Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Pivot Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Target Concepts:
Gene/Protein
Disease
Symptom
Drug
Enzyme
Compound
Query: UNIPROT:P43026 (
lipopolysaccharide
)
62,215
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
The pyrogenic activity of
lipopolysaccharide
(
LPS
) obtained from
Yersinia
enterocolitica was neutralized by the homologous O-antiserum at the optimal antigen/antibody ratio. The level of neutralization in either antigen excess or extreme antibody excess was significantly lower than that at the optimal ratio. These facts suggested that the structure of the so-called "lattice" of
LPS
/antibody complex might influence the neutralization of pyrogenic activity. Moreover, when
LPS
was gradually added to the antiserum to reach the optimal antigen/antibody ratio, the pyrogenic activity of
LPS
was only slightly neutralized by the antibody. The similar event to Danysz phenomenon that has been known in the diphtheria toxin-antitoxin system was also observed in the
LPS
-anti-
LPS
system.
...
PMID:Effects of homologous O-antibody on host responses to lipopolysaccharide from Yersinia enterocolitica: neutralization of its pyrogenicity. 72 51
The chemical properties and the general biological activities of
lipopolysaccharide
(
LPS
) and Boivin-type endotoxin obtained respectively by phenol-water and trichloroacetic acid extraction from
Yersinia
enterocolitica serotypes O3 and O9 were studied. The yield of
LPS
from the O9 strain was about 10% of the O3 strain possibly because of the lower solubility of O9-
LPS
in aqueous phase. However, the chemical composition of O9-
LPS
was similar to that of O3-
LPS
in the proportions of reducing sugar, glucosamine, heptose, KDO, and lipid A. In pyrogenicity and local Shwartzman reactivity in rabbits and lethality for mice, there was also no difference between O3 and O9-
LPS
. The anthrone-positive carbohydrate and lipid A contents of Boivin-type endotoxin from O3 were higher than those of the endotoxin from O9. The biological activities of Boivin-type endotoxin from O3 were also remarkably higher than those of the endotoxin from O9. It seems that endotoxin of Y. enterocolitica serotype O3 may play an important role in infection by this organism.
...
PMID:Biological activities of endotoxins from Yersinia enterocolitica. 97 37
A monoclonal antibody (3D6) was produced which reacted only with Brucella sonicated cell extracts that had been lysozyme-treated after sonication. The monoclonal antibody (mAb) reacted with the three major outer-membrane proteins (OMPs) of B. melitensis B115 in Western blots. A large number of reactive bands ranging from 12 to 43 kDa were present in lysozyme-treated Escherichia coli and
Yersinia
enterocolitica sonicated cell extracts. In a latex agglutination inhibition immunoassay, mAb 3D6 showed better reactivity with purified peptidoglycan (PG) of B. melitensis B115 than with that of Escherichia coli. This mAb was also used in immunogold electron microscopy with whole Brucella cells and sections. No binding was observed on whole cells and immunogold labelling in sections was observed close to the outer membrane, in the periplasmic space and in the cytoplasm. These findings indicate that mAb 3D6 is specific for PG subunits. Immunoblot analysis of B. melitensis B115 rough sonicated cell extracts after SDS-PAGE, with or without lysozyme treatment, was performed using mAbs specific for Brucella OMPs of molecular masses of 10, 16.5, 19, 25-27, 31-34, 36-38 and 89 kDa, for PG and for rough
lipopolysaccharide
(R-LPS) and smooth
lipopolysaccharide
(S-LPS). mAbs specific for the 25-27, 31-34 and 36-38 kDa OMPs reacted with three to six bands. All of them except the band of lowest molecular mass reacted with the PG-specific mAb and not with R-LPS- and S-LPS-specific mAbs.(ABSTRACT TRUNCATED AT 250 WORDS)
...
