transporters. Lobe-specific and nucleotide-frame comparisons place ATP in the corresponding structural region used for -phosphate chemistry by catalytic members of this fold. Published work on UspG provides a precedent for protein-bound AMP in a natural USP. In the examined SLC12 structures and USP models, candidate protein hydroxyls lack an in-line geometry for attack at ATP P. Protein adenylation would require a change in protein or nucleotide geometry, or a different acceptor. These results define a structural basis for testing conditional protein adenylation at SLC12 nucleotide sites. The required evidence is a covalent protein-AMP adduct, identification of its acceptor and measurement of the expected pyrophosphate coproduct, with soluble nucleotide analysis to distinguish accompanying ATP reactions.

biophysics↗