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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867746.pdf | 1.63 MB | Adobe PDF | View/Open |
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