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)

In order to obtain specific tools for studying the alterations of the immunochemical structure of Yersinia enterocolitica lipopolysaccharide in various conditions, we have produced monoclonal antibodies reacting with core and O-polysaccharide chains of Yersinia enterocolitica O:3 LPS. Immunizations were made with whole bacterial cells and outer membrane preparation, respectively. Monoclonal antibody 2B5 reacted in enzyme immunoassay with purified core-lipid A complex, and its binding was not inhibited by Polymyxin B, suggesting that the target determinant is in the outer core. 2B5 recognized 100% of all tested Y. enterocolitica O:3 strains (n = 152) and reacted to some extent also with many other gram-negative bacteria. In immunoblotting with 2B5, a band corresponding to core-lipid A complex was visualized both with Y. enterocolitica, Brucella abortus and Haemophilus influenzae. In immunofluorescence assay, the only positive reaction was seen with Y. enterocolitica. Monoclonal antibody A6 reacted in enzyme immunoassay with purified O-polysaccharide chains, recognized 100% of tested Y. enterocolitica O:3 strains, and showed no cross-reactions with other bacteria. A typical ladder pattern was not seen in the immunoblotting analysis with A6. This suggests that the O-chain of Y. enterocolitica O:3 may be different from those in other gram-negative bacteria. These two antibodies will make it possible to study the structural variations of Yersinia enterocolitica LPS more precisely than described before, because of their fine specificity against important immunogenic components of LPS. They will also be useful in serology measuring the immune response against the target determinants of these antibodies.
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PMID:Monoclonal antibodies reacting selectively with core and O-polysaccharide of Yersinia enterocolitica O:3 lipopolysaccharide. 355 94

Gentian violet resistance was used to select mutants of Yersinia pestis with altered cell envelope permeability. Mutants in one class lacked the 6 and 61 megadalton (Mdal) plasmids, but retained the 47 Mdal plasmid associated with calcium dependence. Mutants in a second class retained all three plasmids. One mutant in the latter class, EV76S7, lacked major outer membrane protein J and yielded reduced levels of minor outer membrane proteins A and C. Protein J is known to interact differently with lipopolysaccharide (LPS) from cells bearing and cells lacking the 47 Mdal plasmid following growth at 37 degrees C. The 47 Mdal plasmid is known to influence gentian violet uptake, novobiocin sensitivity, susceptibility to phagocytosis, the growth in macrophages and the virulence of Y. pestis. Gentian violet uptake was lower and novobiocin sensitivity higher in the mutant than in the parental strain, but the underlying effects of the 47 Mdal plasmid on these parameters had not changed. EV76S7 cells were phagocytized to a greater extent than the parental cells following growth at 37 degrees C, but survival and growth within peritoneal phagocytes and the LD50's of cells with and without the 47 Mdal plasmid were not altered by the loss of protein J, we conclude that protein J--LPS interactions are not required for virulence, and that the reduced virulence of cells lacking the 47 Mdal plasmid does not result from the altered protein J--LPS interactions which are known to result from loss of the plasmid.
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PMID:A permeability mutant of Yersinia pestis with increased susceptibility to phagocytosis which retains potential for intraphagocytic growth and virulence. 356 98

The cellular lipopolysaccharide produced by Yersinia enterocolitica serotype O:5,27 was of the S-type and composed of an antigenic O-chain polysaccharide linked through a core oligosaccharide region, which in turn was linked through 3-deoxy-D-manno-octulonosyl units to a lipid A moiety. The O-chain polysaccharide was composed of equal molar amounts of L-rhamnose and D-xylulose. By partial hydrolysis, periodate oxidation, methylation, specific optical rotation, and 13C and 1H nuclear magnetic resonance studies, the structure of the O-chain was established as being a linear backbone of alternating 1,3-linked alpha-L-rhamnopyranosyl and beta-L-rhamnopyranosyl units, to which 2,2-linked beta-D-threo-pent-2-ulofuranoside (D-xylulofuranoside) units were present on every L-rhamnopyranosyl residue, as shown below. (Formula: see text)
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PMID:Structure of the lipopolysaccharide O-chain of Yersinia enterocolitica serotype O:5,27. 356 66

