Please use this identifier to cite or link to this item: https://hdl.handle.net/2445/222946
Title: Structural and biochemical characterization of a new phage-encoded muramidase, KTN6 Gp46
Author: Sanz-Gaitero, Marta
De Maesschalck, Vincent
Patel, Ankur
Longin, Hannelore
Van Noort, Vera
Rodríguez-Rubio, Lorena
van Ryne, Michael
Danis-Wlodarczyk, Katarzyna
Drulis-Kawa, Zuzanna
Mesnage, Stephane
van Raaij, Mark
Lavigne, Rob
Keywords: Lisina
Hidrolases
Bacteriòfags
Lisozim
Lysine
Hydrolases
Bacteriophages
Lysozyme
Issue Date: 21-Jun-2024
Abstract: Background: Endolysins are phage-encoded lytic enzymes that degrade bacterial peptidoglycan at the end of phage lytic cycles to release new phage particles. These enzymes are being explored as an alternative to small-molecule antibiotics. Methods: The crystal structure of KTN6 Gp46 was determined and compared with a ColabFold model. Cleavage specificity was examined using a peptidoglycan digest and reversed-phase high-performance liquid chromatography coupled to mass spectrometry (HPLC/MS). Results: The structure of KTN6 Gp46 could be determined at 1.4 Å resolution, and key differences in loops of the putative peptidoglycan binding domain were identified in comparison with its closest known homologue, the endolysin of phage SPN1S. Reversed-phase HPLC/MS analysis of the reaction products following peptidoglycan digestion confirmed the muramidase activity of Gp46, consistent with structural predictions. Conclusion: These insights into the structure and function of endolysins further expand the toolbox for endolysin engineering and explore their potential in enzyme-based antibacterial design strategies.
Note: https://doi.org/10.1089/phage.2023.0040
It is part of: 2024, vol. 5, num.2, p. 53-62
URI: https://hdl.handle.net/2445/222946
Related resource: https://doi.org/10.1089/phage.2023.0040
ISSN: 2641-6530
Appears in Collections:Articles publicats en revistes (Física Quàntica i Astrofísica)

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