Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

A hybridoma produced by the polyethylene glycol fusion of the NS-1 variant of the P3x63Ag8 BALB/c plasmacytoma to splenocytes harvested from a BALB/c mouse immunized with whole gonococci was found to be producing antibody to a common region on gonococcal lipopolysaccharide (LPS). Enzyme-linked immunosorbent assay inhibition systems were established by utilizing this antibody, designated 3F11, and 100% inhibition occurred with both LPS and the LPS-LPS and LPS-derived polysaccharides partially inhibited the enzyme-linked immunosorbent assay, whereas similar preparations isolated from Escherichia coli O:111, the J-5 mutant of this strain, and Salmonella minnesota Re595 failed to inhibit the assay. Studies utilizing whole gonococcal strains 4505 and the isogenic variant 4505r, which lacks both the LPS serotype and common determinants as inhibitors, demonstrated that the determinant recognized by the 3F11 antibody was present on the surface of 4505 and absent on 4505r. Inhibition studies were performed with beta-glucose, beta-galactose, D-glucosamine, D-galactosamine, heptose, 2-keto-3-deoxyoctanoate, N-acetylglucosamine, N-acetylgalactosamine, alpha-lactose, and beta-lactose. Complete inhibition of the enzyme-linked immunosorbent assay occurred with D-galactosamine, and partial inhibition was achieved with both alpha-lactose and beta-lactose. Based on these observations, the 3F11 antibody recognizes a site common to gonococcal LPS which is partially shared by meningococcal LPS. The chemical structure of the determinant appears to be a D-galactosamine-O-D-galactopyranosyl-(1-4)-D-glucopyranose. Additional specificity may be conferred by the steric relationship of the determinant on the intact LPS.
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PMID:Monoclonal antibody analysis of lipopolysaccharide from Neisseria gonorrhoeae and Neisseria meningitidis. 617 50

Homologous antisera were raised against lipopolysaccharides (LPSs) isolated from pyocin 103-sensitive JW31 strain Neisseria gonorrhoeae and its isogenic, pyocin-resistant variant, JW31R. Changes in immunochemical reactivity of LPS antigen associated with pyocin-resistance were examined by enzyme-linked immunosorbent assay, employing homologous and heterologous anti-LPS immune sera. The acquisition of pyocin 103 resistance is accompanied by a loss in LPS antigen reactivity with homologous anti-LPS. The variant LPS of pyocin 103-resistant mutants is immunogenic and displays a new, distinct antigenic specificity shared with other pyocin 103-resistant variant gonococcal strains. The acquisition of pyocin 103 resistance by JW31 strain gonococci is also accompanied by a striking loss of LPS cross-reactivity with antistreptococcal polysaccharide reagents having an antibody combining site specificity directed against the chemically defined lactose polymer from Streptococcus faecalis cell wall and pneumococcal type 14 capsular polysaccharide. When examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and sodium dodecyl sulfate-urea-polyacrylamide gel electrophoresis, JW31 and JW31R LPSs show banding patterns characteristic of microheterogeneous, rough-type LPS devoid of O-side chains. Immunoblot transfer analysis of gel-separated gonococcal LPS antigens shows a difference in the pattern of antibody binding by homologous versus cross-reactive anti-LPS, which suggests a heterogeneity in the distribution of cross-reactive determinants among LPS molecules.
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PMID:Antigenic specificity and heterogeneity of lipopolysaccharides from pyocin-sensitive and -resistant strains of Neisseria gonorrhoeae. 619 64

Pooled normal human serum (NHS), as well as 10 individual NHS samples, markedly inhibited the reaction between monoclonal antibodies and their cognate epitopes on protein I of serum-sensitive, serum-resistant, and disseminated gonococcal infection-associated strains of Neisseria gonorrhoeae, as determined by ELISA inhibition. IgG was the immunoglobulin class responsible for the inhibition. Only the Fab fragment of IgG was inhibitory, making it likely that the IgG reacted specifically with protein I. After absorption with purified protein I, NHS did not inhibit the binding of a protein III-specific monoclonal antibody, thus excluding the possibility that protein III-specific antibodies in NHS masked epitopes on protein I. In addition, lipopolysaccharide-specific IgG in NHS did not appear to contribute to the inhibition of monoclonal antibody binding to protein I. The IgG from NHS was opsonic; opsonization was prevented by coating gonococci with the Fab fragment of protein I-specific monoclonal antibodies.
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PMID:Gonococcal protein I-specific opsonic IgG in normal human serum. 619 95

