A team from CEITEC Masaryk University (MUNI) in collaboration with researchers from two research institutes in Norway has, for the first time, captured how echovirus 18, a member of the enterovirus genus, releases its genetic material into cells to initiate infection. The study provides a structural view of an early stage of viral infection under near-native conditions. Using cryo-electron microscopy, the researchers discovered that the virus does not release its RNA through a small pore in its capsid, as had long been assumed. Instead, its protein shell partially disassembles, creating a large opening through which the viral genetic material escapes into the host cell. A detailed understanding of this genome release mechanism could eventually help develop compounds preventing enteroviruses from infecting cells.Enteroviruses are common human pathogens causing diseases ranging from the common cold and gastrointestinal infections to severe neurological disorders. Echovirus 18, the virus investigated in this study, is known primarily as a cause of meningitis and encephalitis in children. It belongs to the picornaviruses, a family of small, non-enveloped viruses whose genetic material is protected by a protein shell, the capsid, organized with icosahedral symmetry.To replicate within a cell, the enteroviruses must release their RNA – the molecule that carries viral genetic information – from the capsid, into the cell cytoplasm. Although this step is crucial for initiating infection, it has never been observed in infected cells.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_71d553bb0e.jpg" alt="CEITEC/Plevka Lab: CEITEC Scientists Are the First to Capture How Enteroviruses Initiate Infection: View into a cell infected by echovirus 18. Echovirus 18 is shown in green and yellow, ribosomes in violet, and actin filaments in cyan. Scale 50 nm. " srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_71d553bb0e.jpg 221w," sizes="100vw" width="1600" height="1128">“For a long time, two main theories existed about how picornaviruses deliver their RNA genomes into cells. One proposed that the genome leaves the capsid through a small opening. The other, supported by earlier work from our laboratory, suggested that the genome escapes from partially disassembled capsids missing pentamers of capsid proteins. However, both models were based on experiments with virus particles outside cells. We wanted to go one step further and see what really happens during infection inside a cell,” says <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/liya-mukhamedova-ph-d/u89248?page=publication">Liya Mukhamedova</a>, the study’s first author from CEITEC MUNI.Using cryo-electron microscopy, which allows scientists to visualize biological structures at exceptionally high resolution, the researchers observed individual echovirus 18 particles directly within infected cells. They discovered that empty virus particles in infected cells lack parts of their capsids. It is through these openings that the virus releases its RNA.The study also revealed the role of the FcRn receptor, a cell-surface molecule that enteroviruses use to enter cells. The binding of the virus to the receptor triggers structural changes in the viral particle that prime it for subsequent genome release. The team showed that receptor binding causes the loss of the so-called pocket factor, a small molecule that normally helps stabilize the virus particle. The virus otherwise remains largely intact, suggesting that receptor binding is only the first step toward uncoating, while additional factors within the cell are required to complete the process and trigger genome release.