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

The immunoglobulin M (IgM) and the IgG1, IgG2ab, and IgG3 subclasses of plaque-forming cells (PFC) specific for lipopolysaccharide (LPS) were measured after immunization of mice with LPS alone and compared with the responses to LPS in combination with nonbacterial proteins and with bacterial membrane phospholipid vesicles or two major outer membrane proteins from Proteus mirabilis. The relative numbers of IgG PFC belonging to the IgG1, IgG2, or IgG3 subclasses induced by immunization with LPS alone depended upon the type of LPS administered. Phospholipids and the proteins effected characteristic alterations in not only the strength but also the subclass of the IgG responses to LPS. The results suggest that the hydrophobic-hydrophilic nature or state of aggregation of the preparations plays a role in the induction of IgG1 and IgG2 subclasses of PFC specific for LPS. Complex formation with LPS and adjuvant was apparently necessary to obtain these effects.
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PMID:Alteration of the immunoglobulin G subclass responses in mice to lipopolysaccharide: effects of nonbacterial proteins and bacterial membrane phospholipids or outer membrane proteins of Proteus mirabilis. 618 89

The chemical structure of the lipid A component from the lipopolysaccharide of a Proteus mirabilis Re-mutant (strain R45) was analysed. It consists of a beta(1-6)-linked D-glucosamine disaccharide which carries two phosphate groups, one being ester-linked to position 4' of the nonreducing glucosaminyl residue and the other being bound to the glycosidic hydroxyl group of the reducing glucosaminyl residue. The ester-bound phosphate group is quantitatively substituted by a 4-amino-4-deoxy-L-arabinopyranosyl residue, the glycosidic phosphoryl group appears to be unsubstituted. Two available hydroxyl groups of the disaccharadide (probably at positions 3 and 3') are acylated by approximately 1 mol each of (R)-3-tetradecanoyloxytetradecanoic and (R)-3-hydroxytetradecanoic acid/mol. The amino group of the nonreducing glucosaminyl residue carries (R)-3-tetradecanoyloxytetradecanoic and that of the reducing residue (R)-3-hydroxytetradecanoic acid. In addition smaller amounts of (R)-3-hexadecanoyloxytetradecanoic acid are present in amide linkage. The attachment site of the oligosaccharide portion to lipid A was also investigated. It was found that the hydroxyl group at position 6' of the nonreducing glucosaminyl residue carries 3-deoxy-D-manno-octulosonic acid. This indicates that the saccharide portion in this Proteus lipopolysaccharide is linked to lipid A via the primary hydroxyl group in position 6'.
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PMID:Chemical structure of the lipid A component of the lipopolysaccharide from a Proteus mirabilis Re-mutant. 636 Jun 83

The determinant responsible for the ability of Bacteroides spp. to inhibit polymorph phagocytic killing of aerobic organisms has not yet been identified. Therefore, the roles of lipopolysaccharide and capsular polysaccharide of B. fragilis were investigated. Serum-resistant and serum-sensitive strains of Proteus mirabilis were used to indicate inhibition of phagocytic killing and serum killing of aerobes. Whole organisms of B. fragilis, purified lipopolysaccharide and capsular polysaccharide were added to an in-vitro phagocytosis system. Results showed that greater than 10(7) bacteroides/ml inhibited both serum and phagocytic killing. Concentrations below 10(7)/ml had little effect on either process. Purified capsular polysaccharide (10 or 100 micrograms/ml), either alone in the system or in combination with sub-inhibitory concentrations of B. fragilis also markedly inhibited serum and phagocytic killing. Lipopolysaccharide (9 micrograms/ml) appeared relatively inert. B. ovatus, reputedly non-capsulated, produced identical results to those obtained with B. fragilis, but an encapsulated strain of Streptococcus pneumoniae did not inhibit serum or phagocytic killing.
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PMID:The effect of capsular polysaccharide and lipopolysaccharide of Bacteroides fragilis on polymorph function and serum killing. 637 50

Western Blotting of whole cell preparations of three strains of Proteus mirabilis after separation by electrophoresis on SDS-polyacrylamide gels revealed a complex pattern of antigens. Similar antigen profiles were obtained with isolated outer membranes indicating that the majority of cell surface antigens are located in the outer membrane. Major outer membrane proteins were strongly antigenic and cross-reactive. The highly immunogenic flagella were detected in whole cell preparations and visible in isolated outer membranes. Whereas the protein and flagellar antigens were cross-reactive, lipopolysaccharide (LPS) could only be detected as immunoreactive material using homologous antisera for each strain. The LPS appeared as two broad bands (high and low Mr, respectively) in immunoblots of whole cells, isolated outer membranes and purified LPS. However, isolated LPS could be resolved into multiple sharp bands when 4 M urea was included in the gel system. These discrete bands are assumed to represent differing O antigen chain lengths of the LPS as reported for other Gram-negative organisms.
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PMID:Surface antigens of Proteus mirabilis revealed by electroblotting from sodium dodecyl sulphate-polyacrylamide gels. 637 19

