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)

An antigen (ZAB) common to Neisseria gonorrhoeae was prepared by stepwise elution of a crude gonococcal antigen (ZA) from columns of diethylaminoethyl cellulose employing 0.02 M phosphate buffers, pH 7.6, containing increasing concentrations of sodium chloride. Rats immunized with ZAB produced reaginic (IgE) antibody which cross-reacted with ZA prepared from eight gonococcal strains by the passive cutaneous anaphylaxis (PCA) test. Heating of the sera at 56 degrees C for 4 h destroyed the PCA activity. The PCA activity of the anti-ZAB rat serum was removed after absorption with ZAB antigen or with rabbit anti-rat IgE but not after absorption with gonococcal lipopolysaccharide or with heat-killed or formalinized gonococci. Treatment of ZAB with trypsin or heating at 100 degrees C for 30 min destroyed or reduced the antigenic activity respectively. Further purification of ZAB by filtration through Sephadex G-100 gave a preparation (ZAB2) which contained the common antigen as shown by the cross-reactivity of anti-ZAB2 rat serum with seven stains of N. gonorrhoeae. Fraction ZAB2 contained material which had a molecular weight less than 13,700 and was associated with the presence of material absorbing at 260 nm. The results of this study indicate that a low molecular weight antigen, which appears to be protein in nature and associated with nuclei acid, is common to the gonococcus and is the main antigenic component inducing reaginic (IgE) antibody in the rat.
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PMID:Induction of reaginic (IgE) gonococcal antibodies in the rat by a common antigen of Neisseria gonorrhoeae. 10 9

Mutants of Salmonella typhimurium with defects in the heptose region of the lipopolysaccharide (LPS) molecule (heptose-deficient, chemotype Re) leak periplasmic enzymes (acid phosphatase (EC 3.1.3.2), cyclic phosphodiesterase, ribonuclease I (EC 3.1.4.22), and phosphoglucose isomerase (EC 5.3.1.9) (PGI is at least partially periplasmic in E. coli and S. typhimurium; see below)) and do not leak an internal enzyme (glucose-6-phosphate dehydrogenase) into the growth medium. The extent of this leakage is markedly increased at higher temperature (42 degrees C). Leakage of periplasmic enzymes from the strains lacking units distal to heptose I in the LPS molecule (chemotype Rd2) occurs only at 42 degrees C, and not at 30 or 37 degrees C. The extent of leakage of these enzymes from smooth strain and mutants of other LPS chemotypes (Rc, Rd1) is not significant, and is not influenced by growth temperatures. The kinetics of leakage of periplasmic enzymes after shift to 42 degrees C in nutrient broth reveal an accelerated release into the medium from heptose-deficient strains of cyclic phosphodiesterase and ribonuclease I after 30 min at 42 degrees C, and phosphoglucose isomerase after 60 min at 42 degrees C; at 30 degrees C the rate of release of cyclic phosphodiesterase and ribonuclease I is relatively slower. After 60 min at 42 degrees C in nutrient broth, growth of these strains has either slowed down or stopped. In L-broth, which permits the growth of the heptose-deficient strain (SA1377) at 42 degrees C, leakage of cyclic phosphodiesterase and phosphoglucose isomerase occurs, whereas there is no detectable leakage of these enzymes from the isogenic smooth strain (SA1355). Thus, leakage of the periplasmic enzymes from the heptose-deficient strain occurs with or without growth. Mg2+ (0.75 mM), sodium chloride (50 mM), and sucrose (100 mM) in nutrient broth at 42 degrees C prevent the leakage of these enzymes. The shedding of LPS from the heptose-deficient as well as the smooth strains is enhanced by high temperature (42 degrees C), whereas considerable leakage of protein occurs only in the heptose-deficient strain at 42 degrees C and not in the smooth strain. The smooth and heptose-deficient strains are equally sensitive to osmotic shock although a significant proportion of acid phosphatase and cyclic phosphodiesterase activities from the heptose-deficient cells grown at 42 degrees C comes off in the Tris-NaCl wash step suggesting a rather loose attachment of these enzymes onto the cell surface.
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PMID:Leakage of periplasmic enzymes from lipopolysaccharide-defective mutants of Salmonella typhimurium. 18

The effect of 0.9% sodium chloride solution on the release of alkaline phosphatases from cells of four strains of Serratia marcescens was studied. Saline had a greater action in the releasability of the enzyme on cells of the polymyxin B sensitive strains than those of the polymyxin B resistant strains. SDS-polyacrylamide gel electrophoresis of the released materials showed the presence of proteins and lipopolysaccharide components of the outer membrane as well as enzyme activity in all four strains. Cells from strains harvested under higher temperatures contained more releasable activity in the salin wash fraction than those harvested under refrigerated condition. Active components with molecular weights of 190,000 and 110,000 daltons were either absent or present to a lesser degree in the extracts released by the polymyxin B treatment of the washed cells. However, active components not released by saline were found in the polymyxin B extracts. Contrary to other reports, results of this study clearly showed the ubiquitous nature of alkaline phosphatase in S. marcescens. It appears that their releasability is related to the polymyxin B susceptibility as well as the instability of the outer membrane of the cell envelope.
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PMID:Effect of saline on the releasability of alkaline phosphatase from cells of Serratia marcescens. 18 60

