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

Three techniques for the measurement of bacterial numbers and biomass in the marine environment are described. Two are direct methods for counting bacteria. The first employs an epifluorescence microscope to view bacteria that have been concentrated on membrane filters and stained with acridine orange. The second uses a transmission electron microscope for observing replicas of bacteria that are concentrated on membrane filters. The other technique uses Limulus amebocyte lysate, an aqueous extract from the amebocytes of the horseshoe crab, Limulus polyphemus, to quantitate lipopolysaccharide (LPS) in seawater samples. The biomass of gram-negative (LPS containing) bacteria was shown to be related to the LPS content of the samples. A factor of 6.35 was determined for converting LPS to bacterial carbon.
 ...
PMID:Determination of bacterial number and biomass in the marine environment. 32 92

Phase I cells of Bordetella pertussis but not those of B. parapertussis, B. bronchiseptica or B. avium were agglutinated by Limulus polyphemus lectin. Most strains of B. pertussis but not those of the other species were also agglutinated by Helix pomatia lectin. In precipitation reactions between lectins and purified Bordetella lipopolysaccharide (LPS) preparations a similar pattern occurred. Lectin agglutination provides a rapid presumptive method for the differentiation of B. pertussis from B. parapertussis and other Bordetella species.
 ...
PMID:Agglutination of Bordetella species by lectins. 155 59

Direct virus inactivation of tachyplesin I and related isopeptides, which are antimicrobial peptides isolated from the hemocytes of the horseshoe crab (Tachypleus tridentatus and Limulus polyphemus), was examined against several viruses. Vesicular stomatitis virus (VSV) was inactivated by incubation with tachyplesin I and its isopeptides. Influenza A (H1N1) virus was slightly inactivated by tachyplesin I, whereas herpes simplex virus 1 and 2, adenovirus 1, reovirus 2 and poliovirus 1 were resistant to inactivation. The inactivation of VSV by tachyplesin I depended on the concentration, the time and the temperature of incubation. Pretreatment of tachyplesin I with trypsin or lipopolysaccharide of gram-negative bacteria entirely abolished the antiviral activity. Electron microscopy of VSV treated with tachyplesin I showed naked and damaged virions. These data suggest that tachyplesin I directly inactivates the VSV by destroying its envelope subunits.
 ...
PMID:Direct virus inactivation of tachyplesin I and its isopeptides from horseshoe crab hemocytes. 166 45

A simple physical-chemical method for estimating the lipopolysaccharide (LPS, i.e. endotoxin) content of meningococcal polysaccharide vaccines is described. The low molecular weight LPS was first separated from the high molecular weight polysaccharide by SDS-polyacrylamide gel electrophoresis. The LPS was then selectively visualized by a highly sensitive silver stain which can detect 5 ng of meningococcal LPS. The method can detect concentrations of LPS in meningococcal polysaccharides as low as 0.01%, and was used to measure semiquantitatively the LPS in bulk powders of meningococcal polysaccharides and in vaccines in final containers. The LPS in the bulk powders and in the vaccines was also assayed by the gelation of Limulus polyphemus ameobocyte lysate and the results of the two methods were in agreement.
 ...
PMID:The analysis of lipopolysaccharide (endotoxin) in meningococcal polysaccharide vaccines by silver staining following SDS-polyacrylamide gel electrophoresis. 242 Aug 3

Immunization of mice with a combination of passively administered syngeneic IgG (anti-p-azophenylarsonate [anti-Ars]) antibody and a soluble, multivalent form of the antibody's corresponding antigen (Limulus polyphemus hemocyanin conjugated with Ars [Lph-Ars]) resulted in specific autoanti-IgG Fc (rheumatoid factor) production. The response was rapid and only anti-IgG of the IgM isotype is found. Because immunization with either the IgG antibody or the antigen alone did not result in rheumatoid antibody production, immune complexes appear to be the active form of the immunogens. Antibody/antigen ratios that resulted in maximal anti-IgG antibody responses were the same as those required for peak in vitro immunoprecipitation, i.e., equivalence. Previous exposure of the mice to the exogenously supplied antigen was not required for the response. The response to immune complexes is specific because mice immunized with IgG2a-containing complexes produced autoanti-IgG2a, while mice immunized with IgG1-containing complexes produced anti-IgG1 with little reactivity to other IgG isotypes. IgG2a blocked in its complement-fixing capacity was more effective in eliciting the anti-IgG2a response than native IgG2a, suggesting a possible role for the complement system in modulating the anti-IgG2a response. Induction of rheumatoid factor production by immune complexes could be induced in xid mice but not in nu/nu mice, indicating T lymphocyte dependence of the response. In contrast, the B lymphocyte activator lipopolysaccharide was able to elicit vigorous rheumatoid factor production in both nu/nu and normal mice, demonstrating that nu/nu mice contain B cells capable of making the response. Rheumatoid antibody produced in the immune complex- or LPS-induced responses is Fc specific and has relatively low affinity for IgG that is not bound to antigen.
 ...
PMID:Immune complexes can trigger specific, T cell-dependent, autoanti-IgG antibody production in mice. 257 42

