Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Changes of endotoxin in plasma, and the response of the coagulation system and blood cells in septicemia of Haemophilus parasuis infection were examined by inoculation with H. parasuis in specific pathogen-free (SPF) pigs. Eight pigs were inoculated intratracheally with 10(5), 10(6) and 10(7) colony formation units (CFU) of the strain Nagasaki (serovar 5). All pigs died 28 to 42 hr after inoculation. Haematologically, severe leukopenia occurred 24 hr post inoculation (hpi) until death. Glucose concentration decreased from 24 hpi to death. In the coagulation system, decrease of platelet counts, prolongation of prothrombin time, activated partial thromboplastin time, and increase of fibrinogen-fibrin degradation products were observed in all inoculated pigs. Endotoxin was detected in the plasma of all the inoculated pigs from 16 hpi to death, and its concentration rose dramatically just before death. H. parasuis was re-isolated from the blood of all inoculated pigs from 16 hpi to death, and also from almost all organs and body fluids of the pigs. The pigs had microthrombi in the kidney, liver and lungs, and many also had pneumonia, meningitis and serositis. H. parasuis antigen was detected in the lesions by the immunoperoxidase technique. The results indicated that disseminated intravascular coagulation (DIC) and endotoxin shock involved aggravation of clinical signs and death on the pigs induced to septicemia of H. parasuis.
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PMID:Effects on endotoxin pathogenicity in pigs with acute septicemia of Haemophilus parasuis infection. 923 19

The biochemical properties of the D-glutamate-adding enzymes (MurD) from Escherichia coli, Haemophilus influenzae, Enterococcus faecalis, and Staphylococcus aureus were investigated to detect any differences in the activity of this enzyme between gram-positive and gram-negative bacteria. The genes (murD) that encode these enzymes were cloned into pMAL-c2 fusion vector and overexpressed as maltose-binding protein-MurD fusion proteins. Each fusion protein was purified to homogeneity by affinity to amylose resin. Proteolytic treatments of the fusion proteins with factor Xa regenerated the individual MurD proteins. It was found that these fusion proteins retain D-glutamate-adding activity and have Km and Vmax values similar to those of the regenerated MurDs, except for the H. influenzae enzyme. Substrate inhibition by UDP-N-acetylmuramyl-L-alanine, the acceptor substrate, was observed at concentrations greater than 15 and 30 microM for E. coli and H. influenzae MurD, respectively. Such substrate inhibition was not observed with the E. faecalis and S. aureus enzymes, up to a substrate concentration of 1 to 2 mM. In addition, the two MurDs of gram-negative origin were shown to require monocations such as NH4+ and/or K+, but not Na+, for optimal activity, while anions such as Cl- and SO4(2-) had no effect on the enzyme activities. The activities of the two MurDs of gram-positive origin, on the other hand, were not affected by any of the ions tested. All four enzymes required Mg2+ for the ligase activity and exhibited optimal activities around pH 8. These differences observed between the gram-positive and gram-negative MurDs indicated that the two gram-negative bacteria may apply a more stringent regulation of cell wall biosynthesis at the early stage of peptidoglycan biosynthesis pathway than do the two gram-positive bacteria. Therefore, the MurD-catalyzed reaction may constitute a fine-tuning step necessary for the gram-negative bacteria to optimally maintain its relatively thin yet essential cell wall structure during all stages of growth.
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PMID:Comparison of the D-glutamate-adding enzymes from selected gram-positive and gram-negative bacteria. 1046 12

The antiphospholipid syndrome (APS) is characterized by the presence of pathogenic autoantibodies against beta2-glycoprotein-I (beta2GPI). The factors causing production of anti-beta2GPI remain unidentified, but an association with infectious agents has been reported. Recently, we identified a hexapeptide (TLRVYK) that is recognized specifically by a pathogenic anti-beta2GPI mAb. In the present study we evaluated the APS-related pathogenic potential of microbial pathogens carrying sequences related to this hexapeptide. Mice immunized with a panel of microbial preparations were studied for the development of anti-beta2GPI autoantibodies. IgG specific to the TLRVYK peptide were affinity purified from the immunized mice and passively infused intravenously into naive mice at day 0 of pregnancy. APS parameters were evaluated in the infused mice on day 15 of pregnancy. Following immunization, high titers of antipeptide [TLRVYK] anti-beta2GPI Ab's were observed in mice immunized with Haemophilus influenzae, Neisseria gonorrhoeae, or tetanus toxoid. The specificity of binding to the corresponding target molecules was confirmed by competition and immunoblot assays. Naive mice infused with the affinity-purified antipeptide Ab's had significant thrombocytopenia, prolonged activated partial thromboplastin time and elevated percentage of fetal loss, similar to a control group of mice immunized with a pathogenic anti-beta2GPI mAb. Our study establishes a mechanism of molecular mimicry in experimental APS, demonstrating that bacterial peptides homologous with beta2GPI induce pathogenic anti-beta2GPI Ab's along with APS manifestations.
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PMID:Bacterial induction of autoantibodies to beta2-glycoprotein-I accounts for the infectious etiology of antiphospholipid syndrome. 1190 Nov 88