“Infection is a complex process, during which enterovirus particles sense various interactions with cell components. The binding of echovirus 18 to the FcRn host-cell receptor triggers conformational changes in the virus, priming it for genome release.” – explains <a target="_blank" rel="noopener noreferrer" href="https://www.ceitec.eu/pavel-plevka-ph-d/u26854">Pavel Plevka</a>, head of the Structural Virology Research Group.The researchers did not observe the so-called activated particles that are key intermediates in the enterovirus uncoating process. This suggests that genome release in cells occurs much faster than previous experiments had suggested.By combining structural data obtained from studies of virus particles outside living cells with observations of infected cells, the study offers a picture of how enterovirus infection begins. Moving beyond simplified experiments with isolated virus particles, it brings scientists closer to understanding the earliest stages of enterovirus infection as they occur in living cells. The study, was published in the <a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1073/pnas.2601182123">PNAS journal</a>.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_2_3601bf1df9.jpg" alt="CEITEC/Plevka Lab: CEITEC Scientists Are the First to Capture How Enteroviruses Initiate Infection: Reconstructions of E18 particles from infected cells. The particles are rainbow-colored based on the distance from the particle center. Scale 10 nm." srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_CEITEC_Vedci_z_CEITEC_jako_prvni_zachytili_jak_enteroviry_spousteji_infekci_bunek_2_3601bf1df9.jpg 245w," sizes="100vw" width="1600" height="906"><blockquote><h4>Article</h4><h4><a target="_blank" rel="noopener noreferrer" href="https://www.pnas.org/doi/10.1073/pnas.2601182123">Particles of echovirus 18 open to release their genomes in vivo</a></h4>Liya Mukhamedova, David Buchta, Zuzana Trebichalská, Yevgen Levdansky, Jana Moravcová, David Potěšil, Zbyněk Zdráhal, Dominik Hřebík, Lucie Nepovímová, Torleif Tollefsrud Gjølberg, Jan Terje Andersen, Jiří Nováček, Tibor Füzik, and Pavel PlevkaProc. Natl. Acad. Sci. U.S.A., 2026, 123, e2601182123<div>&nbsp;</div><div><a target="_blank" rel="noopener noreferrer" href="https://doi.org/10.1073/pnas.2601182123">https://doi.org/10.1073/pnas.2601182123</a></div><h6>licenced under <a target="_blank" rel="noopener noreferrer" href="https://creativecommons.org/licenses/by/4.0/">CC-BY 4.0</a></h6></blockquote><h4>Abstract</h4>Enteroviruses cause a broad spectrum of human diseases, ranging from mild respiratory or gastrointestinal infections to severe neurological disorders such as aseptic meningitis and encephalitis. Enterovirus cell entry involves receptor-mediated endocytosis followed by destabilizing rearrangements of the virus capsid that enable genome release. However, the mechanism of enterovirus genome release has not been visualized in infected cells. Here, we used cryoelectron tomography and microscopy to image echovirus 18 (E18) entry into host cells and its interaction with the neonatal Fc receptor (FcRn). 30 min postinfection, endosomes and cytoplasm contained empty capsids missing one or several pentamers of capsid proteins, providing evidence that in vivo E18 releases its genome through capsid opening. In vitro, FcRn binding induced the expulsion of pocket factors from hydrophobic pockets in VP1, priming the virus for uncoating. The cryoelectron microscopy reconstruction of genome-containing particles of E18 inside infected cells did not reveal pocket factors, indicating that receptor binding triggers the same priming process during infection. We did not detect activated particles in infected cells, suggesting that these intermediates are short-lived and rapidly release their genomes in vivo. Our results identify capsid opening as the in vivo mechanism of echovirus 18 genome release, providing structural evidence for a process previously only inferred from in vitro experiments.