Avidity of IgM, IgG, and IgA class anti-Yersinia antibodies was compared in sera of 22 patients with yersiniosis and subsequent reactive arthritis versus sera of 22 patients without postinfection complications. An enzyme-linked immunosorbent assay was used for antibody determination. Less than 2 months after onset of the infection, the patients with arthritis had fewer high-avidity IgM antibodies against the bacterial lipopolysaccharide (P = 0.035) and more high-avidity IgA antibodies against bacterial cell extract (P = 0.039) than did the patients without arthritis. This difference increased with time.
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PMID:Avidity of anti-Yersinia antibodies in yersiniosis patients with and without Yersinia-triggered reactive arthritis. 367 63

Enteropathogenic Yersinia sp. releases plasmid-associated proteins of low molecular mass (26-67 kilodaltons) at 37 degrees C. In this study, the optimum conditions for the release of proteins were assessed and the released proteins (RPs) were analyzed for the manner of release, immunochemical characteristics, and the location of the genes necessary for their synthesis. Protein release was strongly enhanced when growth media were markedly depleted of calcium ions by precipitation with oxalate or chelation with EGTA [ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid]. RP yields were greatest when Yersinia spp. were in the exponential growth phase. The RPs appeared to be released from the Yersinia spp. by secretion rather than by pinching off of membrane vesicles, because the RPs did not sediment during high-speed centrifugation nor were they contaminated to any significant degree with lipopolysaccharide. Moreover, immunoblot analysis revealed only traces of protein species related to RPs within the outer membranes of plasmid-positive Yersinia spp. grown at 37 degrees C under calcium-restricted conditions. Immunoblot studies also showed that the RPs of Y. enterocolitica serotypes O:3, O:8, and O:9 and the RP of Y. pseudotuberculosis serotype I are highly cross-reactive. Finally, the immunoprecipitates of the products of minicells which harbor Yersinia plasmids were used to demonstrate that at least three proteins immunochemically related to the released fraction were plasmid encoded. These results suggest that at least three of the RPs may be related to or identical with previously described plasmid-encoded Yersinia outer membrane proteins.
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PMID:Immunochemical analysis of plasmid-encoded proteins released by enteropathogenic Yersinia sp. grown in calcium-deficient media. 377 Sep 52

The lipopolysaccharides of Salmonella urbana and Salmonella godesberg, which belong in group N (O:30) of the Kauffmann-White system, were shown by SDS-PAGE electrophoresis, glycose analysis, periodate oxidation, methylation, and 1H- and 13C-n.m.r. analyses to have identical O-chains composed of repeating, branched pentasaccharide units having the structure: [----4)-beta-D-Glcp-(1----3)-alpha-D-GalNAcp-(1----2)-alpha-D-P erNAcp-(1----3)-alpha-L-Fucp-(1----]n 4 increases 1 beta-D-Glcp. The serological cross-reactivity of S. urbana and S. godesberg with Brucella abortus and Yersinia enterocolitica (O:9) can now be related to the presence of a 1,2-glycosylated N-acyl derivative of 4-amino-4,6-dideoxy-alpha-D-mannopyranosyl residues in their respective lipopolysaccharide O-chains.
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PMID:The structure of the antigenic lipopolysaccharide O-chains produced by Salmonella urbana and Salmonella godesberg. 381 4

Cell-mediated immune responses in cattle infected with Brucella abortus Strain 544, cattle infected with Yersinia enterocolitica serotype 09 and non exposed cattle were studied by an in vitro whole-blood lymphocyte stimulation procedure. A soluble Brucella polypeptide containing some lipopolysaccharide prepared from Brucella abortus strain 99 was used as antigen while Concanavalin A was used as mitogen. Results were assayed for (6-3H) thymidine incorporation into deoxyribonucleic acid. All the cattle from which Brucella abortus was recovered developed very high lymphocyte transformation responses while cattle infected with Yersinia enterocolitica 09 and non exposed cattle did not develop high lymphocyte stimulation reactions. The animals infected with Yersinia enterocolitica 09 were strongly positive to the Rose Bengal, serum agglutination, Complement fixation and Coombs' antibovine globulin tests. One lactating cow infected with Yersinia enterocolitica 09 was positive to the Brucella milk ring test. It was concluded that the lymphocyte stimulation assay could be used to differentiate bovine brucellosis from yersiniosis.
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PMID:Differentiation of Brucella abortus and Yersinia enterocolitica serotype 09 infections: use of lymphocyte transformation test. 393 92

