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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The O-specific polysaccharide obtained from the lipopolysaccharide of Shigella dysenteriae type 1 (Shigella shiga) by mild acid hydrolysis followed by fractionation on Sephadex G-50 was found to be identical to that desribed by Morgan's group and was composed of L-rhamnose, D-galactose and N-acetyl-D-glycosamine in a ratio 2:1:1. On the basis of methylation analysis data the polysaccharide was proved to be a linear chain of monosaccharide residues in pyranose forms substituted at position 3, except for that of galactose substituted at position 2. Selective cleavage, based on the N-deacetylation reaction of the polymer, together with determination of linkage configurations by chromic anhydride oxidation showed that the O-specific polysaccharide is built up of repeating tetrasaccharide units whose proposed structure is given below -3)-alpha-L-Rhap (1-3)-alpha-L-Rhap(1-2)-alpha-D-Galp(1-3)-alphapD-GlcNAcp(1- where RHAP = rhamnopyranose, Galp = galactopyranose, and GlcNAcp = N-acetyl-glucosamine. The present findings confirmed the considerations of Heidelberger on the substitution patterns of L-rhamnose and D-galactose residues from the results of serological studies.
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PMID:Somatic antigens of shigella. Structural investigation on the O-specific polysaccharide chain of Shigella dysenteriae type 1 lipopolysaccharide. 0 14

The receptor of coliphage omega8 is the O-specific mannan of Escherichia coli O8 in which the trisaccharide alpha-mannosyl-1,2-alpha-mannosyl-1,2-mannose is joined through alpha-mannosyl-1,3-linkages. Coliphage omega8 produces an endo-alpha-1,3-mannosidase which destroys the receptor, liberating a series of oligosaccharides (repeating trisaccharide and multiples). The enzyme is an integral part of the phage particles and also occurs in a free form in the lysates. Phage particles hydrolyze alpha-1,3-mannosyl linkages in the lipopolysaccharide, the polysaccharide (mannan) moiety, and higher oligosaccharides with an efficiency decreasing in this order. No transmannosylation could be detected. Phage particles also degrade the receptor mannan on whole bacteria, as determined with 14C-labeled E. coli O8. The values of Km and Vmax were determined with omega8 particles and free enzymes using native lipopolysaccharide and its triethylammonium salt. The latter, which was obtained after electrodialysis, has a micellar weight of 2.5 X 10(5), whereas the native lipopolysaccharide forms supermicelles with micellar weights of several millions. With coliphage omega8 as enzyme and supermicellar lipopolysaccharide as substrate Km=5 X 10(-8) M was obtained. This, together with the fact that omega8 attaches irreversibly to E. coli O8, was used in proposing a hypothesis for the possible role of the enzyme in the first steps of infection with coliphage omega8.
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PMID:Enzymatic action of coliphage omega8 and its possible role in infection. 0 21

A method based on the inhibition of agglutination is described that may be used for the differential serological diagnosis between B. abortus and Y. enterocolitica serotype O:9. An antigen with high immunological capacity was isolated from Brucella. This antigen inhibited both homologous and heterologous agglutination by Brucella antiserum, but only the heterologous agglutination by Yersinia antiserum. It proved to be constitued of a polysaccharide (N-acetylglucosamine, glucose, mannose and 2-keto-3-deoxyoctonic acid), a protein and a phosphoglycerid moiety. Lipid A was absent from the Brucella antigen. Incomplete polysaccharide synthesis of the Brucella antigen, with concomitant loss of serological specificity by the rough mutant has been described. Oligosaccharides containing N-acetylgalactosamine, glucose and galactose were isolated from the specific side chain of Yersinia lipopolysaccharide. Lipid A constituents were also identified in the latter.
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PMID:Biochemical basis of the serological cross-reactions between Brucella abortus and Yersinia enterocolitica serotype O:9. 5 66

