Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0008354 (cholera)
 20,452 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

Yersinia pestis plague murine toxin has been found to inhibit the mobilization of free fatty acids in mice in a manner similar to that of beta-adrenergic blocking agents. The blockage is detectable 75 min after injection of the toxin (1 to 2 mean lethal doses). The degree of inhibition was directly correlated with the toxicity of a given toxin preparation. Agents such as cholera toxin or glucagon, with apparently distinct receptors from beta-adrenergic receptors, stimulated adenylate cyclase and lipolysis and effectively modified toxicity. Likewise, cyclic adenosine 3',5'-monophosphate bypassed the toxin block and antagonized toxicity. Energy-rich compounds such as fatty acids, organic acids, and glucose effectively modified the intoxication process. The biological activity of plague toxin showed profound temperature sensitivity. Mice placed at 5 degrees C were highly susceptible to the effects of the toxin, whereas mice placed at 37 degrees C were totally resistant to intoxication. Results showed that plague toxin cannot block epinephrine-induced mobilization of free fatty acids in mice placed at 37 degrees C. These studies suggested that plague toxin acts at the receptor level in a manner similar to that of beta-adrenergic blocking agents. A complete, analogous activity was shown between toxin and known beta-adrenergic antagonists in their effect on beta-adrenergic agonist action in stimulating lipolysis. It is hypothesized that, since toxin shows no in vitro activity, it is in some way modified in animals.
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PMID:Beta-adrenergic blocking activity of Yersinia pestis murine toxin. 19 77

The first part considers pathogenic microorganisms (Vibrio cholerae and parahaemolytic vibrio, Clostridium welchii, enteropathogenic E. coli, Shigella, Salmonella, other enterobacteria and pseudomonas. Yersinia, simply enterotoxic Staphylococcus and that producing acute enteritis) and the process of infection (formation of a surface link without endocellular penetration with elaboration of hexotoxins, formation of a surface link with subsequent intracellular penetration, submucosa penetration). The second part discusses Salmonellae on the basis of personal experience. Particular attention is paid to current aspects of Salmonella microbiological pathomorphosis, the various isolated serotypes in relation to carriers or patients, biochemical atypias of Salmonellae strains, present-day aspects of resistance to chemoantibiotic treatment and the transfer of Salmonella Wien resistances.
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PMID:[Classification of acute bacterial enteropathies]. 89 78

Furazolidone was more active than 3-(1-methyl)-5-nitro-2-imidazolyl-methylideneamino)-2-oxazolidinone (MABN) against a series of 34 isolates of Pasteurella and 11 of Yersinia (formerly designated Pasteurella). However, the nitroimidazole was superior to furazolidone by both subcutaneous and oral routes against a series of mouse infections incited by strains of Pasteurella. It also was superior to furazolidone and sulfaquinoxaline when administered in the diet against two Pasteurella strains in a fowl cholera model infection in chickens. The good in vitro activity of MABN plus its low toxicity suggest its further study as an agent for fowl cholera and the shipping fever complex of cattle.
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PMID:In vitro and in vivo activity of 3-(1-methyl 1-5-nitro-2-imidazolylmethylideneamino)-2-oxazolidinone against Pasteurella. 94 11

The absolute configuration of 3-hydroxy fatty acids has been studied, which are present in the lipopolysaccharides of the following bacteria: Phodopseudomonas gelatinosa, Rh. viridis, Rhodospirillum tenue, Chromobacterium violaceum, Pseudomonas aeruginosa, Bordetella pertussis, Vibrio metchnikovii, Vibrio cholerae, Salmonella spp., Escherichia coli, Shigella flexneri, Proteus mirabilis, Yersinia enterocolitica and Fusobacterium nucleatum. The 3-hydroxy acids were liberated by strong alkaline hydrolysis, converted to 3-methoxy acid L-phenylethylamides and analyzed by gas-liquid chromatography. With the aid of authentic D-3-hydroxy fatty acids it was shown for all lipopolysaccharides that the 3-hydroxy acids, regardless of chain lengths, branching, 3-O-substitution or type of linkage, possess the D-configuration. 2-Hydroxydodecanoic acid, which is present in some lipopolysaccharides, was analyzed in an analogous way and shown to possess the L-configuration.
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PMID:Absolute configuration of 3-hydroxy fatty acids present in lipopolysaccharides from various bacterial groups. 127 68

Heat-stable enterotoxins (ST) activate guanylyl cyclase in T84 cells, rapidly and specifically. Activation is monitored by cGMP production and occurs at lower concentrations of ST than required for eliciting fluid accumulation in suckling mice. Atrial natriuretic factor (ANF) neither activates guanylyl cyclase nor modulates the response to ST in T84 cells, indicating the absence of receptors for ANF on T84 cells. Monitoring the production of cGMP under conditions known to alter fluid accumulation in suckling mice is an accurate and quantifiable assay of ST activity and its interaction with the receptor. STs produced by Escherichia coli, Vibrio cholerae non-01 and Yersinia enterocolitica individually produce elevated levels of cGMP in T84 cells, but to differing extents, suggesting that this model system can be used to elucidate the different events of ST-receptor interactions at the molecular level.
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PMID:Interaction of heat-stable enterotoxins with human colonic (T84) cells: modulation of the activation of guanylyl cyclase. 135 30

