Marion Schuller becomes new research group leader at the MPI of Biochemistry

What happens when bacteriophages infect bacteria? Marion Schuller will be investigating this question from July 1 with her new Lise Meitner Research Group at the Max Planck Institute of Biochemistry.
 

On July 1, Marion Schuller will start as the head of the new Lise Meitner Research Group, ‘Host defence mechanisms’ at the Max Planck Institute of Biochemistry (MPIB). Marion is a biochemist who is interested in the infection mechanisms of bacteriophages, which are viruses that attack and kill bacteria. She will analyze ADP-ribosylation-dependent signaling pathways in bacteria to understand how bacteria deal with infection by bacteriophages. With her research, she hopes to contribute to the long-term fight against multi-resistant bacterial infections.
 

Research group ‘Host defence mechanisms’

The resistance of bacteria to antibiotics is a major threat to healthcare, and therapeutic solutions are urgently needed. Bacteriophages, or phages for short, are viruses that specifically infect bacteria in order to replicate, thereby killing their respective bacterial host. Phage-based therapies are therefore seen as a promising approach to combating multi-resistant bacterial infections. Marion Schuller explains: “The interaction between phages and bacteria is fascinating. It involves highly complex and specific biochemical processes that are still largely unexplored. In the future, I will analyze together with my team so-called ADP-ribosylation-dependent signaling pathways which are involved in the warfare between phages and bacteria.” ADP-ribose is a molecule that can be bound individually or in chains by an enzyme to proteins, DNA, or RNA. This process is called ADP ribosylation. ADP-ribosylation-dependent signaling pathways are particularily known for their role in the DNA damage response and repair in eukaryotic cells. Marion Schuller continues: "I have been working on ADP ribosylation since my time in Oxford; when phages infect bacteria, ADP-ribosylation processes are part of the repertoire of the antiphage defence mechanisms employed by bacteria. We will be investigating the details here.”

About Marion Schuller

Marion Schuller studied Pharmaceutical Sciences at Ludwig Maximilian University in Munich. In 2013, she went to Oxford University in the UK to pursue her PhD, conducting research under the supervision of Stefan Knapp and Benedikt Kessler at the Nuffield Department of Medicine including the Target Discovery Institute and the Structural Genomics Consortium. During her postdoctoral training from 2018 to 2025, she investigated mechanisms of bacterial toxins in Mycobacterium tuberculosis in the Ivan Ahel Laboratory in Oxford in collaboration with Professor Graham Steward from the University of Surrey, UK. She joined the Max Planck Institute of Biochemistry in April 2025. Starting in July of this year, she will head the Lise Meitner Research Group on ‘Host Defence Mechanisms’.

Glossary:
Bacteriophages: Phages for short, are viruses that only infect bacteria.

ADP-ribose: is a molecule consisting of the sugar ribose, two phosphate groups, and the nucleoside adenosine. It plays a central role in the cell, where it is bound to macromolecules such as proteins as a “tag” (modifier) to specifically alter their activity or function. This process is particularly important in the regulation of metabolic processes, DNA repair, and signal transduction within the cell.

ADP-ribosylation: is a reversible, enzymatic modification of macromolecules in which one or more ADP-ribose units are transferred from NAD⁺ either to specific amino acid residues in proteins or to DNA and RNA to regulate their respective functions.

Eukaryotic cells: is a type of cell with a nucleus and internal compartments, found in animals, plants, and fungi.

Multiresistant bacteria: are pathogens that have become resistant to several different antibiotics and are therefore more difficult to treat.

NAD⁺: Abbreviation for nicotinamide adenine dinucleotide; is the oxidized, electron-accepting form of the coenzyme NAD.