Rabbit antibodies to cell wall mannans of various microbial strains and their mutants were found to be cross-reactive to cell carbohydrates of mammalian sperm and 4-6-days-old blastocysts. Immunochemical studies indicate that oligomers of alpha1 yields to 2, alpha1 yields to 3, alpha1 yields to 6, and probably also alpha yields to 4 linked mannose residues of sperm carbohydrates are available for antibody binding. At least 80 percent of binding activity of a yeast mannan antibody to sperm can be effectively inhibited by specific haptens or digestion with exo-alpha-D-mannosidase, an enzyme activity highest in testicular tissue. In order to determine the role of this enzyme in the metabolism of the cross-reactive mannan antigens of sperm, the relative amount of a specific alpha-linked oligomannosyl determinant of bovine sperm from homozygous normals was compared to that of hetero-zygous carriers of alpha-mannosidase deficiency. Extensive cross-reactivity between the microbial and mammalian oligomannosyl determinants suggest that these are conserved structures in cell carbohydrates, although the organization of these units in the microbial cell wall lipopolysaccharide has very little similarity to the carbohydrate moieties of mammalian glycoproteins.
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PMID:Cell antigens recognized by rabbit antibodies specific for oligomannosyl determinants. 7 30

An extract made from the supernatant of Neisseria gonorrhoeae Gc2 strain 1291 degraded the Gc2 polysaccharide antigen. Chemical analysis of this polysaccharide indicated it contains glucose, galactose, glucosamine, galactosamine, glucosamine-6-phosphate, heptose, 2-keto-3-deoxyotonate, and ethanolamine and is the polysaccharide component of gonococcal lipopolysaccharide. Degradation of the polysaccharide by sonic extracts resulted either in complete loss of antigenicity and immunogenicity or in partial degradation to subunits that could inhibit the Gc2-specific hemagglutination inhibition. The factors responsible for degradation were destroyed by heating at 100 degrees C for 5 min or by Pronase digestion, but were unaffected by ribonuclease, deoxyribonuclease, Mg2+, Ca2+, or ethylenediaminetetraacetic acid. The process was pH dependent, with optimal activity occurring at pH 7. Sonic extract supernatants from group B and C meningococcal strains contained degrading properties, whereas similar extracts produced from Escherichia coli, Staphylococcus aureus, Klebsiella pneumoniae, and Streptococcus pneumoniae type II failed to degrade the Gc2 polysaccharide.
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PMID:Degradation of the polysaccharide component of gonococcal lipopolysaccharide by gonococcal and meningococcal sonic extracts. 7 94

The octasaccharide Galp (Formula: see text) Rhap, the synthesized disaccharides methyl 3-O-a-tyvelopyranosyl-a-D-mannopyranoside, methyl 3-O-a-tyvelopyranosyl-beta-D-mannopyranoside and methyl alpha-tyveloside, in order of decreasing effectiveness, inhibited the precipitation of S. typhi T2 alkali-treated lipopolysaccharide by O-factor 9 serum. On a molar basis the relative inhibiting activities of the glycosides were by O-factor 9 serum. On a molar basis the relative inhibiting activities of the glycosides were 100:22:8:2. With rabbit aniserum raised against 3-O-a-tyvelopyranosyl-D-mannopyranosyl covalently linked to bovine serum albumin the relative inhibitory activities of the four glycosides were 11:100:26:3. These data establish that the 3-O-a-tyvelopyranosyl-a-D-mannopyranosyl structure is immunodominant in the Salmonella O-antigen 9. The specificity of the antigen-antibody interaction was high: glycosides in which the tyvelose (3,6-dideoxy-D-arabino-hexose) residue had been replaced by abequose (3,6-dideoxy-D-xylo-hexose) or paratose (3,6-dideoxy-K-ribo-hexose), had less than one fiftieth of the activity of the most active inhibitor in either of the two precipitation systems used. Moreover, the results show that 3-O-a-tyvelopyranosyl-D-mannopyranosyl coupled to bovine serum albumin elicits O-antibodies of higher specificity than those obtained by absorption of antibacterial immune serum.
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PMID:Immunochemistry of Salmonella O-antigens. Specificity and cross-reactivity of factor O9 serum and of antibodies against tyvelose (Formula: see text) mannose coupled to bovine serum albumin. 8 96

