Klebsiella phage KP34gp57 capsular depolymerase structure and function: from a serendipitous finding to the design of active mini-enzymes against K. pneumoniae

• DOI: 10.1128/mbio.01329-23
• Publication Date: 2023-09-14T14:56:01Z
• Authors: Barbara Maciejewska; Flavia Squeglia; Agnieszka Latka; Mario Privitera; Sebastian Olejniczak; Paulina Switala; Alessia Ruggiero; Daniela Marasco; Eliza Kramarska; Zuzanna Drulis-Kawa; Rita Berisio
• Keywords: Klebsiella

In this work, we determined the structure of Klebsiella phage KP34p57 capsular depolymerase and dissected role individual domains in trimerization functional activity. The crystal serendipitously revealed that enzyme can exist a monomeric state once deprived its C-terminal domain. Based on site-directed mutagenesis, localized key catalytic residues an intra-subunit deep groove. Consistently, show C-terminally trimmed variants are monomeric, stable, fully active. elaboration active depolymerases is innovative field, as no previous example exists. Indeed, mini be combined chimeric enzymes to extend their activity ranges, allowing use against multiple serotypes.