8p8e

Publication Abstract from PubMed

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 A 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.

Structural and Biochemical Characterization of a New Phage-Encoded Muramidase, KTN6 Gp46.,Sanz-Gaitero M, De Maesschalck V, Patel A, Longin H, Van Noort V, Rodriguez-Rubio L, van Ryne M, Danis-Wlodarczyk K, Drulis-Kawa Z, Mesnage S, van Raaij M, Lavigne R Phage (New Rochelle). 2024 Jun 21;5(2):53-62. doi: 10.1089/phage.2023.0040. , eCollection 2024 Jun. PMID:39119210^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.