CEITEC Scientists Are the First to Capture How Enteroviruses Initiate Infection 

ISC 2026 officially opened in Prague on Sunday, September 6, bringing the international separation science community together at the Prague Congress Centre. The first day began with six Short Courses covering topics from analytical procedure lifecycle and mass spectral interpretation to HILIC, oligonucleotides, LC/MS data analysis, and supercritical fluids. In the afternoon, conference chairs Michal Holčapek and Lucie Nováková welcomed participants during the Opening Ceremony, followed by the J.F.K. Huber Medal Award Ceremony. The scientific program then moved into its first plenary session, spanning spintronics, single-cell proteomics and robust LC-MS, and rapid evaporative ionisation mass spectrometry. The opening day concluded with the Welcome Reception, giving participants their first opportunity to meet colleagues from around the world and begin a week of scientific exchange, new ideas, and chromatography in the heart of Prague.<h4>Sunday, September 6th</h4><h5>8:30–15:45 Short Courses 3 - 8</h5><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ISC_ISC_2026_Day_1_Short_Courses_Koen_Sandra_176f1c6d52.jpg" alt="ISC: ISC 2026 - Day 1: Short Course SC 6 Oligonucleotides and Other Biopharmaceuticals (Koen Sandra)" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ISC_ISC_2026_Day_1_Short_Courses_Koen_Sandra_176f1c6d52.jpg 235w," sizes="100vw" width="1600" height="1067"><h5>16:00–16:30 Opening Ceremony</h5><ul><li><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/lcms/articles?search=hol%C4%8Dapek">Michal Holčapek</a>, Czech Republic</li><li><a target="_blank" rel="noopener noreferrer" href="https://labrulez.com/en-us/lcms/articles?search=Lucie+Nov%C3%A1kov%C3%A1">Lucie Nováková</a>, Czech Republic</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ISC_ISC_2026_Day_1_Opening_Novakova_and_Holcapek_bbf9dd44e3.jpg" alt="ISC: ISC 2026 - Day 1: Michal Holčapek and Lucie Nováková opened ISC 2026" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ISC_ISC_2026_Day_1_Opening_Novakova_and_Holcapek_bbf9dd44e3.jpg 235w," sizes="100vw" width="1600" height="1067"><h5>16:30–17:00 Award Ceremony</h5><ul><li>J.F.K. Huber Medal (awarded by the Austrian Society for Analytical Chemistry)</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ISC_ISC_2026_Day_1_JFK_Huber_Award_winner_Dave_846f6a5dff.jpg" alt="ISC: ISC 2026 - Day 1: Davy Guillarme as a 2026 recipient of the J.F.K. Lecture Award of the Austrian Society of Analytical Chemistry" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ISC_ISC_2026_Day_1_JFK_Huber_Award_winner_Dave_846f6a5dff.jpg 235w," sizes="100vw" width="1600" height="1066"><h4>Plenary lectures</h4><h5>17:00 - 17:30 Spintronics: A new paradigm in digital bits</h5><ul><li>Tomáš Jungwirth, Czech Republic&nbsp;&nbsp;&nbsp;&nbsp;</li></ul>Besides the rapid developments in the big world of cloud data centers and AI, a remarkable paradigm shift is occurring on the level of the smallest “elementary particle” of information technologies – the single physical bit. For the first time in the history of microprocessor chips, semiconductor bits are being replaced by a fundamentally distinct technology. The technology is based on magnets and is called spintronics. All major developers and manufacturers of the advanced chip technologies are now implementing these new spintronic bits. Not across the entire microprocessor chip, but in some of its vital memory parts. The transition to the spintronic bits is happening because further miniaturization of semiconductor bits has become prohibitively expensive or even reached fundamental physical limits. In the talk we will introduce the distinct physical principle behind the spintronic bits, and highlight some of the recent adbances in spintronics research and development.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ISC_ISC_2026_Day_1_Tomas_Jungwirth_dd6eeca2b5.jpg" alt="ISC: ISC 2026 - Day 1: Spintronics: A new paradigm in digital bits (Tomáš Jungwirth, Czech Republic)" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ISC_ISC_2026_Day_1_Tomas_Jungwirth_dd6eeca2b5.jpg 245w," sizes="100vw" width="1595" height="1008"><h5>17:30 - 18:00 Single cell proteomics requires robust LC-MS: Unexpected findings bring new biological understanding</h5><ul><li>Jennifer Van Eyk, USA&nbsp;&nbsp;&nbsp;&nbsp;</li></ul>Underlying precision medicine is the concept that an individual’s Omic signature (including the proteome) will provide a physician with clinically actionable diagnosis and a subsequent mechanistic therapeutic route that is appropriate for a particular person. This concept is based on the idea of pathological heterogeneity and recognizes the impact of differences in the heath state of individuals. The deployment of single cell technologies has demonstrated heterogeneity within a single cell type which impacts the degree of cellular heterogeneity within an organ. Unlike bulk proteomic approaches, which average signals across heterogeneous populations, single-cell proteomics captures the molecular diversity of cell. Today single-cell proteomics can provide high-resolution characterization of protein quantities and variability within the structural composition and signaling dynamics within individual cells which requires robust, precise and sensitive liquid chromatography and mass spectrometry (LC-MS) workflows with sufficient throughput to quantitatively analyze 1000s of single cells.We have developed stable and precise single