PMID:Demonstration of peptidoglycan-associated Brucella outer-membrane proteins by use of monoclonal antibodies. 138 Sep 79
The murine monoclonal IgM antibody E5 has been shown to significantly reduce the mortality and morbidity of patients with Gram-negative sepsis in a multicenter randomized placebo-controlled clinical trial. The in vitro binding characteristics of monoclonal antibody (mAb) E5 were studied using highly purified smooth
lipopolysaccharide
(
LPS
) isolated from a variety of clinically relevant, wild-type Gram-negative bacteria. Using a sensitive antibody-capture assay which involves immobilized mAb E5 and a chromogenic Limulus amebocyte lysate (LAL)
LPS
-detection system, mAb E5 was shown to bind to all 15 smooth
LPS
preparations tested, including
LPS
isolated from Escherichia, Klebsiella, Proteus, Pseudomonas, Salmonella, Serratia and
Yersinia
species. When
LPS
was fractionated according to size by size-exclusion chromatography, mAb E5 was shown to bind to smooth
LPS
molecules that have long as well as short O-polysaccharide chains. These results confirm and extend those reported previously and demonstrate that the anti-lipid A mAb E5 binds specifically to a diverse spectrum of smooth
LPS
isolated from wild-type Gram-negative bacteria.
...
PMID:Reactivity of monoclonal antibody E5 with endotoxin. II. Binding to short- and long-chain smooth lipopolysaccharides. 138 82
Sera from ten patients with positive brucella serology were used to investigate antibody cross-reactions between the O-antigens of Escherichia coli O157 and
Yersinia
enterocolitica O9. SDS-PAGE profiles of
lipopolysaccharide
(
LPS
), purified from strains of E. coli O157 and Y. enterocolitica O9, were reacted with sera by immunoblotting. All ten sera contained antibodies which bound to the
LPS
of E. coli O157, and five of these sera also contained antibodies which bound to the
LPS
of Y. enterocolitica O9. Absorption studies using these five cross-reacting sera indicated the existence of at least three epitopes exposed on the O-antigens of E. coli O157 and Y. enterocolitica O9. One antigen binding site appeared to be exposed on the
LPS
of both organisms, while one epitope was exposed on the
LPS
of E. coli O157 only, and another on the
LPS
of Y. enterocolitica O9 only.
...
PMID:The serological relationship between Escherichia coli O157 and Yersinia enterocolitica O9 using sera from patients with brucellosis. 154 43
This thesis is based on 8 publications and a review of the literature. The aim was to summarize present knowledge on molecular components of
Yersinia
enterocolitica involved in (i) adhesion, with special reference to plasmid encoded factors and (ii) induction of antibodies in the host, and the quantitation of these two phenomena. Adhesion of Y. enterocolitica was quantitatively studied by methods that measured binding to cultured epithelial cells, mucosal constituents immobilized on polystyrene, intestinal tissue, and nonbiological solid surfaces. The chromosomal inv and ail gene products have been shown by others to be independently able to mediate adhesion to and invasion of cultured epithelial cells. However, the
Yersinia
virulence plasmid, pYV, also encodes for at least one product that may mediate adhesion. It was shown that pYV carrying Y. enterocolitica strains adhered more efficiently than their isogenic pYV cured derivatives to rabbit and human ileal intestinal tissue and to rabbit ileal brush border membrane vesicles (BBVs). Using Y. enterocolitica mutants that were defective for production of the pYV encoded outer membrane protein, YadA, and Escherichia coli strains carrying the cloned yadA gene it was verified that YadA was responsible for the pYV encoded adhesion. The YadA promoted adhesion was found likely to be non-specific and, at least in part, mediated by hydrophobic interaction. YadA, however, also mediated binding to one or more constituents present in intestinal mucus. Such binding led to decreased ability to penetrate a layer of mucus in vitro and subsequent decreased ability to adhere to BBVs. Based upon these results, it remains uncertain whether Y. enterocolitica is able to benefit from the YadA mediated adhesion in the intestinal millieu. In vivo results have suggested that expression of YadA confers on Y. enterocolitica an increased ability to colonize the intestine, but no definitive conclusions have been reached so far. A large number of antigens were identified in Y. enterocolitica by means of crossed immunoelectrophoresis (XIE). Quantitation of serological cross-reactions between chromosome-encoded Y. enterocolitica antigens and antigens from other bacterial species was performed by means of XIE and proved useful for taxonomic purposes. Using XIE it was shown that infection with Y. enterocolitica induced an antibody response against a wide range of antigens. Tube agglutination, enzyme linked immunosorbent assays (ELISAs) using purified
lipopolysaccharide
(
LPS
) or formalin-killed whole pYV carrying cells as antigens, and XIE were evaluated for their applicability to detect recent Y. enterocolitica O:3 infection.(ABSTRACT TRUNCATED AT 400 WORDS)
...
