Research

Bacteriophages are the most abundant biological entities on Earth and display an extraordinary diversity in form, function, and host specificity. This immense diversity is the result of billions of years of evolution, making phages powerful model systems to study how molecular interactions emerge, diversify, and specialize.

Beyond their fundamental interest, phages have gained renewed attention as targeted antibacterial agents. Their inherent specificity and adaptability make them promising tools for phage therapy, offering new opportunities to combat infections in the context of rising antimicrobial resistance.

Phage lysins are specialized enzymes that enable bacteriophages to breach the bacterial cell wall. During infection, they act in a tightly controlled manner, facilitating genome entry at early stages, while driving rapid cell lysis at the end of the replication cycle to release new phage particles.

We harness and engineer lysins as a novel class of antibacterial agents for applications in both human and animal health. Engineered lysins act rapidly and are highly bactericidal, efficiently eliminating target bacteria with a low probability of resistance development. A key advantage of lysins lies in their modular architecture, which makes their activity highly tunable. Through protein engineering, we can tailor their specificity, potency, and functional properties, enabling the development of customized antibacterial solutions adapted to specific pathogens and applications.

Phage receptor-binding proteins (RBPs) mediate the very first step of infection by recognizing and binding to specific structures on the bacterial surface. They determine host range and are key drivers of the remarkable specificity observed in phage-host interactions.

Our research combines experimental and computational approaches to understand how RBP diversity, specificity, and modularity arise and evolve. We study these processes across scales, from the structural and functional properties of individual proteins to their organization and diversification within phage genomes.

RBPs are highly modular systems, in which distinct domains can be recombined and adapted to recognize new targets. This inherent flexibility, shaped by evolution, provides a powerful framework for both understanding molecular recognition and engineering tailored binding specificities for applications in bacterial detection and targeted antimicrobial strategies.