Clostridioides difficile canonical L,D-transpeptidases catalyze a novel type of peptidoglycan cross-links and are not required for beta-lactam resistance-Reference-Cited by-同舟云学术

Clostridioides difficile canonical L,D-transpeptidases catalyze a novel type of peptidoglycan cross-links and are not required for beta-lactam resistance

Published:2024-01 Issue:1 Volume:300 Page:105529
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Galley Nicola F.^ORCID,Greetham Darren^ORCID,Alamán-Zárate Marcel G.^ORCID,Williamson Mike P.^ORCID,Evans Caroline A.^ORCID,Spittal William D.^ORCID,Buddle Jessica E.^ORCID,Freeman Jane^ORCID,Davis Georgina L.,Dickman Mark J.^ORCID,Wilcox Mark H.^ORCID,Lovering Andrew L.^ORCID,Fagan Robert P.^ORCID,Mesnage Stéphane^ORCID

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

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2. Current status of Clostridium difficile infection epidemiology;Lessa;Clin. Infect. Dis.,2012

3. Pathogenicity and virulence of Clostridioides difficile;Buddle;Virulence,2023

4. Mechanism of action of beta-lactam antibiotics at the molecular level;Frere;Biochem. Pharmacol.,1977

5. Beta-lactam antibiotics induce a lethal malfunctioning of the bacterial cell wall synthesis machinery;Cho;Cell,2014

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1. Identification of a family of peptidoglycan transpeptidases reveals that Clostridioides difficile requires noncanonical cross-links for viability;Proceedings of the National Academy of Sciences;2024-08-16

2. The L,D-transpeptidation pathway is inhibited by antibiotics of the β-lactam class in Clostridioides difficile;2024-06-13

3. Identification of a new family of peptidoglycan transpeptidases reveals atypical crosslinking is essential for viability inClostridioides difficile;2024-03-14

4. PGFinder, an Open-Source Software for Peptidoglycomics: The Structural Analysis of Bacterial Peptidoglycan by LC-MS;Methods in Molecular Biology;2024