The nucleotide sequence has been determined for the gene designated tcpN, encoding a putative regulatory protein within the tcp gene cluster associated with the biosynthesis and assembly of the toxin-coregulated pilus of Vibrio cholerae. It is preceded by a powerful transcriptional terminator which presumably delimits the major tcp operon, but at its 3' end is translationally coupled to the gene, tcpJ, encoding the TCP pilin signal peptidase. The tcpN gene encodes a putative 276-residue protein of 31,890 Da. This TcpN shows a high degree of homology to the transcriptional activators, Rns, associated with pilus biosynthesis in enterotoxigenic Escherichia coli, and to VirF, which controls the Yersinia virulence regulon. This homology also extends to the C termini of other members of the AraC family of transcriptional regulators, including RhaS, RhaR and CelD.
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PMID:Homology of TcpN, a putative regulatory protein of Vibrio cholerae, to the AraC family of transcriptional activators. 135 61

Cross-agglutination and cross-agglutinin absorption experiments were carried out on non-O1 Vibrio cholerae bio-serogroup Hakata (Hakata) and Yersinia enterocolitica O9 (O9). It was shown that the O-antigen of Hakata was closely related to that of O9 in an a, b-a, c type of relationship. The antigenic relationship between the O-antigens of the two bacteria was analyzed by passive hemolysis (PH) and passive hemolysis inhibition (PHI) tests by using their lipopolysaccharides (LPS) as antigen for sensitizing sheep red blood cells (SRBC) and, in the case of the latter, as an inhibitor in a PH system consisting of LPS-coated SRBC, guinea-pig complement and anti-Hakata or O9 antiserum, both unabsorbed and absorbed with the heterologous Hakata or O9 antigen. In the PH experiment, unabsorbed anti-Hakata antiserum had hemolytic titers of 126,100 and 2,600 against Hakata- and O9-LPS-coated SRBC, respectively, and anti-O9 antiserum had hemolytic titers of 19,400 and 38,800, respectively, against these SRBC. The PH experiment showed that anti-O9 antiserum contains a hemolysin reacting with the heterologous Hakata antigen at a high titer (19,400), while anti-Hakata antiserum contains a hemolysin reacting with the heterologous O9 antigen at a significant titer (2,600). The former was completely removed from anti-O9 antiserum with the Hakata antigen and the latter from anti-Hakata antiserum with the O9 antigen. Thus, serological cross-reactivity was demonstrated between the Hakata and O9 strains.
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PMID:Serological cross-reaction between Yersinia enterocolitica O9 and non-O1 Vibrio cholerae bio-serogroup Hakata and antigenic analysis of their relationship by their lipopolysaccharides. 138 6

The 70-kb pYV plasmid of Yersinia enterocolitica directs the synthesis and secretion of several virulence determinants called Yops. These proteins are produced during the invasion of the host tissues and induce a strong antibody response. The yop genes are transcribed from strong promoters activated by a common transcription activator. Recombinant Y. enterocolitica strains expressing the B subunit of the cholera toxin were constructed from a yopH-ctxB operon fusion. Integration of the gene ctxB in the pYV plasmid itself, by a double crossing over, ensured its stability in the infecting bacteria. Oral inoculation of recombinant bacteria in mice elicited serum and intestinal antibody responses and resulted in protection of the immunized mice against a cholera toxin challenge. Secretory immunoglobulin A antibodies against the cholera toxin B subunit occurred not only in the intestines but also in the respiratory tract.
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PMID:Oral immunization against cholera toxin with a live Yersinia enterocolitica carrier in mice. 163 86

A monoclonal antibody (MAb) against synthetic heat-stable enterotoxin of Vibrio cholerae non-O1 (NAG-ST) was produced. The MAb, namely, 2F, belonged to the immunoglobulin G1 class. Ascitic fluid drawn from pristane-primed BALB/c mice injected with a 2F-producing clone demonstrated anti-NAG-ST activity which could be detected in enzyme-linked immunosorbent assay even at a dilution of 1:128,000. Fifty-fold-diluted ascitic fluid could completely neutralize the activity of NAG-ST (synthetic and native) and Vibrio mimicus ST (identical to NAG-ST) in suckling mice. In the same assay, 2F could also neutralize Yersinia enterocolitica ST (Y-ST) but did not neutralize Escherichia coli STh and STp. A similar pattern of reactivity occurred in a competitive enzyme-linked immunosorbent assay with homologous and heterologous toxins. Competitive inhibition curves with synthetic peptides representing NAG-ST and its shorter analogs revealed that aspartic acid located at position 2 from the N terminus of NAG-ST was the essential residue of the recognized epitope. Significantly, in Y-ST, to which 2F cross-reacted, aspartic acid is in the corresponding position as that of NAG-ST, thereby confirming our conclusions that the epitope defining this MAb is aspartic acid.
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PMID:Production of a monoclonal antibody to Vibrio cholerae non-O1 heat-stable enterotoxin (ST) which is cross-reactive with Yersinia enterocolitica ST. 169 28


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