Evidence for peptidoglycan-associated protein(s) in Neisseria gonorrhoeae

Hebeler, B H; Morse, Stephen; Wong, William; Young, Frank E.

doi:10.1016/0006-291x(78)91451-1

Cited by 15 publications

(13 citation statements)

References 13 publications

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“…If similar free PG fragments are released in vivo, it seems likely, based on present data, that their small size precludes involvement in complement activation. On the other hand, gonococci growing in vivo may release largemolecular-weight free PG fragments (some of which may possess 0-acetylated derivatives resulting in resistance of PG to degradation by lysozyme) (1) or complexes containing PG associated with other cell envelope components, e.g., protein (9). These PG fragments presumably would be available to react with natural anti-PG antibody and complement in a manner that may generate active mediators of inflammation.…”

Section: -mentioning

confidence: 99%

Complement consumption gonococcal peptidoglycan

Petersen¹,

Rosenthal²

1982

Infect Immun

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Purified peptidoglycan (PG) obtained from Neisseria gonorrhoeae was tested for the ability to consume complement in normal human sera. Sonicated PG (S-PG), a heterogeneous mixture of soluble fragments (molecular weight, greater than 10(6)), as well as intact (insoluble) PG, reduced the level of whole hemolytic complement in a pool of four human sera. The minimal concentration of S-PG required for this activity was approximately 500 micrograms of S-PG per ml of serum. Complete lysozyme digestion of S-PG, yielding PG fragments of less than 10(4) molecular weight, eliminated complement-consuming activity. S-PG-mediated complement consumption resulted in depletion of the individual complement components C4 and C3. Consumption of complement did not occur when C4-deficient human serum or normal human sera treated with Mg2+-(ethylene glycol-bis(beta-aminoethyl ether)-N,N-tetraacetic acid to specifically impair classical complement pathway activity were used. The addition of rabbit anti-PG antibody greatly enhanced gonococcal PG-mediated complement consumption. Together, the data suggested that gonococcal PG-mediated complement consumption occurred via the classical complement pathway, was dependent on the presence of anti-PG antibody, and required glycosidically linked polymers of PG. Individual human sera varied widely in the extent of gonococcal PG-mediated reduction of complement levels, presumably a reflection of either different amounts of natural antibody to gonococcal PG, different levels of human PG hydrolase(s) capable of degrading PG to inactive fragments, or both.

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Section: -mentioning

confidence: 99%

Complement consumption gonococcal peptidoglycan

Petersen¹,

Rosenthal²

1982

Infect Immun

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“…Similarly, it was found that penicillin-induced lysis could also be prevented by growth at a low pH in the presence of Mg2+ (33). These results suggest that the decrease in the autolytic activity of the PG at a low pH was due in part to an increased stability of the cell, possibly through the association of protein with the PG (13,14).…”

mentioning

confidence: 71%

“…In contrast to the situation with other gram-negative organisms (4), a PG-associated protein analogous to Braun lipoprotein (BLP) has not been found in N. gonorrhoeae (15,34). Nonetheless, gonococci are believed to possess a PG-associated protein(s) after in vitro growth in acidic medium (pH 6) (13,14). However, the identity of this protein(s) is complicated because of the extreme insolubility of the N. gonorrhoeae PG-protein complex.…”

mentioning

confidence: 96%

“…MATERIALS AND METHODS Strains. N. gonorrhoeae CS7 (13,14), a gift from Tom Dougherty (Rockefeller University, New York, N.Y.), was primarily used in this study. Strains JS1, JS3, FA635, and FA638 have been described elsewhere (19).…”

mentioning

confidence: 99%

“…The liquid medium was identical to the clear typing medium except for the omission of the agar and the inclusion of NaHCO3 (420 ng/ml) as the CO2 source. The liquid medium was buffered to pH 6 (conditions at which optimum protein association occurs with the PG fraction [13,14]) by adjusting the potassium salt ratios. The cells were grown in conical flasks at 37°C by using a wrist-action shaker.…”

mentioning

confidence: 99%

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Identification and characterization of peptidoglycan-associated proteins in Neisseria gonorrhoeae

Hill

Judd

1989

Infect Immun

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The principal proteins associated with Neisseria gonorrhoeae peptidoglycan (PG), as identified by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, are the following: two proteins at approximately 90 kilodaltons (kDa), single major species at both 60 and 44 kDa, a 34to 36-kDa protein, and three proteins between 28 and 32 kDa. A protein analogous to Escherichia coli Braun lipoprotein was not detected with gonococcal cell wall preparations. The identity of the PG-associated proteins was confirmed immunologically with antibody generated against purified cell wails. Two types of protein species, dithiothreitol extractable (the majority) and alkylation dependent (primarily the 34to 36-kDa protein), appeared to be associated with the N. gonorrhoeae cell wall fraction. It was found that a crucial step in the extraction of the proteins from the PG fraction was the inclusion of an acetone-water wash of the purified PG pellet. Studies with cell wall preparations obtained from N. gonorrhoeae intrinsically labeled with 32P revealed that the acetone wash was removing phospholipid from the cell wall fraction and thus facilitating protein extraction. Autoradiographic analysis with PG material derived from 125j-surface-labeled cells indicated that the 44-kDa protein is exposed on the surface of the organism even when associated with the PG layer. Radioimmunoprecipitation with anti-PG antibody confirmed these findings. Lectin analysis (wheat germ agglutinin conjugated to horseradish peroxidase) suggested that the 34to 36-kDa protein is covalently attached to the PG layer.

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The Outer Membrane of Acinetobacter: Structure-Function Relationships

Borneleit¹,

Kleber²

1991

The Biology of Acinetobacter

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Evidence for peptidoglycan-associated protein(s) in Neisseria gonorrhoeae

Cited by 15 publications

References 13 publications

Complement consumption gonococcal peptidoglycan

Complement consumption gonococcal peptidoglycan

Identification and characterization of peptidoglycan-associated proteins in Neisseria gonorrhoeae

The Outer Membrane of Acinetobacter: Structure-Function Relationships

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