Dr. Roger Castells (Spanish National Cancer Research Center (CNIO), Madrid, Spain)

Viruses are remarkable programmed nanomachines that undergo large-scale structural rearrangements to become functional and infectious. Understanding how these molecular assemblies form and transform provides fundamental insights into biological self-assembly while inspiring new approaches in protein engineering. Using high-resolution cryo-electron microscopy (cryo-EM), we have captured five intermediate states along the maturation pathway of Nudaurelia capensis omega virus (NωV), revealing with unprecedented detail the molecular mechanisms that drive the transition from an immature procapsid to an infectious virion. Beyond viral maturation, these studies uncover general principles of protein assembly that can be applied to the design of synthetic symmetric architectures. Building on these insights, we are engineering protein cages for applications in structural biology and biomedicine, including imaging scaffolds that enable cryo-EM structure determination of otherwise challenging small proteins. Together, these examples illustrate how studying natural nanomachines can inform the design of new molecular tools with broad biological applications.

"Exploring the regulation of virulence and novel virulence factors in priority pathogens"

Second messenger signalling pathways are known to play a fundamental role in governing bacterial physiology and mediating rapid adaptive responses to stimuli. Despite the extensive characterisation of second messenger signalling systems such as the cyclic di-GMP (c-di-GMP) signalling system in pathogens, relatively little is known about the role of these pathways in the priority pathogen Acinetobacter baumannii. To address this, we carried out a comprehensive exploration of c-di-GMP signalling across multiple modern A. baumannii clinical isolates. This talk will explore this second messenger’s regulon and its role in biofilm formation and other virulence-associated behaviours. The talk will also explore the characterisation and regulation novel virulence factors such as plastic degrading enzymes in other priority pathogens including Pseudomonas aeruginosa.

28/11/2025

A detailed understanding of the structural transitions that drive biochemical processes is critical for advancing both basic science and therapeutic discovery. While cryo-electron microscopy (cryo-EM) can, in theory, capture all conformational states of a macromolecule, short-lived high-energy intermediates often go undetected under standard steady-state sample preparation. To overcome this limitation, we are developing scalable time-resolved cryo-EM methods to selectively capture these transient states.

Our approach combines microfluidic-based rapid mixing and vitrification with machine learning-driven automation to streamline grid assessment and data acquisition. This enables high-throughput structural snapshots of dynamic molecular events at sub-second resolution. Current efforts focus on increasing experimental throughput and integrating structural data generation more tightly with ML-driven analysis pipelines, ultimately aiming for a lab-in-the-loop workflow.

We apply these methods to diverse systems relevant to drug discovery, with a particular emphasis on DNA repair and targeted protein degradation. By mapping transient structural states in these pathways, we seek to uncover mechanisms that can inform rational therapeutic design

Evolutionarily conserved cyclo-octasulfur prevents ferroptosis in mammals or why evolution preserved polysulfur in mammals"

 "Second-harmonic generation (SHG) for high-throughput conformational drug discovery and protein structure measurements"

Dr. Tom SERCU on:  "Evolutionary Scale Modeling"

Former: Ex-Meta - ESM Team

Current: EvolutionaryScale 

https://www.evolutionaryscale.ai/

When: Friday, May 17, 2024 at 11:00AM

Where: Promotion Room D.2.01

Prof. John McKinney, PhD

Director, Laboratory of Microbiology and Microtechnology

Swiss Federal Institute of Technology in Lausanne (EPFL)

Biography: https://people.epfl.ch/john.mckinney

Joe Watson will be visiting on the 19^th of April. He is giving a talk at 11am. As usual, we will have 1-1 discussions with PIs in the afternoon.  Please mark your calendar and let me know if you'd like to talk to the visitor, and if you have any specific time constraint on these dates.

The molecular structure of protein-ligand complexes provides much insight into the biochemical processes in living cells. However, to understand protein function, we also need to resolve how proteins interact with their small molecule ligands over time. In this presentation, Dr. Strandfuss will outline the opportunities and challenges of using the Swiss X-ray Free Electron Laser (SwissFEL) to follow protein dynamics at near-atomic spatial and temporal resolution in the femtosecond range.

Proton Channel Activity in de novo Designed Channel Proteins

Protein-mediated selective proton transport is crucial for establishing and utilizing proton gradients in cells. Surprisingly, these proton-conducting pathways, observed in static protein structures, often contain dry apolar stretches that interrupt the flow of protons along water molecule 'wires' and polar side chains. In light of this, we propose that protons navigate these dry regions by creating transient water wires, which are closely associated with the presence of excess protons. To investigate this hypothesis, Huong conducted molecular dynamics simulations to design transmembrane channels that feature stable water pockets interspersed with apolar segments capable of forming flickering water wires. Her findings provide insights into the mechanisms of biological proton conduction and offer principles for engineering proton-conductive materials.

From start to well beyond finish: AI as a vehicle to new discovery

Lennart Martens is a professor of Systems Biology at Ghent University, and Group Leader in, and Associate Director of, the VIB-UGent Center for Medical Biotechnology. His research interests focus on the application of Machine Learning to high-throughput data, and his current projects include the development of novel, advanced data processing and interpretation algorithms that are driven by artificial intelligence. Dr. Martens is a Fellow of the Royal Society of Chemistry, serves on the Board of the Belgian Proteomics Association, on the proteomics section of the Royal Chemistry Society of Flanders, and has been elected to the Human Proteome Organization (HUPO) Council, and to the HUPO Executive Committee. 

Nanobodies open a gate into the liver: transport and hepatitis-B virus receptor mechanisms of human NTCP

Nicolas Reyes is professor at the National Center of Scientific Research (CNRS) in Bordeaux, France, and Group Leader at the European Institute of Chemistry and Biology (IECB) in Pessac, France. His laboratory studies the molecular mechanisms of function and pharmacology of human membrane proteins involved in diseases, with a focus on solute carriers (SLCs). SLCs constitute the second largest superfamily of membrane proteins in mammals, and transport a wide range of substrates across cellular membranes, including nutrients, transmitters, metabolites, lipids, and more. Because their substrates are essential to cell and organ functions, the dysregulations of SLCs are linked to a wide spectrum of human diseases, from cancer to neurological disorders.

PHASAGE-VIB International Conference

Biomolecular condensates in biology and disease

Biosensors Brussels Symposium

Tuning the fluorescence of a β-barrel

We created a forum for international and national speakers to discuss the biochemistry, photophysical properties, fluorescence lifetime, structural properties and bright colours of biosensors.