A new peptidoglycan hydrolase mined from Acinetobacter baumannii proteome by lysin-derived antimicrobial peptide-primed screening strategy undergoes a unique switch between dimer and monomer after heat treatment and protects mice from A. baumannii infection.

Robust NMR approach allowed simultaneous detection of substrate cleavage site and real-time kinetics of hydrolysis for Staphylococcus aureus peptidoglycan hydrolases lysostaphin and LytM, and revealed D-alanyl-glycine activity for LytM.

The peptidoglycan hydrolase activity of Enterococcus faecium secreted antigen A is crucial for cell wall remodeling during bacterial cell separation and generates muropeptides that stimulate host immunity to enhance immune checkpoint inhibitor anti-cancer therapy.

Selective removal of Wall Teichoic Acids from the envelope of Streptococcus pneumoniae prevents bacteriolysis and directs zonal cell wall synthesis.

Enterococci faecium encodes unique peptidoglycan composition and remodeling activity that activates host immunity.

Arabidopsis lysozyme LYS1 generates soluble peptidoglycan fragments to mediate pattern-triggered immunity.

An enzyme that remodels the cell wall of Enterococcus faecium helps these gut bacteria to divide and generate peptide fragments that enhance the immune response against cancer.

MreB filaments bind, orient, and move along the direction of greatest membrane curvature, thus orienting the insertion of new glycan strands around the cell circumference in a manner that may help establish and maintain rod shape.

Molecular genetic analyses define the first homeostatic control pathway that maintains cell wall remodeling activity during bacterial growth.

To avoid recognition by the immune system, bacteria use autolysins to trim fragments of peptidoglycans that are exposed on the bacterial cell wall.