Fig. 3: Effect of LD-crosslinks on peptidoglycan degrading enzymes.
From: Control of bacterial cell wall autolysins by peptidoglycan crosslinking mode
a Schematics showing the activity of exogenous lytic transglycosylases on the cell wall. Panel created with BioRender.com, released under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International license (https://creativecommons.org/licenses/by-nc-nd/4.0/deed.en). b Activity of different PG-degrading enzymes on substrate with indicated LD-crosslinking levels. Activity is calculated relative to sacculi substrate with 0% LD-crosslinks. Enzymes: Tse4 effector of A. baumannii, bacteriophage lambda endolysin (LaL), chicken egg white lysozyme (LYZ) and mutanolysin from Streptomyces globisporus (Muramidase). In vitro assays were performed in triplicate. Data are presented as mean values +/- standard deviation. c Growth curves of E. coli JM109 with empty pBAD33 (pBAD) plasmid or pBAD::ldtE, grown with and without inducer (arabinose 0.2% (w/v), +Ara), infected at time zero with the same amount (∼104 PFUs) of lambda phage particles (λ). d Representative plates showing increased resistance of the LDT-overexpressing strain to lambda phage plaque formation. LB agar plates are supplemented with 20 µg/ml chloramphenicol, 10 mM MgSO4, and 0.2% (w/v) arabinose. e Quantification of PFU/ml produced by different phages encoding endolysins with lytic transglycosylase (LT), lysozyme (LYZ) or endopeptidase (EPase) activities on E. coli JM109 carrying empty pBAD or pBAD::ldtE at 24 h post-infection. Infection assays were performed in triplicate. Data are presented as mean values +/- standard deviation. Statistical significance was determined using an unpaired t-test, corrected for multiple comparisons by the Holm-Sidak method, with an alpha level of 0.05. Two-tailed p-values are reported. **p < 0.01; ***p < 0.001; ns: not significant. Source data are provided as a Source Data file.