cell LC-MS workflow based on high-flow, dual trap with a single analytical column system that can achieve 96 samples per day. Furthermore, we have coupled this with a novel parallel sample preparation method on demand within the autosampler reducing sample lose and matching throughput with the LC-MS. Here, we have investigated the proteomic heterogeneity of cardiac muscle cells, cardiomyocytes, the specialized cells that contain the contractile proteins and which are responsible for the heart contraction and relaxation. By applying single-cell proteomics to cardiomyocytes isolated from human and mouse hearts, as well as human iPSC-derived cardiomyocytes, we uncovered previously unrecognized cellular subpopulations distinguished by differences in contractile and metabolic protein expression. As well unexpectedly, we unambiguously identified proteins traditionally considered absent in adult cardiomyocyte, such as slow skeletal troponin T, previously thought to be restricted to fetal or skeletal muscle or those proposed to be limited to non-cardiac cell types (e.g., neuronal proteins) or species (e.g., myosin heavy chain 7b). This suggests an unexpected fluidity in cardiac protein expression. Furthermore, single cell proteomics has provided critical insight into protein-level remodeling in heart failure, where the same single amino acid mutation in a contractile protein can give rise to diverse clinical phenotypes. At the single cell level, the mutant protein dosage in each cell drives a continuum of subproteomic pathological alterations. Only with precise protein quantification at the single cell level, is this understanding possible – all of which hinges on the LC-MS performance.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ISC_ISC_2026_Day_1_Jennifer_Van_Eyk_f8641196ff.jpg" alt="ISC: ISC 2026 - Day 1: Single cell proteomics requires robust LC-MS: Unexpected findings bring new biological understanding (Jennifer Van Eyk, USA)" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ISC_ISC_2026_Day_1_Jennifer_Van_Eyk_f8641196ff.jpg 235w," sizes="100vw" width="1600" height="1066"><h5>18:00 - 18:30 Rapid evaporative ionisation mass spectrometry: From MSI to LC-MS</h5><ul><li>Zoltan Takats, United Kingdom&nbsp;&nbsp;&nbsp;&nbsp;</li></ul>Rapid Evaporative Ionisation Mass Spectrometry (REIMS) was originally developed for mass spectrometry-guided surgery applications, enabling the direct, real-time analysis of surgical aerosols for in-situ histological identification of tissues in cancer surgery. Coupling the technique with various surgical and non-surgical lasers led to the recognition, that the technique has comparable sensitivity to other, widely used desorption ionisation methods including DESI and MALDI. Laser Ablation REIMS using 3 μm wavelength picosecond lasers was demonstrated to provide sub-cellular resolution metabolic and lipidomic images at 2-5 μm spatial resolution, with clear visualisation of cellular nuclei. The method was subsequently used for regenerative neuroscience and cancer biology applications. The unexpectedly high sensitivity of the method (fg amounts of lipids and metabolites / pixel) encouraged us to attempt using REIMS as an LC-MS ion source. The current commercially available REIMS instrumentation utilises the so-called matrix-assited REIMS technology, involving the co-introduction of a polar solvent (water, acetonitrile or aliphatic alcohols) together with the sample aerosol. The fused droplets containing solvent and soluble components of the aerosol are introduced into the vacuum where they impact a heated (≈900 ºC) surface resulting in their 'rapid evaporation' yielding the detected ion population. In this context, the ionisation matrix was replaced by LC effluent, leading to a fundamentally new way of ionisation. The new technique termed LC-REIMS was characterised using reversed phase LC applications including lipid and metabolite profiling. The new ionisation method was found to exhibit high similarity to sonic spray and related techniques, in spite of the high temperature involved. Analytical sensitivity for complex lipids and amino acids were found to be comparable to those in ESI or APCI, albeit the relative response factors followed markedly different trends. As the technology represents an LC-MS coupling without any requirement for pressurised gas or high voltage, it has significant application potential for field instrumentation including industrial process control or security screening.<img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ISC_ISC_2026_Day_1_Zoltan_Takats_3e0c11a22e.jpg" alt="ISC: ISC 2026 - Day 1: Rapid evaporative ionisation mass spectrometry: From MSI to LC-MS (Zoltan Takats, United Kingdom)" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ISC_ISC_2026_Day_1_Zoltan_Takats_3e0c11a22e.jpg 129w," sizes="100vw" width="1600" height="1933"><h5>18:30–19:30 Welcome Reception</h5><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ISC_ISC_2026_Day_1_Welcome_reception_36bfcb7276.jpg" alt="ISC: ISC 2026 - Day 1: Welcome reception" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ISC_ISC_2026_Day_1_Welcome_reception_36bfcb7276.jpg 235w," sizes="100vw" width="1600" height="1067"><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/ISC_ISC_2026_Day_1_Welcome_reception_2_4ae69091a6.jpg" alt="ISC: ISC 2026 - Day 1: Welcome reception" srcset="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/thumbnail_ISC_ISC_2026_Day_1_Welcome_reception_2_4ae69091a6.jpg 235w," sizes="100vw" width="1600" height="1067">

