Search bioRxiv⌕ Search

Biology subjects

Kosinski, J.

Publications and source records attributed to Kosinski, J..

At least 19 recordsLinked to original sources

Constrained template matching using rejection sampling

Identifying macromolecular complexes in situ using cryo-electron tomography remains challenging, with low signal-to-noise ratios, the missing wedge, and crowded backgrounds among the key limiting factors. By integrating prior knowledge on macromolecular localization, such as the preferred orientations of membrane-associated proteins, detection can be improved by constraining searches to biologically feasible orientations. Here we describe rejection sampling, an approach for integrating such constraints at voxel resolution that remains both accurate and computationally efficient. Using synthetic and experimental data, we show that these constraints improve detection, orientational assignment, and discrimination between macromolecules. The resulting picks match the performance of deep-learning methods informed by membrane structure without requiring annotated data. We further apply rejection sampling to ATP synthase on mitochondrial cristae, illustrating how it extends macromolecular detection to the large and highly curved membrane systems that pervade cells.

biophysics↗

Helfrich Monte Carlo Flexible Fitting: physics-based, data-driven cell-scale simulations

Simulating entire cells represents the next frontier of computational biology. Achieving this goal requires methods that accurately describe cellular membranes across spatial and temporal scales. Although three-dimensional electron microscopy enables detailed membrane visualization, limitations on acquisition geometry, data quality, and field-of-view often result in fragmented membrane representations incompatible with simulations. To resolve this, here we introduce Helfrich Monte Carlo Flexible Fitting (HMFF), an approach that integrates experimental density data into physical simulations to determine membrane structure. Through the accompanying Mosaic software platform, we apply HMFF to influenza virus particles, Mycoplasma pneumoniae cells, and entire eukaryotic organelles. The resulting models enable multi-scale simulations spanning millions of lipids and proteins at experimentally determined positions, support quantitative morphological analysis, assess uncertainty in membrane localization, and reveal physical effects implicit in the data. Together, these capabilities establish a foundation for data-driven whole-cell simulations.

biophysics↗

In-cell discovery and characterization of a non-canonical bacterial protein translocation-folding complex

Cryo-electron tomography has emerged as powerful technology for in-cell structural biology, and in combination with breakthroughs in protein structure prediction, offers a unique opportunity for illuminating functions of previously uncharacterized macromolecular complexes. Here, we used the genome-reduced bacterium Mycoplasma pneumoniae as a minimal cell model, and determined in-cell maps of an unknown complex located at the cell surface. By combining proteomics, structure prediction, and bioinformatics, we identified the complex to include the conserved Sec-translocon and an extracellular dome-like structure largely formed by three uncharacterized proteins (Mdps). The Mdps show structural homology to a periplasmic ATP-independent foldase, PrsA, with Mdp444 retaining key catalytic residues. Our study provides the first sub-nanometer resolution maps of the complete bacterial Sec-translocation machinery, depicting several conformational states that allow us to suggest a model for translocation initiation, and revealing its coordination with a novel, extracellular, protein-folding system.

molecular biology↗

Snapshot of in-cell protein contact sites reveals new host factors and hijacking of paraspeckles during influenza A virus infection

Influenza A virus (IAV) hijacks host cellular machinery, but many virus-IAV interactions and contacting protein sites remain uncharacterised, particularly those dependent on intact cellular architecture, such as membrane-associated or phase-separated compartments. Here, we applied in-cell cross-linking mass spectrometry (XL-MS), integrated with AlphaFold-based structural modelling and functional assays, to map protein-protein contact sites in IAV-infected human cells. This approach revealed previously unrecognised virus-host interactions linked to spatially organised processes, including the maturation pathway of HA through the membrane-bound ER- Golgi system, the novel interaction of M2 with the membrane-embedded LAT1 amino acid transporter, and the progressive disassembly of paraspeckles-phase-separated compartments in the nucleus. We validate M2-LAT1 interaction and paraspeckle disassembly in human primary lung epithelial cells and show that the paraspeckle disassembly constitutes a new and unique infection mechanism through which IAV releases RNA-binding proteins that support viral RNA replication. These findings advance the understanding of IAV manipulation of host cellular processes and illustrate how the integrative in-cell structural system biology approach captures native host-pathogen interactomes, infection pathways, and host cell perturbations.

microbiology↗

AlphaPulldown2 - A General Pipeline for High-Throughput Structural Modeling

AlphaPulldown2 streamlines protein structural modeling by automating workflows, improving code adaptability, and optimizing data management for large-scale applications. It introduces an automated Snakemake pipeline, compressed data storage, support for additional modeling backends like UniFold and AlphaLink2, and a range of other improvements. These upgrades make AlphaPulldown2 a versatile platform for predicting both binary interactions and complex multi-unit assemblies. AvailabilityAlphaPulldown2 is freely available at https://github.com/KosinskiLab/AlphaPulldown.

