Results 31 to 40 of about 8,551 (180)

Structural basis of the novel S. pneumoniae virulence factor, GHIP, a glycosyl hydrolase 25 participating in host-cell invasion. [PDF]

open access: yesPLoS ONE, 2013
Pathogenic bacteria produce a wide variety of virulence factors that are considered to be potential antibiotic targets. In this study, we report the crystal structure of a novel S.
Siqiang Niu   +15 more
doaj   +1 more source

Characterisation of a putative M23-domain containing protein in Mycobacterium tuberculosis.

open access: yesPLoS ONE, 2021
Mycobacterium tuberculosis, the causative agent of tuberculosis remains a global health concern, further compounded by the high rates of HIV-TB co-infection and emergence of multi- and extensive drug resistant TB, all of which have hampered efforts to ...
Andrea Olga Papadopoulos   +4 more
doaj   +2 more sources

Toxin release mediated by the novel autolysin Cwp19 in Clostridium difficile

open access: yesMicrobial 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]

open access: yesMolecular 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   +2 more sources

Bacteriophage virion-associated peptidoglycan hydrolases: potential new enzybiotics [PDF]

open access: yesCritical Reviews in Microbiology, 2012
Virion-associated peptidoglycan hydrolases (VAPGH) are phage-encoded lytic enzymes that locally degrade the peptidoglycan (PG) of the bacterial cell wall during infection. In contrast to endolysins, PGHs that mediate lysis of the host bacteria at the end of the lytic cycle to release of phage progeny, the action of VAPGHs generates a small hole through
Rodríguez, Lorena   +4 more
openaire   +3 more sources

Characterisation of the peptidoglycan hydrolases of Listeria monocytogenes EGD [PDF]

open access: yesFEMS Microbiology Letters, 2006
The peptidoglycan hydrolase profile of Listeria monocytogenes EGD has been characterised under a variety of environmental and physiological conditions, using renaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The profiles show activities ranging from 29 to 186 kDa.
A M, McLaughlan, S J, Foster
openaire   +3 more sources

Zymogram Assay for the Detection of Peptidoglycan Hydrolases in Streptococcus mutans

open access: yesBio-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

open access: yesScientific 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   +4 more
doaj   +1 more source

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

open access: yesBMC 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   +3 more
doaj   +1 more source

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

open access: yesScientific 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   +4 more
doaj   +1 more source

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