Results 31 to 40 of about 8,626 (154)

Peptidoglycan Hydrolase Fusions Maintain Their Parental Specificities [PDF]

Applied and Environmental Microbiology, 2006
ABSTRACT The increased incidence of bacterial antibiotic resistance has led to a renewed search for novel antimicrobials. Avoiding the use of broad-range antimicrobials through the use of specific peptidoglycan hydrolases (endolysins) might reduce the incidence of antibiotic-resistant pathogens worldwide.
David M, Donovan, Shengli, Dong, Wes, Garrett, Geneviève M, Rousseau, Sylvain, Moineau, David G, Pritchard   +5 more
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Toxin release mediated by the novel autolysin Cwp19 in Clostridium difficile

Microbial Cell, 2018
Clostridium difficile, also known as Clostriodioides difficile, is a Gram positive, spore-forming bacterium and a leading cause of antibiotic-associated diarrhea in nosocomial environments. The key virulence factors of this pathogen are two toxins, toxin
Imane El Meouche, Johann Peltier
doaj   +1 more source

Bacterial growth does require peptidoglycan hydrolases [PDF]

Molecular Microbiology, 2012
SummaryMost bacteria surround their cytoplasmic membrane with a net‐like, elastic heteropolymer, the peptidoglycan sacculus, to protect themselves from bursting due to the turgor and to maintain cell shape. It has been assumed that growing bacteria require peptidoglycan hydrolases to open meshes in the peptidoglycan net allowing the insertion of the ...
openaire   +4 more sources

Zymogram Assay for the Detection of Peptidoglycan Hydrolases in Streptococcus mutans

Bio-Protocol, 2013
Peptidoglycan hydrolases or autolysins are enzymes capable of cleaving covalent bonds in bacterial peptidoglycan cell wall layer. They can participate in the cell division process, in the release of turnover products from peptidoglycan during cell growth,
Delphine Dufour, Céline Lévesque
doaj   +1 more source

Cell morphology maintenance in Bacillus subtilis through balanced peptidoglycan synthesis and hydrolysis

Scientific Reports, 2020
The peptidoglycan layer is responsible for maintaining bacterial cell shape and permitting cell division. Cell wall growth is facilitated by peptidoglycan synthases and hydrolases and is potentially modulated by components of the central carbon ...
Jad Sassine, Joana Sousa, Michael Lalk, Richard A. Daniel, Waldemar Vollmer   +4 more
doaj   +1 more source

Diversity of the lysozyme fold: structure of the catalytic domain from an unusual endolysin encoded by phage Enc34

Scientific Reports, 2022
Endolysins are bacteriophage-encoded peptidoglycan-degrading enzymes with potential applications for treatment of multidrug-resistant bacterial infections. Hafnia phage Enc34 encodes an unusual endolysin with an N-terminal enzymatically active domain and
Elina Cernooka, Janis Rumnieks, Nikita Zrelovs, Kaspars Tars, Andris Kazaks   +4 more
doaj   +1 more source

The PECACE domain: a new family of enzymes with potential peptidoglycan cleavage activity in Gram-positive bacteria

BMC Genomics, 2005
Background The metabolism of bacterial peptidoglycan is a dynamic process, synthases and cleavage enzymes are functionally coordinated. Lytic Transglycosylase enzymes (LT) are part of multienzyme complexes which regulate bacterial division and elongation.
Di Guilmi Anne, Vernet Thierry, Dideberg Otto, Pagliero Estelle   +3 more
doaj   +1 more source

Regulation of the cell division hydrolase RipC by the FtsEX system in Mycobacterium tuberculosis

Nature Communications, 2023
The FtsEX complex regulates, directly or via a protein mediator depending on bacterial genera, peptidoglycan degradation for cell division. In mycobacteria and Gram-positive bacteria, the FtsEX system directly activates peptidoglycan-hydrolases by a ...
Jianwei Li, Xin Xu, Jian Shi, Juan A. Hermoso, Lok-To Sham, Min Luo   +5 more
doaj   +1 more source

O-Glycosylation as a Novel Control Mechanism of Peptidoglycan Hydrolase Activity [PDF]

Journal of Biological Chemistry, 2013
Acm2, the major autolysin of Lactobacillus plantarum, is a tripartite protein. Its catalytic domain is surrounded by an O-glycosylated N-terminal region rich in Ala, Ser, and Thr (AST domain), which is of low complexity and unknown function, and a C-terminal region composed of five SH3b peptidoglycan (PG) binding domains.
Rolain, Thomas, Bernard, Elvis, Beaussart, Audrey, Degand, Herve, Courtin, Pascal, Egge-Jacobsen, Wolfgang, Bron, Peter A., Morsomme, Pierre, Kleerebezem, Michiel, Chapot-Chartier, Marie-Pierre, Dufrene, Yves F., Hols, Pascal   +11 more
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Detection and Localization of a Peptidoglycan Hydrolase in Lactobacillus delbrueckiisubsp. bulgaricus [PDF]

Journal of Dairy Science, 2003
Peptidoglycan hydrolase activities in Lactobacillus delbrueckii subsp. bulgaricus were detected by analysis of bacterial extracts on denaturing polyacrylamide gel electrophoresis containing lyophilized Micrococcus lysodeikticus cells as substrate. A hydrolase with an estimated molecular mass of 80 kDa was found to cross-react on Western blot with ...
O J, Kang, S, Laberge, R E, Simard
openaire   +2 more sources