Results 51 to 60 of about 12,407 (196)

Mycobacterium tuberculosis FtsX extracellular domain activates the peptidoglycan hydrolase, RipC [PDF]

open access: yes, 2014
Bacterial growth and cell division are coordinated with hydrolysis of the peptidoglycan (PG) layer of the cell wall, but the mechanisms of regulation of extracellular PG hydrolases are not well understood.
Marakalala, Mohlopheni J   +7 more
core   +1 more source

Peptidoglycan hydrolases-potential weapons against Staphylococcus aureus [PDF]

open access: yesApplied Microbiology and Biotechnology, 2012
Bacteria of the genus Staphylococcus are common pathogens responsible for a broad spectrum of human and animal infections and belong to the most important etiological factors causing food poisoning. Because of rapid increase in the prevalence of isolation of staphylococci resistant to many antibiotics, there is an urgent need for the development of new
Szweda, Piotr   +5 more
openaire   +2 more sources

Chitinase A, a tightly regulated virulence factor of Salmonella enterica serovar Typhimurium, is actively secreted by a Type 10 Secretion System.

open access: yesPLoS Pathogens, 2023
As a facultative intracellular pathogen, Salmonella enterica serovar Typhimurium is one of the leading causes of food-borne diseases in humans. With the ingestion of fecal contaminated food or water, S. Typhimurium reaches the intestine.
Lena Krone   +4 more
doaj   +1 more source

Potential Role of the Host-Derived Cell-Wall Binding Domain of Endolysin CD16/50L as a Molecular Anchor in Preservation of Uninfected Clostridioides difficile for New Rounds of Phage Infection

open access: yesMicrobiology Spectrum, 2022
Endolysin is a phage-encoded cell-wall hydrolase which degrades the peptidoglycan layer of the bacterial cell wall. The enzyme is often expressed at the late stage of the phage lytic cycle and is required for progeny escape.
Wichuda Phothichaisri   +6 more
doaj   +1 more source

O-glycosylation as a novel control mechanism of peptidoglycan hydrolase activity. [PDF]

open access: yesJ Biol Chem, 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 T   +11 more
europepmc   +7 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

Coordinated peptidoglycan synthases and hydrolases stabilize the bacterial cell wall

open access: yesNature Communications, 2023
Abstract Peptidoglycan (PG) defines cell shape and protects bacteria against osmotic stress. The growth and integrity of PG require coordinated actions between synthases that insert new PG strands and hydrolases that generate openings to allow the insertion.
Huan Zhang   +3 more
openaire   +3 more sources

Interaction of Mycobacterium tuberculosis Virulence Factor RipA with Chaperone MoxR1 Is Required for Transport through the TAT Secretion System

open access: yesmBio, 2016
Mycobacterium tuberculosis is a leading cause of death worldwide. The M. tuberculosis TAT (twin-arginine translocation) protein secretion system is present at the cytoplasmic membrane of mycobacteria and is known to transport folded proteins.
Manish Bhuwan   +7 more
doaj   +1 more source

A mycobacterial enzyme essential for cell division synergizes with resuscitation-promoting factor. [PDF]

open access: yesPLoS Pathogens, 2008
The final stage of bacterial cell division requires the activity of one or more enzymes capable of degrading the layers of peptidoglycan connecting two recently developed daughter cells. Although this is a key step in cell division and is required by all
Erik C Hett   +3 more
doaj   +1 more source

Structural Investigations on the SH3b Domains of Clostridium perfringens Autolysin through NMR Spectroscopy and Structure Simulation Enlighten the Cell Wall Binding Function

open access: yesMolecules, 2021
Clostridium perfringens autolysin (CpAcp) is a peptidoglycan hydrolase associated with cell separation, division, and growth. It consists of a signal peptide, ten SH3b domains, and a catalytic domain.
Yubao Shan   +6 more
doaj   +1 more source

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