The chemical structure of the lipid A of lipopolysaccharide I and II from Yersinia pestis, strain EV 40, was studied. It consists of a (1 ---- 6), beta-linked D-glucosamine disaccharide which carries two phosphate groups; one phosphate is linked glycosidically with a glucosamine unit, the other one is linked to the non-reducing glucosamine. Various degradation methods combined with 31P nuclear magnetic resonance spectroscopy showed that the ester-bound phosphate group is linked to a 4-aminoarabinosyl residue and the glycosidically linked phosphate group is linked to a D-arabinofuranosyl residue in lipopolysaccharide II and to the phosphorylethanolamine in lipopolysaccharide I. The hydroxyl groups of the disaccharide are acylated by dodecanoic, hexadecenoic, 3-hydroxytetradecanoic and 3-dodecanoyloxytetradecanoic acids. The amino groups of the disaccharide carry 3-hydroxytetradecanoic and 3-dodecanoyloxytetradecanoic acids. In addition smaller amounts of 3-tetradecanoyloxyltetradecanoic and 3-hexadecanoyloxytetradecanoic acids are present in ester linkage.
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PMID:Lipopolysaccharides from Yersinia pestis. Studies on lipid A of lipopolysaccharides I and II. 402 40

Lipopolysaccharide prepared from cells of Yersinia (Pasteurella) pseudotuberculosis of serogroups I, II, III, IV, and V is known to contain the 3,6-dideoxyhexose (DDH) paratose, abequose, paratose, tyvelose, and ascarylose in its respective O-specific side chains. Lipopolysaccharides or lipid-free polysaccharides of all of the 10 known serogroups and subgroups were subjected to methylation analysis and determined as alditol acetates by gas-liquid chromatography and mass spectrometry. The results indicated that the O-specific side chains of nine serotypes are composed of oligosaccharide repeating units in the form of four alternative general structures in which a terminal DDH may vary. These structures are DDH [Formula: see text] 6-deoxy-d-manno-heptose [Formula: see text] d-galactose (serogroups IA, IIA, and IVB), DDH [Formula: see text] d-mannose [Formula: see text] l-fucose (serogroups IB and IIB), and two configurations similar to the latter except that the 4-position of l-fucose was either linked to the d-mannose residue (serogroups VA and VB) or to the DDH residue (serogroups III and IVA). In contrast, O-groups in lipopolysaccharide of the newly discovered serogroup VI contained the DDH colitose and 2-acetamido-2-deoxy-d-galactose. Accordingly, all five known types of DDH have now been detected in lipopolysaccharides of Y. pseudotuberculosis. The sugar 6-deoxy-d-manno-heptose, present in O-specific side chains of serogroups IA, IIA, and IVB, has not yet been reported to occur elsewhere in nature.
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PMID:Structure of O-specific side chains of lipopolysaccharides from Yersinia pseudotuberculosis. 481 91

An enzyme immunoassay, with phenol-water extracted lipopolysaccharide (LPS) from Brucella abortus as antigen, was used to detect the class-specific antibody response in sera from 173 patients with B. abortus, B. melitensis or B. suis infection. Sera from 30 patients with salmonellosis, yersiniosis or tularaemia and from 25 healthy individuals served as controls. The B. abortus LPS antigen permitted a safe diagnosis of acute and chronic brucellosis with high IgM and rising IgG titres in sera collected in the acute stage of the disease, and with elevated IgG titres only in the chronic stage. The B. abortus LPS antigen also permitted a specific diagnosis with the exception of the high titres estimated in sera from patients with Yersinia enterocolitica 09 infection. The problem with that well-known reciprocal cross-reactivity was overcome by using two additional antigens: Y. enterocolitica 09 native and periodate oxidized and borohydride reduced LPS preparations. In sera from patients with brucellosis high titres were estimated against all three antigens, whereas in sera from patients with yersiniosis caused by serotype 09 high titres were measurable only with the B. abortus and the Y. enterocolitica native LPS antigens. These data suggest that the B. abortus and Y. enterocolitica 09 LPS share one antigenic determinant resistant to periodate oxidation and borohydride reduction, and that in addition the Y. enterocolitica 09 LPS has a determinant which is sensitive to periodate oxidation and borohydride reduction.
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PMID:Enzyme immunoassay of the antibody response to Brucella and Yersinia enterocolitica 09 infections in humans. 617 1


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