bioinformatics↗

Improving AlphaFold 3 structural modeling by incorporating explicit crosslinks

AlphaFold 3 has significantly advanced the modeling of macromolecular structures, including proteins, DNA, RNA, and their interactions with small molecules or post-translational modifications. However, challenges remain when modeling specific structural conformations or complexes with limited evolutionary data, such as protein-antibody complexes. Previous studies with AlphaFold2 demonstrated that adding distance restraints from crosslinking mass spectrometry (XL-MS) can improve predictions for such cases. In this study, we investigate whether XL-MS restraints can be incorporated into AlphaFold 3 by explicitly modeling crosslinks as covalently-bound ligands. Our results show that this approach is able to increase the accuracy of AlphaFold 3 models. We explore the opportunities and limitations of this method, which has been implemented as a proof-of-concept pipeline named AF3x, available at https://github.com/KosinskiLab/af3x.

molecular biology↗

Nuclear pores as conduits for fluid flow during osmotic stress

Changing environmental conditions necessitate an immediate cellular adaptation to ensure survival. Dictyostelium discoideum, a bacteriovore slime mold present in the soil of most terrestrial ecosystems, is known for its ability to tolerate drastic changes in osmolarity. How the cells cope with the resulting mechanical stress remains understudied. Here we show that D. discoideum has extraordinarily elaborate and resilient nuclear pores that serve as conduits for massive fluid exchange between cytosol and nucleus. We capitalize on the unique properties of D. discoideum cells to quantify flow across the nuclear envelope that is necessitated by changing nuclear size in response to osmotic stress. Based on mathematical concepts adapted from hydrodynamics, we conceptualize this phenomenon as porous flow across nuclear pores. This type of fluid flow is distinct from the canonically characterized modes of nucleocytoplasmic transport, i.e. passive diffusion and active nuclear transport, because of its dependence on pressure. Our insights are relevant in any biological condition that necessitates rapid nuclear size changes, which includes metastasizing cancer cells squeezing through constrictions, migrating cells and differentiating tissues.

cell biology↗

PyTME (Python Template Matching Engine): A fast, flexible, and multi-purpose template matching library for cryogenic electron microscopy data

Cryogenic electron microscopy (cryo-EM) is a key method in structural and cell biology. Analysis of cryo-EM images requires interpretation of noisy, low-resolution densities which relies on identifying the most probable orientation of macromolecules in a target using template matching. Many method-specific template matching software exist for single-particle cryo-EM, cryo-electron tomography (cryo-ET), or fitting atomic structures into averaged 3D maps of macromolecules. Here, we report the Python Template Matching Engine (pyTME), a software engine that consolidates method-specific template matching problems. The underlying library provides highly efficient template-matching implementation and abstract data structures for storing and manipulating input and output data. It scales favorable to large datasets, both with multiple CPUs and GPUs, compared to existing software enabling template matching of even unbinned cryo-ET data in hours, which was previously nearly impossible due to technical restraints. Any hardware-specific optimization needed for dealing with large data is automatically performed to increase ease of use and minimize user intervention. The efficiency and simplicity of pyTME will enable high throughput mining of a variety of cryo-EM and ET datasets in the future.

bioinformatics↗

The Shape of Things in Cryo-ET: Why Emojis Aren't Just for Texts

Detecting specific biological macromolecules in cryogenic electron tomography (cryo-ET) data is frequently approached by applying cross-correlation-based 3D template matching. To reduce computational cost and noise, high binning is used to aggregate voxels before template matching. This remains a prevalent practice in both practical applications and method development. Here, we systematically evaluate the relation between template size, shape, and angular sampling to identify ribosomes in a ground truth annotated dataset. We show that at the commonly used binning, a detailed subtomogram average, a sphere, and the heart emoji [Formula] results in near-identical performance. Our findings indicate that with current template-matching practices, macromolecules can only be detected with high precision if their shape and size are sufficiently different from the background. Using theoretical considerations we rationalize our experimental results and discuss why at high binning, primarily low-frequency information remains and that template matching fails to be accurate because similarly shaped and sized macromolecules have similar low-frequency spectrums. We discuss these challenges and propose potential enhancements for future template-matching methodologies.

biophysics↗

Identifying repurposed drugs with moderate anti-influenza virus activity through computational prioritization of drug-target pairs

