Results 21 to 30 of about 14,027 (185)

Identification of a novel zinc metalloprotease through a global analysis of clostridium difficile extracellular proteins [PDF]

open access: yes, 2013
Clostridium difficile is a major cause of infectious diarrhea worldwide. Although the cell surface proteins are recognized to be important in clostridial pathogenesis, biological functions of only a few are known.
A Barketi-Klai   +73 more
core   +12 more sources

The hydrolase LpqI primes mycobacterial peptidoglycan recycling [PDF]

open access: yesNature Communications, 2018
Abstract Growth and division by most bacteria requires remodelling and cleavage of their cell wall. A byproduct of this process is the generation of free peptidoglycan (PG) fragments known as muropeptides, which are recycled in many model organisms.
Moynihan, Patrick J.   +7 more
openaire   +4 more sources

Staphylococcus aureus sacculus mediates activities of M23 hydrolases

open access: yesNature Communications, 2023
Peptidoglycan, a gigadalton polymer, functions as the scaffold for bacterial cell walls and provides cell integrity. Peptidoglycan is remodelled by a large and diverse group of peptidoglycan hydrolases, which control bacterial cell growth and division ...
Alicja Razew   +6 more
doaj   +1 more source

Treating Bacterial Infections with Bacteriophage-Based Enzybiotics: In Vitro, In Vivo and Clinical Application

open access: yesAntibiotics, 2021
Over the past few decades, we have witnessed a surge around the world in the emergence of antibiotic-resistant bacteria. This global health threat arose mainly due to the overuse and misuse of antibiotics as well as a relative lack of new drug classes in
Katarzyna M. Danis-Wlodarczyk   +2 more
doaj   +1 more source

Peptidoglycan Hydrolase Fusions Maintain Their Parental Specificities [PDF]

open access: yesApplied 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   +5 more
openaire   +2 more sources

Imbalance of peptidoglycan biosynthesis alters the cell surface charge of Listeria monocytogenes

open access: yesThe Cell Surface, 2022
The bacterial cell wall is composed of a thick layer of peptidoglycan and cell wall polymers, which are either embedded in the membrane or linked to the peptidoglycan backbone and referred to as lipoteichoic acid (LTA) and wall teichoic acid (WTA ...
Lisa Maria Schulz   +4 more
doaj   +1 more source

A predator-prey interaction between a marine Pseudoalteromonas sp. and Gram-positive bacteria [PDF]

open access: yes, 2020
Predator-prey interactions play important roles in the cycling of marine organic matter. Here we show that a Gram-negative bacterium isolated from marine sediments (Pseudoalteromonas sp.
Chen, Xiu-Lan   +16 more
core   +2 more sources

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

A new peptidoglycan hydrolase in Streptococcus pneumoniae [PDF]

open access: yesFEMS Microbiology Letters, 1986
The use of a mutant of Streptococcus pneumoniae deleted in the lytA gene coding for the N-acetyl-muramyl-l-alanine amidase, and therefore devoid of any amidase, has allowed the identification of a new murein hydrolase activity in this bacterium. This enzyme (or enzymes) acted as an autolysin when the cultures were grown at 30°C.
J.M. Sańchez-Puelles   +5 more
openaire   +2 more sources

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