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]
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
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Characterisation of a putative M23-domain containing protein in Mycobacterium tuberculosis.
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
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
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Bacterial growth does require peptidoglycan hydrolases [PDF]
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]
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
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Characterisation of the peptidoglycan hydrolases of Listeria monocytogenes EGD [PDF]
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
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Zymogram Assay for the Detection of Peptidoglycan Hydrolases in Streptococcus mutans
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
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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
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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
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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

