Complement consumption gonococcal peptidoglycan

Petersen, Bruce H.; Rosenthal, R S

doi:10.1128/iai.35.2.442-448.1982

Cited by 20 publications

(11 citation statements)

References 23 publications

(24 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…To test this hypothesis, our main objectives have been to identify and purify those PG fragments that might arise in vivo and to test their biological activities in diverse assays that are associated with modulation of inflammation and immunity. In general, we have found that various classes of physiologically realistic PG fragments possess numerous activities consistent with the notion that PG plays a role in gonococcal disease, e.g., toxicity (14), ability to activate complement (15), arthritogenicity (6), and ability to stimulate the release of functional interleukin-1 and prostaglandin E2 (T. J. Fleming and S. L. Myers, Abstr. Annu.…”

supporting

confidence: 76%

“…However, a recurrent theme to date is that several activities are potentiated by the persistence of highmolecular-weight PG. This persistence correlates closely with PG hydrolase resistance afforded by extensive substitution of glycan chains with O-acetyl residues (2,6,15,(19)(20)(21). Thus, for exatnple, extensively 0-acetylated PG (O-PG) exhibits greater resistance to commercial and human lysozyme (muramidase) and is more highly arthropathic than * Corresponding author.…”

mentioning

confidence: 92%

See 1 more Smart Citation

Degradation of gonococcal peptidoglycan by granule extract from human neutrophils: demonstration of N-acetylglucosaminidase activity that utilizes peptidoglycan substrates

et al. 1987

Self Cite

View full text Add to dashboard Cite

The degradation of purified Neisseria gonorrhoeae peptidoglycan (PG) by granule extract derived from normal human polymorphonuclear leukocytes was examined. Hen egg lysozyme-resistant, extensively 0acetylated [3H]PG (O-PG) from strain FA19 and lysozyme-sensitive, non-O-acetylated ['4CJPG (non-O-PG) from strain RD5 (each containing label in both glucosamine and muramic acid) were mixed and incubated with granule extract at pHs 4.5, 5.5, and 6.5. The rate of degradation of O-PG was uniformly slower than that of non-O-PG in the same tube, but ultimately, even the O-PG was rendered completely soluble. Molecular-sieve high-performance liquid chronmatography revealed that both PGs were degraded by granule extract at the pH values tested to disaccharide peptide monomers and peptide-cross-linked oligomers, reflecting the action of human lysozyme. Of particular interest was the appearance of a peak containing free N-acetylglucosamine which was quite prominent in reaction mixtures at pH 4.5, less prominent at pH 5.5, and not detectable at pH 6.5. Free N-acetylglucosamine was not released from control PG samples at any pH in the absence of granule extract. Treatment of purified gonococcal PG monomers with granule extract at pH 4.5 yielded exclusively free N-acetylglucosamine and muramyl peptides with no N-acetylglucosamine. These data suggest that granule extract contains a previously undescribed pH-dependent N-acetylglucosaminidase with specificity for PG as well as an N-acetylmuramidase activity that degrades O-PG less efficiently than it does non-O-PG.on August 5, 2020 by guest http://iai.asm.org/ Downloaded from 2580 STRIKER ET AL.

show abstract

supporting

confidence: 76%

mentioning

confidence: 92%

Degradation of gonococcal peptidoglycan by granule extract from human neutrophils: demonstration of N-acetylglucosaminidase activity that utilizes peptidoglycan substrates

et al. 1987

Self Cite

View full text Add to dashboard Cite

show abstract

“…In regard to the second objective, the essential conclusion is that purified PG fragments collectively do initiate biological reactions compatible with their playing a role in modulation of the host reaction to gonococcal infection. Gonococcal PG-mediated activities include (i) intrinsic toxicity for human fallopian tube mucosa (21), (ii) consumption of human complement and generation of active mediators of inflammation (24) Biemann, manuscript in preparation) have indicated that anihydro-muramic acid-containing monomers, released by growing gonococci, induce slow-wave sleep in experimental animals. This conclusion is consistent with the original observations on the somnogenic properties of muramyl peptides (18) in that a major component of anhydromonomers (the disaccharide tetrapeptide) is identical to the naturally occurring somnogenic factor (factor S) present in numerous animals including humans (17,20,32).…”

mentioning

confidence: 99%

“…(i) Sonicated (S) PG, e.g., S-O-PG and S-non-O-PG, prepared from O-PG and non-O-PG as described previously(24), were heterogeneous mixtures of soluble fragments (greater than 106 daltons) that simulated the large-molecular-weight fragments released by the action of host PG hydrolases (27), e.g., human polymorphonuclear leukocyte lysozyme. S-PG preparations used in experiments contained between less than 0.1 to 0.9% (wt/wt) non-PG amino acids, and between 0.05 and 0.25 ng of lipopolysaccharide (LPS) per ,ug of PG, as determined by the Limulus amoebocyte lysate assay (see below).…”

mentioning

confidence: 99%

Arthropathic properties of gonococcal peptidoglycan fragments: implications for the pathogenesis of disseminated gonococcal disease

