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)

Ozone and chlorine are agents that disinfect by destroying, neutralizing or inhibiting the growth of pathogenic microorganisms. The treatment of drinking water with ozone has shown to be more efficient against spores of Bacillus subtilis. It was observed that the ozone already in dose of 0.35 mg/l produced the reduction of at least 5 log in populations of approximately 1 x 10(6) cells/ml of Escherichia coli, Vibrio cholerae, Salmonella typhi, Yersinia enterocolitica, Pseudomonas aeruginosa, Aeromonas hydrophila, Listeria monocytogenes and Staphylococcus aureus. With a dose of 0.50 mg/l of chlorine, the reduction was much smaller for the tested microorganisms (except Vibrio cholerae), while the effect of 2 mg/l of chlorine was similar to the ozone treatment. For spores of Bacillus subtilis, the reduction observed with ozone concentrations of 0.35 and 0.70 mg/l was of almost 3 log, while no considerable effect was obtained with chlorine in the tested conditions. Our results have shown that both disinfectans were consumed during the treatment period, probably because of the own water demand and the added bacterial mass.
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PMID:[Water disinfection: comparative activities of ozone and chlorine on a wide spectrum of bacteria]. 885 Jan 29

Fluoroquinolones are efficient antimicrobial drugs for the treatment of enteric fever, shigellosis, Escherichia coli diarrhea, cholera, and traveler's diarrhea. They also play a role in the therapy of yersiniosis, campylobacteriosis, and intestinal salmonellosis. A single dose of quinolones has been effective in the treatment of traveler's diarrhea and cholera. Uncomplicated typhoid fever was cured by norfloxacin, pefloxacin, and ofloxacin 400 mg twice daily (b.i.d.) for 7-14 days or ciprofloxacin 500 mg b.i.d. for 10 days. A single daily dose of 400 mg fleroxacin for 3 days has been shown to be effective in this indication. A few reports suggest that the newer quinolones can eliminate the carrier state. The efficacy of quinolones in the prophylaxis and treatment of intra-abdominal infections following abdominal surgery requires further investigation.
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PMID:Quinolones in gastrointestinal infections. 886 34

Chemical and serological studies of LPS from Vibrio cholerae O76 (O76) were performed. The LPS of O76 contained D-glucose, D-galactose, L-glycero-D-manno-heptose, D-fructose, D-glucosamine, D-quinovosamine (2-amino-2,6-dideoxy-D-glucose) and L-perosamine (4-amino-4,6-dideoxy-L-mannopyranose). The sugar composition of the LPS from O76 was quite similar to that of LPS from V. cholerae O1 with the exception of the presence of a small amount of D-galactose in the LPS of O76. However, perosamine, a major sugar component of the LPS from O76, was in the L configuration in contrast to the D configuration of the perosamine in the LPS of V. cholerae O1. The L-perosamine was N-acylated with an (S)-(+)-2-hydroxypropionyl group in the LPS from O76. Structural analysis by NMR spectroscopy, as well as GC/MS, revealed that the O polysaccharide chain of the LPS from O76 was an alpha(1-->2)-linked homopolymer of N-[(S)-(+)-2-hydroxypropionyl]-L-perosamine. The serological cross-reactivity between the LPS of O76 and the LPS from other strains, such as V. cholerae O1 (Ogawa and Inaba O forms), Vibrio bio-serogroup 1875 (Original and Variant strains), V. cholerae O140 (Hakata) and Yersinia enterocolitica O9, was examined in passive haemolysis tests with sheep red blood cells that had been sensitized with LPS and antisera raised against whole cells of these bacteria. The latter six strains have in common the O antigen that includes Inaba antigen factor C, in addition to their own O-antigenic factors. Thus, they crossreact serologically. The O polysaccharide chains of the LPS of these six trains are known to consist exclusively of alpha(1-->2)-linked D-perosamine homopolymers and differences are found only among the N-acyl substituents. In passive haemolysis tests, the LPS of O76 did not cross-react serologically with any of the other LPS examined. Thus, the results obtained in this study support the hypothesis that Inaba antigen factor C, associated with the O antigens of these six strains, which include V. cholerae O1, is related substantially and exclusively to their alpha(1-->2)-linked homopolymers of N-acylated D-perosamine, and not to such homopolymers of N-acylated L-perosamine.
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PMID:The O polysaccharide chain of the lipopolysaccharide from Vibrio cholerae O76 is a homopolymer of N-[(S)-(+)-2-hydroxypropionyl]-alpha-L-perosamine. 888 4