Live bacterial suspensions, original as well as concentrated filtrates of Proteus mirabilis cultures caused positive reaction in the rapid skin test (vascular permeability reaction) and also in the delayed test (combination of haemorrhagic reaction, dilatation of vessels and induration) as well as in the test of mice-foot edema. The test on suckling mice did not prove the presence of thermostable enterotoxin. After separating the concentrated culture filtrates the biologic activity appeared in fraction 1 (relative molecular mass over 100 000) concerning the delayed skin test and in the fraction 2 (relative molecular mass approx. 40 000) in the rapid skin test. The activity localized in the fraction 1 can be ascribed to a lipopolysaccharide. The fraction 2 with an expressed activity in the rapid skin test showed also cytotoxic and proteolytic activity. In both fractions the presence of active antigen substances with different mobility and different antigen specificity was demonstrated.
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PMID:Toxinogenic potential of Proteus mirabilis strains. 643 15

Two murine monoclonal antibodies of the IgG3 class have been isolated after immunization with Brucella abortus. An indirect immunofluorescence test was used to screen hybridoma supernatants and subsequently to determine the cross-reactivity of the monoclonal antibodies with other bacteria. One monoclonal antibody reacted with all the smooth Brucella biotypes tried and with Yersinia enterocolitica serogroup 0:9, though not with rough Br. ovis or with strains of Escherichia, Proteus, Salmonella, Pseudomonas, Francisella and Bordetella. The other monoclonal antibody displayed a high degree of specificity for brucellae carrying the A lipopolysaccharide-protein surface antigen. The implications for the diagnosis of brucellosis are discussed.
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PMID:A monoclonal antibody specific for the A antigen of Brucella spp. 643 72

After mild acid hydrolysis, a disaccharide of 3-deoxy-D-manno-octulosonic acid (dOclA) was obtained from Re-mutant lipopolysaccharide of Salmonella minnesota, Salmonella godesberg, Proteus mirabilis, and Escherichia coli, and from the lipopolysaccharide of an S. minnesota Rb2 mutant. Combined gas-liquid chromatography/mass spectrometry of the reduced and permethylated derivatives indicated that the disaccharide is interlinked by a 2----4-glycosidic bond in all lipopolysaccharides tested. In addition, it was shown by gas-liquid chromatography of appropriate synthetic standards and a previously characterized alpha 2----4-linked dOclA disaccharide (derived from lipopolysaccharide of S. godesberg) that the non-reducing dOclA residue possesses the alpha configuration. In the case of lipopolysaccharide of S. minnesota Rb2 mutant, this result, together with earlier findings, suggests that it contains a linear dOclA trisaccharide of the sequence dOclA(alpha 2-4)dOclA. The results show that a dOclA(alpha 2-4)dOclA disaccharide represents a common architectural principle in enterobacterial lipopolysaccharides.
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PMID:Alpha-2----4-interlinked 3-deoxy-D-manno-octulosonic acid disaccharide. A common constituent of enterobacterial lipopolysaccharides. 654 5

Two lipopolysaccharides (LPS) were obtained by phenol-water procedure from Proteus mirabilis O27 strain -- LPS I as sediment and LPS II from the supernatant after ultracentrifugation. There was shown a distinct predominance of the O-specific material in LPSII, whereas in LPS I the core material prevailed. Heterogeneity of the P. mirabilis.O27 lipopolysaccharide was confirmed by the sodium dodecyl sulphate-polyacrylamide gel electrophoresis, in crossed immunoelectrophoresis and by the column chromatography.
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PMID:Heterogeneity of the lipopolysaccharide from Proteus mirabilis O27. 675 Dec 82

Antisera were raised against the purified Escherichia coli K12 outer membrane proteins ompA-, ompC- and ompF proteins and protein e. Several immunological methods were used to investigate the specificity of the antisera and the immunological relationship between the major outer membrane proteins. Although the antisera had been raised against highly purified proteins, several of them contained activity against lipopolysaccharide and lipoprotein due to minor impurities in the immunogens. The three general porins ompF protein, ompC protein and protein e were shown to be cross-reactive. Anti-(ompA protein) serum only reacted with the homologous protein. None of these antisera reacted with the phage lambda receptor protein or with protein III. Pore protein preparations isolated from Salmonella typhimurium, Klebsiella aerogenes, Enterobacter cloaceae and Proteus mirabilis were found to be structurally related to the E. coli K12 porins as they reacted with the antisera raised against E. coli K12 porins.
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PMID:Antigenic relationships between pore proteins of Escherichia coli K12. 700 46

Membranes of the stable protoplast L-form of Proteus mirabilis strain VI were highly immunogenic carriers of lipopolysaccharide when compared with the immune responses to lipopolysaccharide contained in cell walls of the bacterial form of this organism.
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PMID:Comparison of quantitative and qualitative antibody-producing cell responses to lipopolysaccharide in cell walls of the bacterial form and in membranes of the protoplast L-form of Proteus mirabilis. 700 96


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