Mineral acid hydrolysis of the lipopolysaccharide from Vibrio cholerae 569B (Inaba) gives an oligosaccharide fraction which was shown, by use of 13C NMR and chemical methods, to be a regular alpha-(1 leads to 2) linked chain of D-perosamine (4-amino-4,6-dideoxy-D-mannose) units. This chain represents the O-antigen of the lipopolysaccharide, in which the amino functions are acylated with 3-hydroxypropionyl groups. The chromatographic properties of some hydroxamic acids are described and used to characterize these acyl groups.
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PMID:The structure of the O-antigenic side chain of the lipopolysaccharide of Vibrio cholerae 569B (Inaba). 8 66

Lipid A isolated from lipopolysaccharide of Yersinia pseudotuberculosis was used for immunization of rabbits to afford antisera to lipid A with titers of 1:640 in the passive hemolysis test. Exhaustion of immune serume with sheep erythrocytes decreased antibody titers up to 1:160. Authentic samples of 2-(DL-3-hydroxytetradecanoyl)amino-2-deoxy-D-glucose 6-phosphate, 2-tetradecanoylamino-2-deoxy-D-glucose 6-phosphate and 2-acetamido-2-deoxy-D-glucose 6-phosphate have been synthesized in order to carry out a comparative study of inhibitory activity of these compounds and lipid A using a system of lipid A and antiserum to lipid A. As a result, the immunodominant moiety of the lipid A of Y. pseudotuberculosis proved to contain a D-glucosamine residue acylated with 3-hydroxytetradecanoic acid at the amino group. The nature of the fatty acid acylating the amino group of glucosamine does not play an important role in the structure of immunodominant moiety of lipid A.
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PMID:Structural studies on the immunodominant group of lipid A from lipopolysaccharide of Yersinia pseudotuberculosis. 8 32

A procedure is described for isolating a high-molecular-weight polysaccharide (PS) from the slime of Pseudomonas aeruginosa immunotype 1. The resultant material, obtained from the void volume of a Sephadex G-100 column, was composed of carbohydrate and water. No lipopolysaccharide (LPS), 2-keto-3-deoxyoctonoate, heptose, phosphate, or protein was detectable, and nucleic acid contamination was generally below 1%. The carbohydrate composition of the PS was glucose, rhamnose, galactose, arabinose, and mannose. PS had a molecular weight of between 100,000 and 350,000 and did not disaggregate when chromatographed in the presence of sodium deoxycholate. An antigen immunologically indistinguishable from PS could be obtained from LPS by either acetic acid hydrolysis and column chromatography or by allowing solutions of LPS to stand at room temperature for 3 days. Some of this LPS-associated polysaccharide eluted as the void volume of a G-100 column but differed from PS by its lack of galactose and arabinose. LPS also contained an immunodeterminant not shared with PS that was detected by its stability to dilute alkali treatment (0.1 N NaOH, 37 degrees C, 2 h). PS was destroyed by alkali treatment. PS appeared to represent a form of LPS polysaccharide side chain that contains galactose and arabinose and is of a high molecular weight.
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PMID:Isolation and characterization of a high-molecular-weight polysaccharide from the slime of Pseudomonas aeruginosa. 10 40

The presence of two distinct lipopolysaccharides in Yersinia enterocolitica O:9 is described: one isolated from the aqueous phase and one from the phenol phase (Westphal system). The sugar moiety of the phenol phase lipopolysaccharide has been identified as being responsible for the serologic cross-reaction of Y. enterocolitica O:9, Brucella abortus and Vibrio cholerae. The phenol phase antigen consists of glucose, galactose, glucosamine, 2-keto-3-deoxyoctonic acid, heptose, lipid A and a protein moiety. Haemagglutination experiments revealed two different structures: one that readily coats erythrocytes and another that requires alkali treatment. The former may be separated by repeated adsorptions on erythrocytes. Serologically, the two structures behave like a single antigen. The action of normal rabbit serum on the erythrocyte-containg capacity of the two structures was studied.
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PMID:Immunochemical studies on a Yersinia enterocolitica O:9 lipopolysaccharide cross-reacting with Brucella abortus and Vibrio cholerae extracts. 10 56


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