The natural occurrence of cations Fe, Zn, Mg, and Ca in the lipopolysaccharide (LPS) of both the S and R forms of Shigella dysenteriae 1 was studied. LPS preparations were obtained either by phenol-water extraction (according to the method of Westphal et al., Z. Naturforsch. 7b:148-155, 1952) or by extraction of cells with hypertonic sodium chloride-sodium citrate (according to the method of Raynaud and Digeon, C. R. Acad. Sci. (Paris) 229:564-566, 1949), with subsequent chromatographic purification on Sephadex G200 and Sepharose 4B columns. The cation in highest concentration in the Westphal extract was Mg(2+) (as much as 30 mug/mg), and the lowest one was Fe (ca. 0.10 mug/mg). In LPS of the Raynaud type, the cation in highest concentration was Ca(2+) (as much as 13 mug/mg), and the lowest one was Fe (ca. 0.10 mug/mg). The effects of increasing and decreasing the concentrations of cations (Fe, Zn, Mg, Ca) upon the biological activity of the endotoxins was evaluated by using toxicity in mice and the Limulus test. It appeared that increased concentrations of Fe (chiefly of Fe(3+)) decreased the toxicity of the R form of LPS, whereas Mg(2+) decreased the toxicity of the S form. After prolonged dialysis of LPS preparations against deionized water, there was no consistent relationship between toxicity as determined in white mice and with the Limulus test.
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PMID:Effects of certain cations (Fe, Zn, Mg, and Ca) on bacterial endotoxins. 35 92

Different antigens of Pasteurella multocida Carter's type 6:B including whole bacterium, antigen heated at 56 degrees C, antigen heated at 100 degrees C, sonicated antigen, capsular antigen, potassium thiocyanate extract, lipopolysaccharide and sodium salicylate extract were evaluated to assess protection in buffalo calves against haemorrhagic septicaemia. Sera from calves with known protection status in experimental challenge were titrated by enzyme-linked immunosorbent assay (ELISA) against all antigens. Capsular antigen extracted with 2.5% sodium chloride was superior to other antigens for assessing protection status of buffalo calves against P. multocida by ELISA. This capsular antigen was able to differentiate clearly between well-protected, protected and unprotected animals.
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PMID:Serological evaluation of Pasteurella multocida antigens associated with protection in buffalo calves. 147 36

Corncobs, which are distinct morphological units formed by the ordered coaggregation of a filamentous microorganism and streptococci, can be made in vitro by using oral strains of Fusobacterium nucleatum and Streptococcus sanguis. Previous studies have shown that strains of F. nucleatum contain one of at least two different types of corncob receptor. The objective of this study was to isolate the receptor from F. nucleatum ATCC 10953 as the first step in the elucidation of the molecular basis of corncob formation. The cell envelope fraction from this bacterium was treated with trypsin, delipidated with chloroform-methanol, and subjected to ion-exchange chromatography. A single polypeptide (apparent Mr, 39,500), which was eluted from the column with 0.5 M sodium chloride and extracted with dodecyltrimethylammonium bromide to remove contaminating lipopolysaccharide, inhibited corncob formation between strain ATCC 10953 and S. sanguis CC5A. Similarly derived cell fractions from either F. nucleatum FDC 364 or Fusobacterium necrophorum failed to effect coaggregation in the inhibition assay. Amino acid analysis of the polypeptide showed a moderately hydrophobic character (polarity index, 41) and 11% basic residues. Antiserum made against the purified polypeptide agglutinated F. nucleatum ATCC 10953, neutralized the ability of this bacterium to form corncobs, and agglutinated whole cells of S. sanguis CC5A that were precoated with the receptor polypeptide. The identification and isolation of this receptor should greatly enhance our ability to define some of the complex intergeneric coaggregation mechanisms that are thought to occur in the human oral cavity.
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PMID:Isolation of a corncob (coaggregation) receptor polypeptide from Fusobacterium nucleatum. 291 93

Various buffers (0.2 M acetate, pH 4.2; 0.01 M phosphate with 0.15 M sodium chloride, pH 7.2; 0.15 M borate, pH 8.2 and 0.025 M carbonate, pH 9.6) were used as coating buffers with Brucella abortus alkali treated lipopolysaccharide on two types of plastic matrices. Maximum binding occurred using the phosphate buffer. However, as was the case with the other buffers 50 per cent or more of the antigen was removed by five washing procedures. B abortus S19 or S2308, suspended in ammonium acetate-carbonate buffer, pH 8.2, was shown to bind maximally when 10(9) cells were dried onto the plastics. Less than 20 per cent of the cells were removed by five washings.
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PMID:Binding of Brucella abortus whole cell and lipopolysaccharide antigens to plastics. 640 79

