Zuzanna Drulis-Kawa
University of Wroclaw, Poland
Department of Pathogen Biology and Immunology
Dr. Zuzanna Drulis-Kawa is a Professor at the Department of Pathogens Biology and Immunology at the University of Wrocław, Poland. Her research focuses on bacteriophage therapy, antimicrobial resistance, and phage-bacteria interactions, with a particular emphasis on developing phage-derived treatments for multidrug-resistant bacterial infections. She has published extensively on phage endolysins, depolymerases, and phage-host interactions, contributing to the advancement of phage-based therapeutics.
Affiliations: (1). Department of Pathogen Biology and Immunology, University of Wrocław, Wrocław (Poland) (2). Department of Biotechnology, Ghent University, Ghent (Belgium) (3). Malopolska Centre of Biotechnology, Jagiellonian University, Kraków (Poland) (4). Department of Bionanoscience, Delft University of Technology, Netherlands (5). Centre of Immunology and Microbial Infections, Sorbonne University, Paris, France (6). UTechS Photonic BioImaging Direction de la Technologie, Centre de Recherche et de Ressources Technologiques, Institut Pasteur, Paris, France (7). Bundeswehr Institute of Microbiology, Munich, Germany
The diversity of Klebsiella phage capsule depolymerases is probably greater than 160 cps locus types for capsule biosynthesis in Klebsiella spp. discovered so far. The knowledge of depolymerases structure and function, the genomic annotation and detection tools to predict their enzymatic specificity are still very limited. We present the dataset of experimentally verified Klebsiella phage depolymerases, comprising 106 enzymes targeting 59 distinct capsule types with 46 prepared and tested by our team. Their activity cover both classical K-types and genomically defined KL-types reported in clinical K. pneumoniae strains. Notably, 19 of the characterized enzymes originated from prophages—an underexplored but rich source of depolymerase diversity. Some capsule types (e.g., K23, K28, KL111) were independently recognized and degraded by enzymes produced by both lytic and temperate phages suggesting convergent evolution. While most proteins exhibited narrow serotype specificity recognizing only one type of CPS, 15 depolymerases showed activity on bacterial strains belonging to 2 or 3 cps locus types. Six major architectural classes were identified based on the arrangement of the central β-helical catalytic domain and the C-terminal substrate recognition modules. Structural modeling revealed extensive domain arrangements including insertions within the β-helix, tail fiber-like extensions, and chaperone-associated peptidase folds. Depolymerases targeting the same capsule type typically share structural traits, although notable exceptions suggest multiple evolutionary strategies for CPS degradation. Altogether, this dataset provides a foundation for comparative and functional studies of phage-encoded capsule-degrading enzymes.