Scientists reveal how gut pathogens assemble tiny protein ‘factories’ to survive


Researchers at the University of Liverpool have uncovered the step-by-step process by which pathogenic bacteria build specialised protein compartments, called Eut microcompartments, that allow them to digest ethanolamine - a nutrient abundant in the gut.


These microscopic structures are essential for bacterial growth and virulence. Mapping how they assemble provides crucial insight into how pathogens thrive in the gut and highlights potential targets for new antimicrobial strategies.


The study [1], published in Science Advances, combines advanced techniques including super-resolution fluorescence microscopy, structural biology, genetic engineering, biochemical assays, and computational modelling to track the roles of individual proteins in nella’s Eut microcompartments.


By analysing bacteria with mutations in specific proteins, the team pinpointed the key steps in compartment construction. They found that the protein shell forms first, followed by the packing of enzymes required to break down ethanolamine. A protein called EutQ acts as a molecular linchpin, ensuring enzymes are correctly incorporated; without it, compartment assembly fails and bacterial growth is severely impaired.


The researchers also discovered that the enzymes inside


Pathogenic bacteria construct tiny protein-based compartments, known as Eut microcompartments, which enable them to digest ethanolamine. Credit: University of Liverpool


the compartments behave like a liquid droplet, dynamically moving and interacting to enhance metabolic efficiency. Ethanolamine, released during cell membrane breakdown, serves as a vital carbon and nitrogen source for pathogens such as Salmonella.


Dr Mengru Yang, first author from the University of Liverpool’s Institute of Systems, Molecular and Integrative Biology, said: “It was known that bacteria use these


compartments to digest ethanolamine safely, but we can now see the precise molecular choreography behind their construction. Observing these dynamic protein condensates in action offers an unprecedented view of bacterial organelle assembly.”


Professor Lu-Ning Liu, corresponding author, added: “Our work uncovers fundamental mechanisms of microcompartment assembly, revealing new opportunities to disrupt pathogen metabolism. These insights could inform antimicrobial development and even synthetic biology applications.”


The team plans to investigate how these assembly processes operate in other health-relevant bacteria, explore atomic-level protein interactions, and test ways to manipulate these systems for medical use.


This research was funded by the Biotechnology and Biological Sciences Research Council (BBSRC) and involved collaborators from Huazhong Agricultural University and Ocean University of China.


More information online: ilmt.co/PL/OmOX


1. Molecular basis of the biogenesis of a protein organelle for ethanolamine utilization (doi.org/10.1126/sciadv.adx9774) published in Science Advances


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p53 protein rewrites cancer rules: Signalling guides immune response


Researchers at The Wistar Institute have overturned decades of accepted wisdom about p53 – the so-called ‘guardian of the genome’ – revealing that this crucial tumour suppressor is far more sophisticated than previously believed.


For 30 years, scientists assumed that p53 activated the same set of genes regardless of the situation, leaving the cell itself to decide whether to halt division or self- destruct. But a study published in Molecular Cell [1] shows that p53 can, in fact, interpret cellular signals and direct distinct genetic programmes, including those that enlist the immune system to destroy cancer cells.


The team discovered that p53’s behaviour is shaped by an enzyme called PADI4, which modifies p53 through a chemical process known as citrullination. This subtle alteration changes where p53 binds on DNA - prompting it to abandon many of its usual target genes and relocate to regions associated with immune response activation.


“p53 isn’t as simple as we once thought,” said Maureen Murphy, PhD, Deputy Director of Wistar’s Ellen and Ronald Caplan Cancer Center and senior author of the study. “It can ‘read’ intracellular signals and decide where to act, and that decision appears to mobilise the immune system against tumours.”


Murphy’s group has long studied genetic variants of p53 found in families of African descent, some of which are only partially functional. Comparing these hypomorphic variants to normal p53 led the researchers to identify PADI4 as a key missing link. When PADI4 is active, it rewires p53’s binding profile, enhancing immune-related gene expression.


Using advanced techniques including ChIP-seq and CUT&Tag, the team mapped these changes in live cells and confirmed the effect in mouse models. They found that when p53 is citrullinated, around 30% of its conventional binding sites are replaced by new ones that drive interferon signalling – the cell’s core antiviral and anti-tumour response.


The findings carry important clinical implications. Patients with certain p53 variants that fail to activate PADI4 may respond poorly to immunotherapies, suggesting that PADI4 status could serve as a biomarker for personalised treatment decisions.


“By understanding how p53 collaborates with PADI4, we may be able to predict who will benefit most from immune- based cancer therapies,” said Murphy.


Beyond its therapeutic potential, the work highlights the


(L-R) Dr Maureen Murphy with lab members Maya Foster and Andrea Valdespino.


value of studying genetic diversity in underrepresented populations. “By examining p53 variants in families of African ancestry – people often left out of research – we uncovered a fundamental new mechanism of tumour suppression,” Murphy added.


More information online: ilmt.co/PL/WDmX


1. Targeted Citrullination Enables p53 Binding to Non- canonical Sites published in Molecular Cell, 2025. Online publication.


65983pr@reply-direct.com PFAS in pregnancy linked to children’s brain development


Exposure to forever chemicals during pregnancy may shape how children’s brains develop, according to new research led by the University of Turku in Finland, in collaboration with Turku University Hospital and Örebro University in Sweden.


The study [1], published in The Lancet Planetary Health, found that higher levels of per- and polyfluoroalkyl substances (PFAS) in mothers’ blood were associated with differences in brain structure and function in their five-year- old children.


PFAS are a group of synthetic chemicals used in everything from non-stick pans to firefighting foams. They are known for their persistence in the environment and in human bodies, earning them the nickname ‘Forever chemicals’.


Using data from the long-running FinnBrain Birth Cohort, researchers analysed blood samples from expectant mothers and later performed MRI brain scans on their children. The results revealed that different PFAS compounds were linked to changes in specific brain regions, including the corpus callosum, occipital lobe, and hypothalamus.


“PFAS are everywhere – in our food, water, and even the air we breathe – and they pass from mother to child during pregnancy,” explained Senior Researcher and lead author, Aaron Barron from the University of Turku. “Our findings suggest these chemicals may influence early brain development, though we still need to understand how.”


While the long-term impact of these associations remains


unclear, the findings add to growing concern about PFAS exposure and its potential role in human health.


The research was funded by the EU Horizon Europe project INITIALISE (‘Inflammation in human early life: targeting impacts on life-course health’).


More information online: ilmt.co/PL/OmJ4


1. Prenatal exposure to perfluoroalkyl substances predicts multimodal brain structural and functional outcomes in children aged 5 years: a birth cohort study published in The Lancet Planetary Health.


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