1972
DOI: 10.1128/mmbr.36.4.407-477.1972
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Peptidoglycan types of bacterial cell walls and their taxonomic implications.

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Cited by 2,530 publications
(1,304 citation statements)
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References 242 publications
(384 reference statements)
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“…Bacterial cell walls contain peptidoglycan, with N-acetylmuramic acid being the molecular signature for the presence of peptidoglycan [31]. Archaea are considerably more diverse in the composition of the cell wall; they lack peptidoglycan in any form, but instead, proteins, glycoproteins and polysaccharides cover the outside of the cell membrane [32].…”
Section: Cell-wall Synthesis Inhibitorsmentioning
confidence: 99%
“…Bacterial cell walls contain peptidoglycan, with N-acetylmuramic acid being the molecular signature for the presence of peptidoglycan [31]. Archaea are considerably more diverse in the composition of the cell wall; they lack peptidoglycan in any form, but instead, proteins, glycoproteins and polysaccharides cover the outside of the cell membrane [32].…”
Section: Cell-wall Synthesis Inhibitorsmentioning
confidence: 99%
“…One candidate is the PGN cross-linking peptide which is highly variable in theses species (Fig. 1) (Schleifer and Kandler, 1972). Another possibility is the presence of significant amounts of Glycine-substituted D -Glu at the second position of the stem-peptide in M. luteus PGN, but not other PGNs (Schleifer and Kandler, 1972).…”
Section: Bacterial Recognition In the Toll Pathwaymentioning
confidence: 99%
“…Experimental studies have tested the specificity of purified native endolysins against Gram-positive bacterial panels, mostly composed by multiple strains or species belonging to a single genus, and overall displaying an intra-genus specificity (Yoong et al, 2006;Park et al, 2012;Hojckova et al, 2013;Schmelcher et al, 2015). Contrarily, a novel endolysin against Acinetobacter have shown a broad activity spectrum against Gram-negative bacteria (Oliveira et al, 2016), which are known to share the A1γ chemotype (Schleifer and Kandler, 1972). More recently, engineered endolysins with altered specificity have been developed by shuffling their enzymatic active domain (EAD) and cell wall binding domains (CBD), or by changing their net charge, contributing to the understanding of the molecular mechanisms underlying specificity (Low et al, 2011;Schmelcher et al, 2011;Wu et al, 2014;Yang et al, 2015;São-José, 2018).…”
Section: Introductionmentioning
confidence: 99%