Influenza A virus (IAV) causes up to five million cases of severe illness and half a million deaths worldwide each year. While there are a few clinically approved drugs for treating IAV, they are challenged by the rapid evolution of the virus leading to emergence of drug resistance and the adverse effects of the drugs. Targeting host cellular factors that support virus replication could limit resistance, increase the broad-spectrum antiviral properties of drugs, and benefit from repurposing drugs already existing against those factors. However, selecting the right drug-target pairs with low toxicity and minimal adverse effects has been challenging, even though hundreds of cellular host factors have been identified. In this study, we applied a computational and knowledge-based drug-target prioritization approach to identify promising drug-target pairs. We selected five pairs for experimental validation: telmisartan-Angiotensin II receptor, type 1 (AGTR1), metoclopramide hydrochloride-Cholinergic receptor muscarinic 1 (CHRM1), cefepime hydrochloride-phosphogluconate dehydrogenase (PGD), ranolazine dihydrochloride-sodium channel voltage-gated type v alpha subunit (SCN5A), and ofloxacin-topoisomerase II alpha 170kDa (TOP2A). Except for cefepime hydrochloride, all four drugs showed significant plaque reduction in Madin Darby canine kidney (MDCK) cells. In the immunofluorescence assay, metoclopramide hydrochloride, ranolazine dihydrochloride, and telmisartan showed antiviral activity in MDCK and/or adenocarcinoma human alveolar basal epithelial (A549) cell lines. In conclusion, our approach can prioritize and identify drugs with antiviral activity against influenza virus. Refining and strengthening such approaches could be valuable for rapid antiviral discovery and pandemic preparedness. HighlightsO_LIComputational drug-target prioritization indicated drugs for validation C_LIO_LITelmisartan showed anti-influenza virus activity in MDCK cells C_LIO_LIMetoclopramide and ranolazine showed anti-influenza activity in A549 and MDCK cells C_LI

systems biology↗

ColabSeg: An interactive tool for editing, processing, and visualizing membrane segmentations from cryo-ET data

Cellular cryo-electron tomography (cryo-ET) has emerged as a key method to unravel the spatial and structural complexity of cells in their near-native state at unprecedented molecular resolution. To enable quantitative analysis of the complex shapes and morphologies of lipid membranes, the noisy three-dimensional (3D) volumes must be segmented. Despite recent advances, this task often requires considerable user intervention to curate the resulting seg-mentations. Here, we present ColabSeg, a Python-based tool for processing, visualizing, cleaning, and fitting membrane segmentations from cryo-ET data for downstream analysis. ColabSeg makes many well-established algorithms for point-cloud processing easily available to the broad community of structural biologists for applications in cryo-ET through its graphical user interface (GUI). We demonstrate the usefulness of the tool with a range of use cases and biological examples. Finally, for a large Mycoplasma pneumoniae dataset of 50 tomograms, we show how ColabSeg enables high-throughput membrane segmentation, which can be used as valuable training dataset for fully automated convolutional neural network (CNN)-based segmentation.

bioinformatics↗

An RNA to rule them all: Critical steps in Lassa virus ribonucleoparticle assembly and recruitment

Lassa virus is a negative-strand RNA virus with only four structural proteins that causes periodic outbreaks in West Africa. The nucleoprotein (NP) encapsidates the viral genome, forming the ribonucleoprotein complexes (RNPs) together with the viral RNA and the L protein. RNPs have to be continuously restructured during viral genome replication and transcription. The Z protein is important for membrane recruitment of RNPs, viral particle assembly and budding, and has also been shown to interact with the L protein. However, the interaction of NP, viral RNA and Z is poorly understood. Here, we characterize the interactions between Lassa virus NP, Z and RNA using structural mass spectrometry. We identify the presence of RNA as the driver for disassembly of ring-like NP trimers, a storage form, into monomers to subsequently form higher order RNA-bound NP assemblies. We locate the interaction site of Z and NP and demonstrate that while NP binds Z independently of the presence of RNA, this interaction is pH-dependent. These data improve our understanding of RNP assembly, recruitment and release in Lassa virus.

biophysics↗

The distance between the plasma membrane and the actomyosin cortex acts as a nanogate to control cell surface mechanics

Animal cell shape changes are controlled by the actomyosin cortex, a peripheral actin network tethered to the plasma membrane by membrane-to-cortex attachment (MCA) proteins. Previous studies have focused on how myosin motors or actin turnover can generate the local deformations required for morphogenesis. However, how the cell controls local actin nucleation remains poorly understood. By combining molecular engineering with biophysical approaches and in situ characterization of cortical actin network architecture, we show that membrane-to-cortex tethering determines the distance between the plasma membrane and the actomyosin cortex at the nanoscale of single actin nucleators. In turn, the size of this gap dictates actin filament production and the mechanical properties of the cell surface. Specifically, it tunes formin activity, controlling actin bundling and cortical tension. Our study defines the membrane-to-cortex distance as a nanogate that cells can open or close by MCA proteins to control the activity of key molecules at the cell surface.

biophysics↗

AlphaPulldown - a Python package for protein-protein interaction screens using AlphaFold-Multimer