Chemical and serological studies were performed with the lipopolysaccharide (LPS) from Vibrio cholerae O144 (O144). The LPS of O144 contained D-glucose, D-galactose, L-glycero-D-manno-heptose, D-fructose, D-quinovosamine (2-amino-2,6-dideoxy-D-gluco-pyranose) and L-perosamine (4-amino-4,6-dideoxy-L-manno-pyranose). The perosamine, a major component sugar of the LPS from O144, was in an L-configuration, as is also the case in the LPS from V. cholerae O76 (O76), in contrast to the D-configuration of the perosamine in the LPS of V. cholerae O1. A structural analysis revealed that the O polysaccharide chain of the LPS from O144 is an alpha(1-->2)-linked homopolymer of (R)-(-)-2-hydroxypropionyl-L-perosamine. The serological cross-reactivity between O144 and O76 was clearly revealed by cross-agglutination and cross-agglutinin absorption tests with whole cells, as well as by passive hemolysis tests with sheep red-blood cells that had been sensitized with the LPS from O144 and O76. In contrast, in passive hemolysis tests, the LPS of O144 did not cross-react serologically with the LPSs from other strains such as V. cholerae O1 (Ogawa and Inaba), V. cholerae O140, Vibrio bio-serogroup 1875 (Original and Variant) and Yersinia enterocolitica O9. The LPSs from these strains consist of O polysaccharide chains composed of alpha(1-->2)-linked homopolymers of D-perosamine with various N-acyl groups, and they share the Inaba antigen factor C of V. cholerae O1 in common. The results obtained in this study demonstrate that the absolute configuration of the perosamine residue in homopolymers plays a very important role in the expression of the serological specificity of the Inaba antigen factor C of V. cholerae O1.
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PMID:An N-[(R)-(-)-2-hydroxypropionyl]-alpha-L-perosamine homopolymer constitutes the O polysaccharide chain of the lipopolysaccharide from Vibrio cholerae O144 which has antigenic factor(s) in common with V. cholerae O76. 898 46

Microencapsulated Fl and V sub-unit antigens of Yersinia pestis were used to immunize mice intraperitoneally with a combination of 25 micrograms of each of the microencapsulated sub-units. The combined microsphere formulation induced both mucosal and systemic immunity. There was an additive effect in combining sub-units and the protection afforded by the combined microencapsulated antigens was superior to that provided by the administration of any single encapsulated antigen and by the existing whole cell vaccine. The protective efficacy of the combined microencapsulated sub-units was further enhanced by co-administering cholera toxin B sub-unit. Microencapsulation of the sub-units offered advantages which included depot release of the vaccine in vivo and the facilitation of oral, intranasal or inhalational delivery. Therefore, immunization with microencapsulated sub-unit antigens was an effective means of generating humoral and cellular responses which endowed protective immunity.
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PMID:Local and systemic immune response to a microencapsulated sub-unit vaccine for plague. 903 89

Various lymphocyte subpopulations have the capacity to bind different strains of Gram-negative bacteria. The capacity of a strain of Vibrio cholerae, biotype El Tor, isolated during an outbreak of cholera, to adhere to mononuclear cells isolated from peripheral blood was evaluated. V. cholerae binds to mononuclear cells in a dose-dependent manner. The binding was 76.1% at a cells/bacteria ratio of 1:200 and significantly decreased to 43.1% at a ratio of 1:1. The value of bound bacteria, a marker of the mean number of binding sites on the cell surface, decreased at lower cell/bacteria ratios. Studies on isolated cellular populations demonstrated that 51, 42 and 38%, respectively, of CD4+, CD8+ and B cells were bound by V. cholerae whereas monocytes exhibited a higher binding capacity. The data suggest that the percentage binding of V. cholerae to lymphocytes and monocytes was higher than the percentage found in previous studies with Gram-negative bacteria such as Yersinia enterocolitica, and Salmonella, but similar to Helicobacter pylori. The findings indicate that V. cholerae possesses multiple 'adhesins' such as fimbriae, flagella, haemagglutinins, lipopolysaccharides, and outer membrane proteins. The capacity to bind to blood lymphocytes may reflect the same capacity for the lymphocytes from the gastrointestinal associated lymphoid tissue. This cytoadherence may contribute to the uptake of V. cholerae from the gut and may contribute to activation of B cells and CD4+ lymphocytes.
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PMID:Spontaneous binding of Vibrio cholerae to human leucocytes. 914 13