Two S-form-revertant strains were isolated from a S. typhimurium Rd1 culture on account of their phage resistance. In microbiological and serological (O-agglutination) characterization - as well as in stability tests (agglutination in auramin and saline and heating at 100 degrees C) - the behaviour of the two strains was the same as that of the wild type. The two strains were found to be indistinguishable from the wild type strain also with respect to the chemical composition of their lipopolysaccharides. Thus the amount and proportion of fatty acids and sugar residues as well as the number of repeating units in the O-chain were all identical. In contrast, the isolated revertants were similar to the Rd1 mutant with respect to their auxotrophic markers methionine and tryptophane, to the absence of flagella as well as to the reduced content of cyclopropane fatty acids (C17, C19). Protein analysis revealed no significant qualitative or quantitative differences between the wild type strain and the two revertants with respect to the major proteins of their outer membranes. The sensitivity of the revertants to crystal violet, erythromycin and rifamycin SV was intermediate between the wild type and the Rd1 mutant. Their temperature maximum in nutrient broth was 43 degrees C, the retardation in growth at this temperature corresponding to that of the Rd1 mutant. At 37 degrees C, however, the growth rate of the revertants was identical to that of the wild-type, while that of the Rd1 mutant was slower. Addition of sodium chloride to the growth medium rendered the temperature dependent behaviour of the mutants and revertants similar to that of the wild type. Studies in NMRI mice revealed that the revertants, also with regard to their virulence, occupy an intermediate position between the mutant and the wild type. Nevertheless their ability to afford protection to Salmonella typhimurium infection following active immunization with acetone killed cells was as high as that of the wild type. The results show that the biologic behaviour of S. typhimurium is determined by the type of lipopolysaccharide it contains but also to a large extent by other cell-wall constituents.
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PMID:[Chemical and biological properties of revertants derived from a Salmonella typhimurium Rd1-mutant (author's transl)]. 700 6

Macrophage-enriched peritoneal exudate cells from mice infected with Mycobacterium bovis BCG, macrophage-like tumor cells (PU 5-1.8), and peritoneal macrophages propagated in vitro with macrophage growth factor released tumoricidal activity into the culture medium within 2 to 3 h after stimulation with nanogram quantities of bacterial lipopolysaccharide. The cytotoxic activities from each of the macrophage culture supernatants eluted from diethylaminoethyl-Sephacel columns at a sodium chloride concentration of 200 mM exhibited a molecular weight of 50,000 to 60,000 as estimated by gel filtration, were stable at 56 degrees C for 30 min, and were active at a pH range of 6 to 10. A rabbit antiserum directed against serum-derived cytotoxic activity (tumor-necrotizing factor) from BCG-infected and lipopolysaccharide-challenged mice inhibited all of the cytotoxic activities generated in vitro. This suggests that the macrophage-derived cytotoxins are identical with serum-derived cytotoxic factor, which further implies that the macrophage is the cellular source of tumor-necrotizing factor.
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PMID:Macrophages as a source of tumoricidal activity (tumor-necrotizing factor). 700 1

The lipopolysaccharide of Acinetobacter calcoaceticus NCTC 10305 (London) was obtained by a modified phenol/chloroform/light petroleum method from the bacterial cells and from the culture medium in yields of 1.6% and 2.2% respectively (based on the bacterial dry weight). On chemical analysis, both preparations proved to be identical. The lipopolysaccharide obtained from the cells was purified by repeated ultracentrifugation, electrodialysis, and precipitation with sodium chloride. It was free of nucleic acids, proteins, and glycans. In the analytical ultracentrifuge, the triethylamine and sodium salt forms of the lipopolysaccharide showed a s20 value of 8.9 S and 51 S, respectively. The lipopolysaccharide consisted of glucosamine, 3-deoxy-D-manno-octulosonic acid, D-glucose, fatty acids, and phosphate in a molar ratio of 2:1:7:6:4. The fatty acids were predominantly lauric acid, 2-hydroxy, and 3-hydroxylauric acid in a molar ratio of 1:1:2. Only 3-hydroxylauric acid was found in amide linkage. On mild acid hydrolysis of the lipopolysaccharide, 65% lipid A were obtained, to which glucosamine was retained quantitatively. It still contained 50% of the original glucose, while one third (15%) of the liberated glucose was in monomeric form.
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PMID:Isolation, purification, and chemical analysis of the lipopolysaccharide and lipid A of Acinetobacter calcoaceticus NCTC 10305. 706 May 73


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