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For any organism, survival is enhanced by the ability to sense and respond to threats in advance. For bacteria, danger sensing among kin cells has been observed, but the presence or impacts of general danger signals are poorly understood. Here we show that different bacterial species use exogenous peptidoglycan fragments, which are released by nearby kin or non-kin cell lysis, as a general danger signal. Using microscopy and gene expression profiling of Vibrio cholerae, we find that even brief signal exposure results in a regulatory response that causes three-dimensional biofilm formation, which protects cells from a broad range of stresses, including bacteriophage predation. A diverse set of species (Pseudomonas aeruginosa, Acinetobacter baumannii, Staphylococcus aureus, Enterococcus faecalis) also respond to exogenous peptidoglycan by forming biofilms. As peptidoglycan from different Gram-negative and Gram-positive species triggered three-dimensional biofilm formation, we propose that this danger signal and danger response are conserved among bacteria.
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http://dx.doi.org/10.1038/s41564-024-01886-5 | DOI Listing |
Microbiol Spectr
September 2025
Department of Biological Sciences, University of Illinois at Chicago, Chicago, Illinois, USA.
D-glu is a key component of peptidoglycan (PG) and is essential for growth in most bacteria. To assess constraints on PG evolution and bacterial requirements for D-glu, we sought to artificially evolve PG biosynthesis, leading to either replacement of D-glu in the PG peptide or alternative pathways to D-glu incorporation. We previously found that suppression of D-glu auxotrophy in a mutant of grown on lysogeny broth salts (LBS) medium was rare but could be accomplished by mutation of , with restoration of wild-type PG structure.
View Article and Find Full Text PDFmBio
August 2025
Centre for Immunology and Infection Control, School of Biomedical Sciences, Queensland University of Technology, Brisbane, Queensland, Australia.
Bile salts (BS) are antimicrobials that disrupt bacterial cell membranes and induce oxidative stress. The gut bacterium is naturally resistant to BS, including the model strain K12 MG1655 that produces a lipopolysaccharide (LPS) without O-antigen (OAg) on the cell surface. Paradoxically, we have previously shown that restoring a wild-type like LPS with attached OAg (MG1655-S) sensitizes K12 to exogenous BS.
View Article and Find Full Text PDFJ Bacteriol
July 2025
Department of Microbiology and Immunology, Center for Infectious Disease Research, Medical College of Wisconsin, Milwaukee, Wisconsin, USA.
Unlabelled: Infections caused by enterococci are increasingly prevalent and difficult to treat due to multidrug resistance. exhibits intrinsic resistance toward cephalosporins, which inhibit the final step of peptidoglycan (PG) synthesis. Intrinsic resistance requires multiple factors in the PG synthesis pathway and at least two cell-wall-stress signal transduction systems; however, the complete molecular mechanism of enterococcal cephalosporin resistance remains to be elucidated.
View Article and Find Full Text PDFAntimicrob Agents Chemother
July 2025
Department of Bacteriology, Hiroshima University Graduate School of Biomedical and Health Sciences, Hiroshima, Japan.
D-alanine is an important amino acid for peptidoglycan biosynthesis in . In addition, D-alanine is used for the modification of teichoic acids to weaken the net surface negative charge, leading to decreased susceptibility to cationic antimicrobial agents. D-alanine synthesis is dependent on only two enzymes.
View Article and Find Full Text PDFbioRxiv
May 2025
Department of Biology, Texas A&M University, College Station, Texas, USA.
Gram-negative bacteria divide by separating two cell wall layers: peptidoglycan (PG) and the outer membrane (OM). In certain model organisms, the OM is tethered to PG, ensuring it closely follows PG throughout invagination, constriction, and separation. In contrast, exhibits autonomous OM partitioning, occurring only after complete PG fission.
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