SummaryThe Artificial Intelligence-based structure prediction program AlphaFold-Multimer enabled structural modelling of protein complexes with unprecedented accuracy. Increasingly, AlphaFold-Multimer is also used to discover new protein-protein interactions. Here, we present AlphaPulldown, a Python package that streamlines protein-protein interaction screens and high-throughput modelling of higher-order oligomers using AlphaFold-Multimer. It provides a convenient command line interface, a variety of confidence scores, and a graphical analysis tool. Availability and implementationAlphaPulldown is freely available at https://www.embl-hamburg.de/AlphaPulldown.

bioinformatics↗

Form follows function: Variable microtubule architecture in the malaria parasite

The malaria parasite undergoes a series of extensive morphological changes within its human host and mosquito vector. A scaffold of microtubules beneath a peripheral double membrane establishes and maintains the distinct shapes of all infectious forms, but the underlying structural basis remains unknown. Here we applied in situ electron cryo-tomography after focused ion beam milling to follow changes in the microtubule cytoskeleton throughout the Plasmodium life cycle. This revealed an unexpected level of structural and architectural diversity so far not observed in other organisms. Microtubules in migrating mosquito forms consist of 13 protofilaments reinforced by interrupted luminal helices. Conversely, gametocyte microtubules consist of 13 to 18 protofilaments with doublets, triplets and quadruplets of varying arrangements. We show the microtubule cytoskeleton within the native cellular context, highlighting structurally diverse apical rings which act as microtubule organising centres. This provides a unique view into a relevant human pathogen with an unusual microtubule cytoskeleton.

microbiology↗

Artificial intelligence reveals nuclear pore complexity

Nuclear pore complexes (NPCs) mediate nucleocytoplasmic transport. Their intricate 120 MDa architecture remains incompletely understood. Here, we report a near-complete structural model of the human NPC scaffold with explicit membrane and in multiple conformational states. We combined AI-based structure prediction with in situ and in cellulo cryo-electron tomography and integrative modeling. We show that linker Nups spatially organize the scaffold within and across subcomplexes to establish the higher-order structure. Microsecond-long molecular dynamics simulations suggest that the scaffold is not required to stabilize the inner and outer nuclear membrane fusion, but rather widens the central pore. Our work exemplifies how AI-based modeling can be integrated with in situ structural biology to understand subcellular architecture across spatial organization levels. One sentence summaryAn AI-based, dynamic model of the human nuclear pore complex reveals how the protein scaffold and the nuclear envelope are coupled inside cells.

molecular biology↗

Integrative structural modelling of macromolecular complexes using Assembline

Integrative modelling enables structure determination of macromolecular complexes by combining data from multiple experimental sources such as X-ray crystallography, electron microscopy (EM), or crosslinking mass spectrometry (XL-MS). It is particularly useful for complexes not amenable to high-resolution EM--complexes that are flexible, heterogenous, or imaged in cells with cryo-electron tomography. We have recently developed an integrative modelling protocol that allowed us to model multi-megadalton complexes as large as the nuclear pore complex. Here, we describe the Assembline software package, which combines multiple programs and libraries with our own algorithms in a streamlined modelling pipeline. Assembline builds ensembles of models satisfying data from atomic structures or homology models, EM maps and other experimental data, and provides tools for their analysis. Comparing to other methods, Assembline enables efficient sampling of conformational space through a multi-step procedure, provides new modeling restraints, and includes a unique configuration system for setting up the modelling project. Our protocol achieves exhaustive sampling in less than 100 - 1,000 CPU-hours even for complexes in the megadalton range. For larger complexes, resources available in institutional or public computer clusters are needed and sufficient to run the protocol. We also provide step-by-step instructions for preparing the input, running the core modelling steps, and assessing modelling performance at any stage.

bioinformatics↗

Structure of the mycobacterial ESX-5 Type VII Secretion System hexameric pore complex

To establish an infection, pathogenic mycobacteria use the Type VII secretion or ESX system to secrete virulence proteins across their cell envelope. The five ESX systems (ESX-1 to ESX-5) have evolved diverse functions in the cell, with the ESX-5 found almost exclusively in pathogens. Here we present a high-resolution cryo-electron microscopy structure of the hexameric ESX-5 Type VII secretion system. This 2.1 MDa membrane protein complex is built by a total of 30 subunits from six protomeric units, which are composed of the core components EccB5, EccC5, two copies of EccD5, and EccE5. The hexameric assembly of the overall ESX-5 complex is defined by specific inter-protomer interactions mediated by EccB5 and EccC5. The central transmembrane pore is formed by six pairs of EccC5 transmembrane helices that adopt a closed conformation in the absence of substrate in our structure. On the periplasmic face of the ESX-5 complex, we observe an extended arrangement of the six EccB5 subunits around a central cleft. Our structural findings provide molecular details of ESX-5 assembly and observations of the central secretion pore, which reveal insights into possible gating mechanisms used to regulate the transport of substrates.

microbiology↗