ISC 2026 - Day 1

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Since its establishment in 2011, CEITEC has quickly developed into a cutting-edge infrastructure for research which performs highly alongside the best institutes in Europe. Among the main priorities of CEITEC are the promotion of a motivating and dynamic international scientific environment, the provision of state-of-the-art research infrastructure, and the policy of open communication and equal opportunities.

CEITEC

The International Symposium on Chromatography (ISC) represents the oldest conference series focussing on separation science. ISC symposia have been organised since 1956 in each even year. ISC is internationally recognised as one of the premier meeting series for discussion of all modes of chromatography and separation science with a broad coverage of techniques and applications.

International Symposium on Chromatography - (ISC)

Watrex xTrovert XT Automatic DNA/RNA extractor

Watrex xTrovert XT is an automatic DNA/RNA extractor. It streamlines the extraction process, making it more efficient and reproducible.

Automatic extractor utilises a simple principle of two pipetting heads serving a 96-well plate.Thanks to easy replacement head options of pipetting with 300 μl tips or 1000 μl tips are available. Automatic optical sensor calibration enables the use of pipetting tips and 96-well plates from virtually any supplier. The device is equipped with two magnetic arms for protocols including paramagnetic SPR beads. It also allows for thermal incubation in the range of 25 to 85 °C. In addition to internal LED lighting, the station is equipped with an integrated UV-C sterilisation unit. Intuitive control from TFT touch panel user interface facilitates easy set-up. xTrovert™ XT is a fully programmable open system where user can create their own workflow scripts downloadable as text files from USB flas disk.<h3>APPLICATIONS</h3><ul><li>Sample prep for PCR testing</li><li>NGS library prep</li><li>Sanger DNA sequencing</li></ul><h3>CURRENT PROTOCOLS</h3><ul><li>DNA/RNA extraction</li><li>DNA purification</li><li>PCR clean-up/desalting</li></ul><img src="https://storage.googleapis.com/labrulez-bucket-strapi-h3hsga3/Watrex_Watrex_x_Trovert_XT_Automatic_DNA_RNA_extractor_Compatible_with_any_magnetic_bead_based_kit_23886eea52.jpg" alt="Watrex: Watrex xTrovert XT Automatic DNA/RNA extractor - Compatible with any magnetic bead based kit"><h3>TECHNICAL SPECIFICATION</h3><ul><li>Capacity: 16 or 32 samples/run</li><li>Volume range: 10 – 600 μl</li><li>Temperature: 25 – 85 °C</li><li>Sterilization: UV-C</li><li>Display: 3,5“ TFT touch display</li><li>Connectivity: USB 1.0/2.0</li><li>Power source: 24 V adaptor</li><li>Dimensions in cm: 65(w) x 65(h) x 34(d)</li><li>Weight: 25 kg</li></ul><h3>Ordering information:</h3><h5>PN/Component:</h5><ul><li>XTR000-001 xTrovert™ XT Universal robotic pipettor for DNA/RNA extraction &amp; handling</li><li>XTR000-003 Replaceable 8-channel 1000uL pipetting head for xTrovert™ XT</li><li>XTR000-004 Replaceable 8-channel 300uL pipetting head for xTrovert™ XT</li><li>XTR000-100 Deepwell plates (empty) for xTrovert™ XT</li><li>XTR000-220 DNA/RNA extraction kit, mgn. beads, 16-rxns per plate</li></ul>The entire system was designed and developed by Watrex Praha and is manufactured in the Czech Republic and promises a shift in the performance and efficiency of laboratory processes worldwide!You can also visit this product on the <a target="_blank" rel="noopener noreferrer" href="https://watrex.com/obchod/laboratory-automation/xtrovert-xt/?utm_source=labrulez&amp;utm_medium=propagace&amp;utm_campaign=labrulez_produkty">Watrex website</a>.

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