Fleming¹,

Wallsmith²,

Rosenthal³

1986

Infect Immun

Self Cite

View full text Add to dashboard Cite

We examined the arthropathic activity of purified peptidoglycan (PG) fragments derived from (i) lysozymeresistant, extensively 0-acetylated PG from Neisseria gonorrhoeae FA19 (0-PG), and (ii) lysozyme-sensitive, 0-acetyl-deficient PG from N. gonorrhoeae RD5 (non-O-PG). Male Lewis rats were injected intradermally in the tail with 200 ,ug of PG emulsified in mineral oil and water (1:1) or with the oil and water emulsion alone (controls). Quantitation of hind paw size indicated that macromolecular PG of various chemical and physical forms induced paw swelling (P versus controls, less than 0.01) that was evident at about day 14 and that reached a maximum at about day 24. PG-mediated paw swelling was accompanied by intense synovitis with some cartilage and bone involvement. The minimal arthropathic dose of soluble macromolecular PG was 20 ,ug per rat. Of particular interest was that macromolecular O-PGs from strain FA19 caused considerably more extensive swelling than did either their RD5 non-O-PG counterparts or the homologous FA19 PG that had been de-0-acetylated by mild alkali treatment. This suggested that the persistence of hydrolase-resistant highmolecular-weight fragments, afforded by extensive 0-acetylation, may be important for optimal expression of arthropathic activity. However, oligomeric PG was not an absolute requirement, since even low-molecularweight fragments, including the anhydro-muramyl-containing disaccharide peptide monomer released by growing gonococci, were also arthritogenic. Experiments employing purified gonococcal lipopolysaccharide indicated that the arthropathic activity of PG preparations was not due to contaminating lipopolysaccharide. Based on the arthritogenicity of gonococcal PG in this model system, we suggest that PG may play a role in the pathogenesis of gonococcal arthritis, and that such an activity might be potentiated by the persistence of hydrolase-resistant O-PG. 600 on July 31, 2020 by guest http://iai.asm.org/ Downloaded from

show abstract

“…Another aspect of gonococcal biology in which the diverse peptidoglycan structures may be of importance is host interactions. Gonococci exhibit substantial cell wall turnover, and release of gonococcal peptidoglycan fragments has been implicated in several pathological host responses (10,13). The possibility of variations in host effects by different peptidoglycan subunits must be entertained.…”

Section: Discussionmentioning

confidence: 99%

Analysis of Neisseria gonorrhoeae peptidoglycan by reverse-phase, high-pressure liquid chromatography

Dougherty¹

1985

J Bacteriol

View full text Add to dashboard Cite

The muramidase digest of peptidoglycan from Neisseria gonorrhoeae was isolated and analyzed by the use of a reverse-phase, high-pressure liquid chromatography system. As was found previously in the case of Escherichia coli, gonococci peptidoglycan is also composed of a greater number of muropeptides than can be resolved with thin-layer chromatography systems. Preliminary classification of the muropeptide components into subclasses based on O-acetyl modification and degree of cross-linkage was achieved. Examination of a penicillin-susceptible strain and a highly resistant strain with two penicillin-binding protein alterations synthesized distinctly different peptidoglycan structures, as revealed by this technique.All gram-negative bacteria studied possess one chemical type of peptidoglycan, Aly, and variations have been believed to be limited to degree of muropeptide cross-linkage, degree of amidation of the carboxyl groups of the peptide subunit, and O-acetylation of the disaccharide (15,21). Recent investigations by Glauner and Schwarz, who used the extreme resolving power of reverse-phase, high-pressure liquid chromatography (HPLC), established that Escherichia coli peptidoglycan has a much greater heterogeneity in muropeptide structure than previously thought (5). Variations include substitution of amino acids, such as glycine for alanine, and direct cross-links between diaminopimelic acid residues at the site of lipoprotein attachment. These findings raise the possibility of specialized domains within the peptidoglycan structure and roles for the multiple penicillin-binding proteins (PBPs) in assembly of these regions. In another recent study, this technology was used to characterize several modifications that the peptidoglycan of E. coli undergoes during transitions in growth states (11).In the present study, the reverse-phase HPLC system was used for examination of the peptidoglycan structure of Neisseria gonorrhoeae. A complex, reproducible pattern of muramidase-digested peptidoglycan fragments was obtained. The fragments were classified into groups by the degree of peptide cross-linkage and O-acetylation, and preliminary identification of some species was assigned. Peptidoglycan from a highly penicillin-resistant strain with reduced binding affinity in two of its PBPs was examined. Several differences in the peptidoglycan digest from penicillin-susceptible and -resistant strains of gonococci were evident. N.Y. Strains were kept frozen in gonococcal broth with 15% glycerol at -70°C. Stocks were thawed, and cultures were maintained by daily passage on GCBA agar plates with 1% IsoVitaleX supplement (BBL Microbiology Systems, Cockeysville, Md.). Incubation was at 37°C in 5% CO2. Colonies were p-, transparent by the criteria of Swanson (19).Peptidoglycan preparation. Gonococci were inoculated into 500-ml volumes of gonococcal broth with 1% IsoVitaleX and 420 ,ug of NaHCO3 per ml. These cultures, in 2-liter flasks, were grown at 37°C with agitation (140 rpm) in a New Brunswick G-25 shaker (New Brunswick Scienti...

show abstract

Complement consumption gonococcal peptidoglycan

Cited by 20 publications

References 23 publications

Degradation of gonococcal peptidoglycan by granule extract from human neutrophils: demonstration of N-acetylglucosaminidase activity that utilizes peptidoglycan substrates

Degradation of gonococcal peptidoglycan by granule extract from human neutrophils: demonstration of N-acetylglucosaminidase activity that utilizes peptidoglycan substrates

Arthropathic properties of gonococcal peptidoglycan fragments: implications for the pathogenesis of disseminated gonococcal disease

Analysis of Neisseria gonorrhoeae peptidoglycan by reverse-phase, high-pressure liquid chromatography

Contact Info

Product

Resources

About