Strain-related differences in lysozyme sensitivity and extent of O-acetylation of gonococcal peptidoglycan

Rosenthal, R S; Blundell, Jennifer; Perkins, H. R.

doi:10.1128/iai.37.2.826-829.1982

Cited by 60 publications

(48 citation statements)

References 15 publications

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“…Rheumatoid arthritis, an autoimmune disease, is induced in animal models by undigestible high-molecularweight peptidoglycan fragments (Hamerman, 1966;Ginsburg & Sela, 1976;Chedid et al, 1978;Fox et al, 1982;Esser et al, 1985;Koga et al, 1985;Fleming et al, 1986;Stimpson et al, 1986). Indeed, in vivo studies demonstrated that the persistence of peptidoglycan in a host is directly attributable to the high degree of O-acetylation (Blundell et al, 1980;Rosenthal et al, 1982;Swim et al, 1983;Fleming et al, 1986). As in the case of deacetylation, O-acetylation could have an effect on the recognition of peptidoglycan fragments by host factors such as peptidoglycan recognition proteins.…”

Section: Biological Roles Of Peptidoglycan O -Acetylationmentioning

confidence: 99%

Structural variation in the glycan strands of bacterial peptidoglycan

2008

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The normal, unmodified glycan strands of bacterial peptidoglycan consist of alternating residues of beta-1,4-linked N-acetylmuramic acid and N-acetylglucosamine. In many species the glycan strands become modified after their insertion into the cell wall. This review describes the structure of secondary modifications and of attachment sites of surface polymers in the glycan strands of peptidoglycan. It also provides an overview of the occurrence of these modifications in various bacterial species. Recently, enzymes responsible for the N-deacetylation, N-glycolylation and O-acetylation of the glycan strands were identified. The presence of these modifications affects the hydrolysis of peptidoglycan and its enlargement during cell growth. Glycan strands are frequently deacetylated and/or O-acetylated in pathogenic species. These alterations affect the recognition of bacteria by host factors, and contribute to the resistance of bacteria to host defence factors such as lysozyme.

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Section: Biological Roles Of Peptidoglycan O -Acetylationmentioning

confidence: 99%

Structural variation in the glycan strands of bacterial peptidoglycan

2008

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“…1) there was no evidene that either the mono-or the di-O-acetylated dimer was the better substrate. Enzyme from strain RD 5, known to have poorly O-acetylated peptidoglycan [3,4] produced almost identical results (not shown). Our previous work [7] showed that 20% of the endopeptidase activity of ether-treated gonococci was resistant to beta-lactam antibiotics.…”

Section: Resultsmentioning

confidence: 79%

“…The peptidoglycan of N. gonorrhoeae is Oacetylated [|] on about 40-50% of the available muramic acid residues [2][3][4], although strain RD 5 has greatly decreased levels of O-acetylation [3,4]. In growing cells, 65% of the total O-acetylation takes 10 rain, the remainder taking a further 50 min [5].…”

Section: Introductionmentioning

confidence: 99%

Selectivity for O-acetylated peptidoglycan during endopeptidase action by permeabilized Neisseria gonorrhoeae

Blundell

1985

FEMS Microbiology Letters

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The endopeptidase(s) of ether-treated cells of Neisseria gonorrhoeae cleaved O-acetylated peptidoglycan dimers about 3 times as rapidly as non-O-acetylated dimers. This was true whether the enzyme came from a highly O-acetylated strain or from one with low O-acetylation. The penicillin-resistant fraction of the endopeptidase activity also showed the same substrate selectivity. acetylated monomers would arise solely as a result of endopeptidase action. However, although dimer units were O-acetylated slightly more rapidly than monomer units [5], a precursor-product relationship seemed unlikely.In the present experiments we have compared the rates of cleavage of dimer units with 0, 1 or 2 O-acetyl groups by gonococcal endopeptidases. MATERIALS AND METHODS

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“…Both the composition of peptidoglycan itself and of associated polysaccharide affect the inflammatory properties of streptococcal cell walls. Extensive O-acetylation of the glycan backbone of PG decreases the susceptibility of peptidoglycan to lysozyme ( Gallis et al 1976, Rosenthal et al 1982. Extensive N-acetylation has the opposite effect (Amano et al 1980).…”

Section: Elimination and Degradation Of Bacterial Debrismentioning

confidence: 99%

Role of bacterial debris in inflammatory diseases of the joint and eye

Fox

1990

APMIS

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Fox, A. Role of bacterial debris in inflammatory diseases of the joint and eye. APMIS 98: 957-968,1990.Several distinct rheumatic conditions (including Lyme arthritis, Reiter's syndrome and rheumatic fever) as well as certain forms of the blinding disease, uveitis, may share a common etiology. In each instance specific bacterial pathogens may infect a distant site, which on interaction with the immune system, leads to a sterile inflammation in the joint or eye. These "reactive" conditions may result, in some cases, from prior localization of non-viable bacterial remnants (including the cell wall or peptidoglycan) or alternatively "dormant" fastidious bacteria in the affected joint or eye where they act as persisting antigens. Classical culture techniques, would not detect the presence of these putative microbial antigens. Alternative approaches for detection of ubiquitous components of bacteria in the host (using appropriate chemical, molecular and immunological techniques) are discussed.

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Strain-related differences in lysozyme sensitivity and extent of O-acetylation of gonococcal peptidoglycan

Cited by 60 publications

References 15 publications

Structural variation in the glycan strands of bacterial peptidoglycan

Structural variation in the glycan strands of bacterial peptidoglycan

Selectivity for O-acetylated peptidoglycan during endopeptidase action by permeabilized Neisseria gonorrhoeae

Role of bacterial debris in inflammatory diseases of the joint and eye

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