Bacterial cell envelope peptidoglycan

Vollmer, Waldemar; Born, Petra

doi:10.1016/b978-0-12-374546-0.00002-x

Cited by 12 publications

(14 citation statements)

References 93 publications

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“…LYSO activity is dominant in phages infecting G Ϫ species. This can be explained by the ability of many G ϩ pathogens to modify their glycan strands by N-glycosylation, de-N-acetylations, and/or O-acetylations that contribute to high levels of resistance to lysozyme (62).…”

Section: Resultsmentioning

confidence: 99%

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Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Oliveira

Melo

Santos

et al. 2013

J Virol

242

247

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Phages are recognized as the most abundant and diverse entities on the planet. Their diversity is determined predominantly by their dynamic adaptation capacities when confronted with different selective pressures in an endless cycle of coevolution with a widespread group of bacterial hosts. At the end of the infection cycle, progeny virions are confronted with a rigid cell wall that hinders their release into the environment and the opportunity to start a new infection cycle. Consequently, phages encode hydrolytic enzymes, called endolysins, to digest the peptidoglycan. In this work, we bring to light all phage endolysins found in completely sequenced double-stranded nucleic acid phage genomes and uncover clues that explain the phage-endolysin-host ecology that led phages to recruit unique and specialized endolysins.

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Section: Resultsmentioning

confidence: 99%

“…For instance, because Staphylococcus, Streptococcus, and Lactococcus have unique 3¡4 glycine pentaglycine (Gly) 5 , dialanine (L-Ala-L-Ala), or L-Lys-D-Asp interpeptide bridges within the PG, their specific phages have acquired a CHAP domain that exclusively cleaves these links (62). LYSO activity is dominant in phages infecting G Ϫ species.…”

Section: Resultsmentioning

confidence: 99%

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Oliveira

Melo

Santos

et al. 2013

J Virol

242

247

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“…Penicillin binding proteins (PBPs) use lipid II to polymerize glycan chains through their glycosyltransferase (GTase) activity ( Goffin and Ghuysen, 1998 ; Sauvage et al, 2008 ). These chains are then attached to the existing PG layer by transpeptidases (TPases) forming peptide cross-links ( Vollmer and Born, 2010 ). Escherichia coli , transpeptidation occurs mainly by the activity of PBPs with DD-TPase activity, which carry out the formation of the peptide cross-link between D -Ala 4 and meso -DAP 3 (4–3 or DD cross-link) ( Vollmer and Born, 2010 ).…”

Section: Introductionmentioning

confidence: 99%

The Fluorescent D-Amino Acid NADA as a Tool to Study the Conditional Activity of Transpeptidases in Escherichia coli

et al. 2018

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The enzymes responsible for the synthesis of the peptidoglycan (PG) layer constitute a fundamental target for a large group of antibiotics. The family of β-lactam antibiotics inhibits the DD-transpeptidase (TPase) activity of the penicillin binding proteins (PBPs), whereas its subgroup of carbapenems can also block the TPase activity of the LD-TPases. D-Ala fluorescent probes, such as NADA, are incorporated into the PG presumably by TPases in Escherichia coli and can be used to study conditions that are required for their function. Of all LD-TPases of E. coli, only LdtD was able to incorporate NADA during exponential growth. Overproduction of LdtD caused NADA to be especially inserted at mid cell in the presence of LpoB-activated PBP1b and the class C PBP5. Using the NADA assay, we could confirm that LpoB activates PBP1b at mid cell and that CpoB regulates the activity of PBP1b in vivo. Overproduction of LdtD was able to partly compensate for the inhibition of the cell division specific class B PBP3 by aztreonam. We showed that class A PBP1c and the class C PBP6b cooperated with LdtD for NADA incorporation when PBP1b and PBP5 were absent, respectively. Besides, we proved that LdtD is active at pH 7.0 whereas LdtE and LdtF are more active in cells growing at pH 5.0 and they seem to cooperate synergistically. The NADA assay proved to be a useful tool for the analysis of the in vivo activities of the proteins involved in PG synthesis and our results provide additional evidence that the LD-TPases are involved in PG maintenance at different conditions.

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“…Peptidoglycan is found as thick outer layer in the cell wall of Gram-positive bacteria, whereas a relatively thin layer is present in the cell wall of Gram-negative bacteria, where it is overlaid with lipopolysaccharides Vollmer and Born 2009 ). Peptidoglycan from both Gram-positive and Gram-negative bacteria is composed of a network of glycan strands that are interlinked by short peptides.…”

Section: Muropeptides and Sugar Backbone Structure Pamps In Peptidoglmentioning

confidence: 99%

PAMP Signaling in Plant Innate Immunity

Vidhyasekaran

2014

PAMP Signals in Plant Innate Immunity

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Plant innate immunity is a potential basal defense system existing in plant kingdom. This system provides powerful weapons to the host plants to fi ght against viral, bacterial, fungal, and oomycete pathogens and serves as a surveillance system against invasion of pathogens. It is not active in normal healthy plants and it requires specifi c signals to get activated. Pathogen-associated molecular patterns (PAMPs) act as alarm/danger signals to trigger the plant innate immune responses. When pathogens land on the plant's surface, plants read the molecular fi ngerprints/signatures of pathogens (PAMPs) by binding the PAMPs with cognate pattern-recognition receptors (PRRs) residing in plant cell plasma membrane and trigger several defense signaling systems.

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Bacterial cell envelope peptidoglycan

Cited by 12 publications

References 93 publications

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

Molecular Aspects and Comparative Genomics of Bacteriophage Endolysins

The Fluorescent D-Amino Acid NADA as a Tool to Study the Conditional Activity of Transpeptidases in Escherichia coli

PAMP Signaling in Plant Innate Immunity

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