PMID:Interactions between Yersinia enterocolitica and the host with special reference to virulence plasmid encoded adhesion and humoral immunity. 161 21
Enzyme-linked immunosorbent assays (ELISA) were developed for direct measurement of protein HC-IgA complexes (HC-IgA) in serum with antibody specificity for rabbit IgG (rheumatoid factor (RF) activity),
lipopolysaccharide
from
Yersinia
enterocolitica serotype O:3 (Y3) and tetanus toxoid (TT). About 80% of patients with rheumatoid arthritis had increased concentrations of HC-IgA-RF. The values were correlated with the concentrations of IgA-RF and IgM-RF. HC-IgA anti-Y3 was measured in 45 sera with anti-Y3 antibodies of IgM, IgG and IgA class. The HC-IgA anti-Y3 levels were correlated with those of anti-Y3 of IgG and IgM class, but not of IgA class. For HC-IgA anti-Y3, the closest correlation was that with the specific IgM antibody concentration, rs = 0.63 (p less than 0.001). In 25 normal sera, significant correlations were observed between HC-IgA anti-TT and specific antibodies of IgG and IgA class, but not of IgM class. In 107 sera containing IgA M-components, the total concentration of HC-IgA correlated poorly with both protein HC and with IgA concentrations. It was concluded that specific HC-IgA antibodies are normal constituents of serum, and that their concentrations are not directly related to the serum content of specific IgA antibodies.
...
PMID:HC-IgA antibodies of different specificities are normally present in serum: quantitation by ELISA and relationship to the major Ig classes. 169 May 57
Mild acid hydrolysis of the
lipopolysaccharide
from
Yersinia
kristensenii strain 103 (0:12.26) afforded teichoic acid-like polysaccharide. From the results of methylation, dephosphorylation, partial Smyth degradation, and 13C and 31P NMR data the structure of the repeating unit of the polysaccharide was deduced as follows: [formula: see text] The structure was confirmed by complete interpretation of polysaccharide 13C NMR spectrum.
...
PMID:[The structure of a repetitive unit of the glycerolphosphate- containing O-specific polysaccharide chain from Yersinia kristensenii strain 103 (0:12,26) lipopolysaccharide]. 169 78
O-specific polysaccharide has been isolated on mild hydrolysis of
lipopolysaccharide
from
Yersinia
aldovae and shown to consist of 2-acetamido-2-deoxy-D-glucose, D-glucose, 2-acetamido-2-deoxy-D-galactose, and 3,6-dideoxy-3- [(R)-3-hydroxybutyramido]-D-galactose in molar ratio 2:2:1:1. Acid hydrolysis, methylation, solvolysis with anhydrous hydrogen fluoride, 1H and 13C NMR studies indicated the polysaccharide to be composed of hexasaccharide repeating units of the following structure: [formula see text].
...
PMID:[Structure of the O-specific polysaccharide chain of Yersinia aldovae lipopolysaccharide]. 177 68
Protection against the intravenous lethal effect of
Yersinia
enterocolitica serovar O:3 for mice can be achieved by oral immunization with bacteria expressing the O:3
lipopolysaccharide
(
LPS
). Under similar experimental conditions, Ca(2+)-dependent cells are more protective than their Ca(2+)-independent counterparts, live vaccines are more efficacious than killed ones, and parenteral immunization is more efficient than the oral route. Antibodies induced by enzyme-treated
LPS
from an O:3 strain are able to mediate protection against challenge with one homologous strain, but they do not prevent induction of arthritis.
...
PMID:Protection against the lethal effect and arthritogenic capacity of Yersinia enterocolitica serovar O:3 for mice. 179 50
<< Previous
1
2
3
4
5
6
7
8
9
10
Next >>