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. 2023 Jun 7;14:3338. doi: 10.1038/s41467-023-38950-3

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 3 — a ANTS visualization of peptidoglycan (from M. luteus) digests of LPH showed that it generated specific products migrating similarly to the synthetic muropeptide MDP, the red asterisk indicates the space for MDP. b Heatmap illustrating the peptidoglycan (from M. luteus) digests of different enzymes or enzyme combinations analyzed by untargeted HPLC-MS/MS. Rows indicated all detected peptidoglycan fragments; columns show different enzymes or enzyme combinations; The gray shade represents relative peptidoglycan fragments abundance as quantified by the log2-transformed area under the curve. c Targeted LC-MS/MS analysis of fecal MDP levels in mice gavaged with different doses (0, 1, 2.5, 5 mg/kg body weight) of LPH-containing beads for three days, n = 7 mice (female) per group. Data are representative of 3 independent experiments and presented as mean ± SD. Statistical analysis was performed using one-way ANOVA with Bonferroni post hoc test. d Representative peptidoglycan structure from gram-positive bacteria (lysine on the third amino acid in the peptide stems), and the minimal enzymes required to generate MDP. e The predicted three-dimensional structure of the 3D-domain of LPH, with the electrostatic potentials and the active sites for the N-Acetyl-β-D-muramidase activity shown on the left, and the active sites for the DL-endopeptidase activity shown on the right. f–g Untargeted HPLC-MS/MS analysis of peptidoglycan (from M. luteus) digests of indicated enzymes or enzyme combinations. The line indicates the MDP peak. Data are representative of 3 independent experiments. h ANTS visualization of peptidoglycan (from M. luteus) digests of different enzymes or enzyme combinations, data are representative of 3 independent experiments. BSA: bovine serum albumin; PG; peptidoglycan, LPH-AS1: the D316A mutation of LPH; LPH-AS2: the D329A mutation of LPH; LPH-AS3: P295A, G297A, and T298A mutations of LPH; Mutanlolysin (M) was used as a positive control for N-Acetyl-β-D-muramidase; SagA was used as a positive control for DL-endopeptidase. Source data are provided as a Source data file.