The complete amino acid sequence of anti-lipopolysaccharide (LPS) factor purified from the hemocytes lysate of the American horseshoe crab, Limulus polyphemus, was determined by characterization of the NH2-terminal sequence and the peptides generated after digestion of the protein with lysyl endopeptidase, clostripain, and Staphylococcus aureus V8 protease. Upon sequencing the peptides by the automated Edman method, the following primary structure was obtained: (Sequence: in text). During the sequence analysis, two species of the protein, which differed from each other at one locus, were found and characterized. L. polyphemus anti-LPS factor was a basic protein consisting of a single polypeptide chain of 101 residues and a calculated molecular weight of 11,786 or 11,800. The hydrophobic NH2-terminal sequence and the clustering of positive charges found in the disulfide loop yielded a typical amphipathic character of this protein. Moreover, L. polyphemus anti-LPS factor showed 83% sequence identity with the Tachypleus tridentatus protein, and the sequence similar to that observed in the EF-hand structure was found to contain in the COOH terminal portions of these proteins, although its function is unknown.
 ...
PMID:Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus. 366 49

Capsular structure and biochemical composition varied between two isolates (virulent and avirulent) of Haemophilus pleuropneumoniae serotype 5. The presence of capsule was determined by transmission electron microscopy with glutaraldehyde-osmium, ruthenium red, alcian blue, and phosphotungstic acid staining procedures. The virulent isolate of H. pleuropneumoniae had a distinct, adherent capsule. The avirulent isolate had a fragile, easily removed capsule. Capsular material (CM) and a lipopolysaccharide (LPS) were isolated from each bacterial isolate and were compared biochemically and biologically. CM from both isolates contained carbohydrates, no detectable protein, and no detectable to trace amounts of lipid A. Each LPS contained heptose, hexose, galactose, glucosamine, 2-keto-3-deoxyoctonate, and lipid A. Biological responses to CM and LPS from both isolates were demonstrated in the proclotting enzyme of Limulus polyphemus amebocyte lysate activation and in serological cross-reactions by immunofluorescence and immunodiffusion precipitation. The virulent isolate contained approximately 10 mg of LPS per g more on an original dry weight basis than the avirulent isolate. LPS from the virulent isolate contained approximately 13 times more galactose than LPS from the avirulent isolate. The differences of capsular structure and biochemical composition may contribute to the role of CM in porcine H. pleuropneumoniae infections.
 ...
PMID:Morphological and biochemical comparison of virulent and avirulent isolates of Haemophilus pleuropneumoniae serotype 5. 394 95

Hemolymph samples obtained from Limulus polyphemus at the time of collection and after a 1-week holding period exhibited a significant increase in bacterial levels. No differences were observed in the ability of amoebocyte lysate, prepared from these same samples, to gel in the presence of lipopolysaccharide.
 ...
PMID:Presence of microorganisms in hemolymph of the horseshoe crab Limulus polyphemus. 399 74

Exposure of limulus hemocytes to bacterial endotoxins (lipopolysaccharide, LPS) results in the activation of the intracellular clotting system, consisting of several protein components. During the separation of these components, a potent anticoagulant, named anti-LPS factor, which inhibits the endotoxin-mediated activation of the coagulation cascade, was found in hemocytes from both Tachypleus tridentatus and Limulus polyphemus (Tanaka, S., et al. (1982) Biochem. Biophys. Res. Commun. 105, 717-723). The principle isolated from the Tachypleus hemocyte lysate by column chromatographies on dextran sulfate-Sepharose CL-6B and Sephadex G-50 under sterile conditions was a simple basic protein with an apparent molecular weight of 15,000. It consisted of a single chain polypeptide containing a total of 128 amino acids. The COOH-terminal end was presumed to be histidine, but no NH2-terminal end reactive to phenylisothiocyanate was detected. The isolated anti-LPS factor specifically inhibited the endotoxin-mediated activation of factor C, which has recently been identified as an LPS-sensitive serine protease zymogen in the hemocytes. This inhibition appeared to be due to the binding of anti-LPS factor with LPS. Moreover, anti-LPS factor had an antibacterial effect on the growth of Gram-negative bacteria (Salmonella minnesota R595 and 1114W) but not on that of Gram-positive bacteria (Staphylococcus aureus 209P). These biological activities of the isolated anti-LPS factor suggest an important role in cellular defence of limulus against microbial invasion.
 ...
PMID:Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS). 403 Jul 41

Lysates obtained from amoebocytes of Limulus polyphemus, the horseshoe crab, showed gel formation after the addition of bacterial endotoxin. In contrast to living gram-negative bacteria, viable gram-positive microorganisms did not cause gelation of lysate. Nevertheless, peptidoglycan isolated from the cell walls of various gram-positive organisms did induce the reaction. However, the activity of peptidoglycan was 1,000 to 400,000 times less than that of Escherichia coli lipopolysaccharide. After exposure to lysozyme, peptidoglycan no longer gelled amoebocyte lysate, therefore apparently excluding endotoxin contamination. Gelation of amoebocyte lysate by endotoxin or peptidoglycan was inhibited by different concentrations of sodium polystyrolsulfonate. Whereas these studies confirm the specificity of the Limulus test for bacterial endotoxins, they also indicate that other substances of bacterial origin should be investigated for their ability to gel amoebocyte lysate.
 ...
PMID:Investigations on the specificity of the Limulus test for the detection of endotoxin. 461 71


1 2 3 4 Next >>