The antigen-specific basis of human serum immunoglobulin G antibody response to complicated gonococcal infection was studied in 13 patients by using the Western blot technique for transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to nitrocellulose paper. Of 13 patients (8 with disseminated gonococcal infection, 4 with pelvic inflammatory disease, 1 with gonococcal epididymitis), 12 reacted with protein I antigens and 9 with lipopolysaccharide (LPS). Sera from eight patients reacted with both protein I and LPS, whereas sera from four reacted only with protein I, and one sera reacted with LPS alone. One serum with antibody to both protein I and LPS by Western blot analysis was tested for bactericidal activity before and after adsorption of antibody to LPS. Removal of antibody to LPS reduced the bactericidal titer of this serum from 1:100 to 1:50, indicating that antibody to both antigens may be bactericidal for Neisseria gonorrhoeae.
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PMID:Analysis of the antigen specificity of the human serum immunoglobulin G immune response to complicated gonococcal infection. 619 84

The technique of immuno-blotting was used to examine the specificity of serum antibodies in patients with gonorrhoea and to define the significant antigenic determinant present in the desoxycholate extracts of gonococcal cell walls used previously for serological diagnosis. IgG but not IgA antibody was directed predominantly against lipopolysaccharide. Antibodies to outer membrane proteins were not found as frequently as expected. There was a suggestion from the results that antibodies to antigen PI was more common in systemic than in local infections.
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PMID:Application of immuno-blotting to the differentiation of specific antibodies in gonorrhoea. 619 94

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of purified lipopolysaccharide (LPS) from Neisseria gonorrhoeae resulted in the formation of multiple bands. Many of the bands consisted of LPS aggregates, which could be dissociated by treatment with 0.1 M NaOH or by addition of 4 M urea to the separating gel. The unaggregated LPS was usually found in one to three bands toward the bottom of the gels, a result suggesting that a long repeating O antigen is not present on gonococcal LPS. SDS-PAGE of LPS from different LPS serotypes of N gonorrhoeae indicated that structural heterogeneity exists. Antigenic analysis by enzyme-linked immunosorbent assay inhibition of gonococcal LPS extracted with phenol-chloroform-petroleum ether (PCP) and phenol-water revealed that PCP-extracted LPS contained substantially less serotype-specific antigen than did phenol-water-extracted LPS. These results suggest that the PCP and phenol-water methods extract different molecular species of LPS from N gonorrhoeae.
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PMID:Electrophoretic and serological characterization of the lipopolysaccharide produced by Neisseria gonorrhoeae. 620 6