Two monoclonal antibodies (MAbs), designated as H9 (IgG2a) and H20 (IgM), directed against heat-shock protein 60 (HSP60) of Helicobacter pylori strain TK1029 were established. Affinity-purified antigens cross-reacted in immunoblots with MAb H9 and MAb H20 respectively. These antigens also reacted with the 3C8 MAb previously established in this laboratory, which recognised Yersinia enterocolitica HSP60. By amino-acid sequence analysis, the N-terminal amino-acid sequence of the protein recognised by both H9 and H20 MAbs was confirmed as the amino-acid sequence of H. pylori HSP60 reported previously. Both MAbs reacted with nine strains of H. pylori in enzyme-linked immunosorbent assay (ELISA) and immunoblot analysis. In addition, MAb H9 reacted with extracts of other bacteria including H. mustelae, Pseudomonas aeruginosa, Vibrio cholerae, Serratia marcescens, Proteus mirabilis, Escherichia coli and Shigella sonnei. In contrast, MAb H20 reacted only with strains H. pylori. These results suggest that both the species-specific epitope recognised by MAb H20 and the common epitope recognised by MAb H9 exist on HSP60 of the bacterial cell. Both MAbs also reacted with the 60-kDa protein in the lysate of human gastric carcinoma (MKN45) cells. It was shown by immunohistochemical staining that gastric epithelial cells of four out of six biopsy specimens examined stained positively with MAb H20. These results suggest that there is a common epitope in H. pylori HSP60 and human gastric epithelial cells.
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PMID:Production and characterisation of monoclonal antibodies to heat-shock protein 60 of Helicobacter pylori. 936 37

In analogy with Vibrio cholerae and other toxigenic enteropathogens such as Yersinia enterocolitica it seems most likely today that H. pylori by specific surface proteins binds to epithelial cell receptors (Table 1) allowing the pathogen to deliver urease, vacuolating toxin and other toxic metabolites to cause tissue damage and inflammation (1-3). H. pylori as well as animal gastric pathogens as H. mustelae and H. felis have developed an efficient flagellar apparatus allowing rapid and efficient penetration of the gastric mucus layer (3). Most interestingly, flagellae seems to be synthesized in the late stage of growth before the switch of spiral-shaped organisms to coccoidal forms in a liquid medium.
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PMID:Biochemical aspects of H. pylori adhesion. 937 15

The RfaH protein controls the transcription of a specialized group of Escherichia coli and Salmonella operons that direct the synthesis, assembly and export of the lipopolysaccharide core, exopolysaccharide, F conjugation pilus and haemolysin toxin. RfaH is a specific regulator of transcript elongation; its loss increases transcription polarity in these operons without affecting initiation from the operon promoters. The operons of the RfaH-dependent regulon contain a short conserved 5' sequence, the ops element, deletion of which increases operon polarity to an extent similar to that caused by loss of RfaH. The ops element is also present upstream of polysaccharide gene clusters of Shigella flexneri, Yersinia enterocolitica, Vibrio cholerae and Klebsiella pneumoniae and the RP4 fertility operon of Pseudomonas aeruginosa, suggesting that this is a widely spread control system. The mechanistic coupling of RfaH and the ops element has been demonstrated in vitro and in vivo, and we suggest that the ops element recruits RfaH and potentially other factors to the RNA polymerase complex, modifying the complex to increase its processivity and allowing transcription to proceed over long distances.
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PMID:RfaH and the ops element, components of a novel system controlling bacterial transcription elongation. 942 23

The production of several virulence factors in Vibrio cholerae O1, including cholera toxin and the pilus colonization factor TCP (toxin-coregulated pilus), is strongly influenced by environmental conditions. To specifically identify membrane proteins involved in these signal transduction events, we examined a transposon library of V. cholerae generated by Tnbla mutagenesis for cells that produce TCP when grown under various nonpermissive conditions. To select for TCP-producing cells we used the recently described bacteriophage CTX phi-Kan, which uses TCP as its receptor and carries a gene encoding resistance to kanamycin. Among the isolated mutants was a transposon insertion in a gene homologous to nqrB from Vibrio alginolyticus, which encodes a subunit of a Na(+)-translocating NADH:ubiquinone oxidoreductase, and tcpI, encoding a chemo-receptor previously implicated in the negative regulation of TCP production. A third transposon mutant had an insertion in tcpP, which is in an operon with tcpH, a known positive regulator of TCP production. However, TcpP was shown to be essential for TCP production in V. cholerae, as a tcpP-deletion strain was deficient in pili production. The amino-terminal region of TcpP shows sequence homology to the DNA-binding domains of several regulatory proteins, including ToxR from V. cholerae and PsaE from Yersinia pestis. Like ToxR, TcpP activates transcription of the toxT gene, an essential activator of tcp operon transcription. Furthermore, TcpH, with its large periplasmic domain and inner membrane anchor, has a structure similar to that of ToxS and was shown to enhance the activity of TcpP. We propose that TcpP/TcpH constitute a pair of regulatory proteins functionally similar to ToxR/ToxS and PsaE/PsaF that are required for toxT transcription in V. cholerae.
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PMID:TcpP protein is a positive regulator of virulence gene expression in Vibrio cholerae. 943 61


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