The lipopolysaccharide (LPS) of Neisseria gonorrhoeae whole-cell lysates and proteinase K-digested lysates was examined and compared with purified homologous LPS by a method which preferentially stains LPS in polyacrylamide gels. The silver-stained profile of gonococcal LPS in the proteinase K-digested lysate was similar to that of homologous purified LPS; however, the LPS profile in whole-cell lysates was much smaller than that of digested lysates or purified LPS. Conditions of solubilization did not affect these differences. Since it is known that LPS migrates in a unique fashion in second-dimension electrophoresis, the location of LPS in the whole-cell lysates was probed by second-dimension sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a variety of stains and radiolabels. Results from these experiments indicated a stable and reproducible association of LPS with proteins ranging between 23,000 to 36,000 in Mr, in particular major outer membrane protein I. In addition to staining with the silver method, which preferentially stains LPS, the putative LPS was resistant to digestion by proteinase K, did not stain with Coomassie brilliant blue, and was not labeled extrinsically with 125I (Iodogen method) or intrinsically with [35S]methionine. Analysis of two-dimensional gels by immunoblotting with rabbit antisera prepared from protein I bands removed from a polyacrylamide gel revealed the presence of antigens in the same area of the gel (below proteins that were 23,000 to 36,000 in Mr). Antibodies to constituents which migrated below the diagonal were essentially removed by adsorption of antisera with purified LPS, as were antibodies to homologous LPS and LPS in proteinase K-digested whole-cell lysates. Immunoblotting with a monoclonal antibody specific for LPS demonstrated reactivity of the antibody with LPS and with the protein I band. On the basis of these data, we conclude that protein I and perhaps other proteins in the whole-cell lysate are stably associated with LPS; this complex is resistant to dissociation in sodium dodecyl sulfate at high temperature (approximately 100 degrees C) but does, for unknown reasons, dissociate with electrophoresis in the second dimension. The association of LPS with protein antigens in sodium dodecyl sulfate-polyacrylamide gels adds another dimension of complexity to analysis of these antigens by immunoelectroblotting. Furthermore, the tight association of LPS with the major outer membrane protein I may alter the nature of the immune response generated by "purified" protein I vaccine antigens. The possible role of protein-LPS complexes in the pathogenesis of gonorrhea is discussed.
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PMID:Analyses of gonococcal lipopolysaccharide in whole-cell lysates by sodium dodecyl sulfate-polyacrylamide gel electrophoresis: stable association of lipopolysaccharide with the major outer membrane protein (protein I) of Neisseria gonorrhoeae. 620 9

Pyocins from Pseudomonas aeruginosa were used to select several lipopolysaccharide (LPS) mutants of Neisseria gonorrhoeae strain FA19. Three classes of LPS mutans were found in the initial group selected for study. The LPS of one class lacked galactose. That of a second group lacked the typical heptose found in the parental LPS, was reduced in glucose, galactose, and N-acetylglucosamine content, appeared to contain a new unidentified sugar component, and consisted of two species of LPS separable on sodium dodecyl sulfate-polyacrylamide gels. The LPS of a third strain lacked the heptose, glucose, galactose, and N-acetylglucosamine found in the oligosaccharide portion of parental FA19 LPS. The minimal inhibitory concentration for polymyxin B of the mutant strains was 3 to 4 times that of the parental strain. The strains lacking only galactose were as resistant as the parent to the bactericidal action of normal human serum, but cells of the other two classes were quickly killed by serum. Gonococcal LPS thus appears to be important in determining phenotypic properties of the cells.
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PMID:Pyocin-resistant lipopolysaccharide mutans of Neisseria gonorrhoeae: alterations in sensitivity to normal human serum and polymyxin B. 628 51

Growth of Neisseria gonorrhoeae strain FA171 in continuous culture under glucose-limiting conditions resulted in a growth-rate-dependent change in the lipopolysaccharide (LPS). The evidence for this change is an alteration in the mobility of purified alkali-treated LPS on sodium dodecyl sulfate-polyacrylamide gels and a quantitative difference in the amount of the LPS serotype antigen. The LPS from cells grown at a low dilution rate (0.12 h-1) contained ca. eightfold less serotype antigen than the LPS from cells grown at a high dilution rate (0.56 h-1). The decrease in LPS serotype antigen was associated with an increase in sensitivity to the bactericidal activity of normal human serum and an increase in cell surface hydrophobicity. An increase in the amount of serotype antigen was associated with a reduction in the accessibility of a monoclonal antibody to a core LPS determinant, an increase in resistance to normal human serum, and a decrease in cell surface hydrophobicity. The microheterogeneity of gonococcal LPS with respect to the content of serotype antigen may result from an alteration in the metabolism of glucose.
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PMID:Effect of dilution rate on lipopolysaccharide and serum resistance of Neisseria gonorrhoeae grown in continuous culture. 640 6

The gonococcal isolates from 15 contact pairs and three large contact groups were examined using various methods to assess the stability of different typing markers. With the exception of one contact group which showed variable proline requirements, the auxotypes were stable during natural transmission. Serogrouping using the coagglutination method to detect W and M antigens was undertaken. The lipopolysaccharide M antigens were readily lost and gained during transmission whereas the protein W antigens represented stable markers and are thus useful for epidemiological studies.
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PMID:Neisseria gonorrhoeae: stability of typing markers after natural transmission. 640 44


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