Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0043167 (pertussis)
 19,595 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

In a previous study, all convalescent-phase sera from patients with culture-confirmed legionellosis reacted on immunoblots with a Legionella genus-wide 58-kilodalton (kDa) protein antigen (J.S. Sampson, B.B. Plikaytis, and H.W. Wilkinson, J. Clin. Microbiol. 23:92-99, 1986). The present study was done to immunologically characterize and determine the diagnostic relevance of this purified antigen. The antigen was precipitated from enriched cell extracts with ammonium sulfate and purified by high-pressure liquid chromatography. High-titered rabbit antiserum produced to the purified protein was used to show its presence on immunoblots in the 60-kDa range in 38 Legionella serogroups, representing 23 species, and in 39 non-Legionella bacteria. The antiserum was made specific for Legionella strains by sequential absorptions with Bordetella pertussis, Pseudomonas aeruginosa, and Pseudomonas fluorescens whole cells. Serum from legionellosis patients reacted with both specific and nonspecific epitopes. Results of indirect immunofluorescence experiments showed that neither specific nor nonspecific epitopes of the 60-kDa protein were surface exposed on Legionella cells and that cross-reactive epitopes were variably exposed on non-Legionella bacteria. The 60-kDa protein antigen should be useful in diagnostic tests for legionellosis if care is taken to expose cryptic epitopes and if the tests use or measure only the Legionella-specific epitopes.
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PMID:Purified 60-kilodalton Legionella protein antigen with Legionella-specific and nonspecific epitopes. 244 17

In superfused striatal synaptosomes, previously unexposed to Ca2+ during isolation and superfusion, 1.25 mM Ca2+ evokes the release of [3H]dopamine. This Ca2+-evoked release is produced without elevating K+ (4.5 mM) before or after Ca2+ exposure, can be blocked by the Na+ channel antagonist tetrodotoxin, and modulated by dopamine (D2) receptor agonists and antagonists. We now present evidence that functional K+ channels regulate Ca2+-evoked [3H]dopamine release and may be necessary for the dopamine (D2) modulation of this release. The K+ channel blocker tetraethyl ammonium (TEA) could partially prevent D2 agonist (LY-171555) inhibition of Ca2+-evoked release in both olfactory tubercle and striatal synaptosomes. Another K+ channel blocker, 4-aminopyridine, also partially blocked dopamine (D2) agonist inhibition of release. When both 5 mM tetraethyl ammonium and 0.1 mM 4-aminopyridine were employed, by, dopamine (D2) inhibition of Ca2+-evoked [3H]dopamine release was prevented. However, with both K+ channel blockers present, only the initial portion of the release could be blocked by tetrodotoxin. These results are consistent with what might be expected if K+ channels were linked to dopamine (D2) receptors. In additional experiments we found that stimulation of adenylate cyclase by 1 microM forskolin with 0.25 mM 3-isobutyl-1-methylxanthine present potentiated Ca2+-evoked [3H]dopamine release but that this combination did not affect dopamine (D2) inhibition of [3H]dopamine release. Furthermore, although the protein alkylator n-ethylmaleimide could block dopamine (D2) inhibition of release, pertussis toxin, a specific inactivator of the inhibitory protein regulating adenylate cyclase, had little effect on dopamine (D2) inhibition. Therefore, dopamine (D2) inhibition of dopamine release may not be coupled to adenylate cyclase activity.
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PMID:K+ channel and adenylate cyclase involvement in regulation of Ca2+-evoked release of [3H]dopamine from synaptosomes. 246 5

The relationship between the chemotactic-factor-elicited changes in the intracellular pH and the shape of human neutrophils was investigated using simultaneous measurements of both parameters. The results demonstrate first that fMet-Leu-Phe and leukotriene B4 elicit qualitatively similar pH and shape change responses from the neutrophils. A relationship between the chemoattractant-elicited decrease in cytoplasmic pH and the shape changes is indicated by several findings including: 1) the similarities in the time courses of the two responses, 2) the ability of propionic acid to induce a transient and pertussis-toxin-sensitive shape change response, and 3) the ability of the calcium ionophore A23187 to similarly induce both responses under conditions when the degranulation is minimized. On the other hand, several other results indicate that the drop in pH is not a sufficient condition for the chemotactic-factor-stimulated shape changes. These include: 1) the ability of pertussis toxin to inhibit the shape changes induced by propionic acid and by A23187 without affecting the drop in pH, and 2) the observation that the drop in pH induced by propionic acid persists significantly longer than the shape change. Increasing the cytoplasmic pH by adding ammonium chloride was also found to cause shape changes in the neutrophils. The response to the base differs in two important aspects from that caused by propionic acid: it is pertussis-toxin-insensitive, and it is long-lived. Chemotactic factors have been found to induce a shape change under conditions when the internal pH was artificially increased or decreased, indicating that it is not the absolute cytoplasmic pH that represents the internal signalling parameter. The results are discussed in terms of the activation of the cytoskeletal network of the neutrophils by chemotactic factors.
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PMID:Relationship between pH, sodium, and shape changes in chemotactic-factor-stimulated human neutrophils. 282 Oct 15

Fimbriae were detached from Bordetella pertussis by mechanical shearing and purified by successive precipitations with ammonium sulfate, phosphate buffer (pH 6.0), and magnesium chloride. In each of these purification steps, the fimbriae aggregated into bundles as seen by electron microscopy. These aggregates could be disaggregated at pH 9.5. By electron microscopy, the purified fimbriae appeared as long filaments with a diameter of 5 nm. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of the purified fimbriae showed a single protein subunit with a molecular weight of 22,000. The purified fimbriae did not have hemagglutinating activity when assayed with several types of erythrocytes, and they were antigenically, chemically, and structurally distinct from the filamentous hemagglutinin of B. pertussis. The purified fimbriae were also identified as serotype 2 agglutinogens, since antibody to the purified fimbriae agglutinated B. pertussis strains serotyped as 1.2.4, 1.2.3, or 1.2.3.6 but did not agglutinate those serotyped as 1.3.6.
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PMID:Purification and characterization of fimbriae isolated from Bordetella pertussis. 285 48

Fimbriae were removed from Bordetella pertussis by mechanical shearing and purified by successive precipitations with ammonium sulfate, pH 6.0 phosphate buffer, and magnesium chloride. Electron microscopy showed the purified fimbriae to be long filamentous structures (5 nm in diameter) which aggregated into bundles at pH 6.0. Sodium dodecyl sulfate gel electrophoresis of the purified fimbriae gave a single protein subunit with a molecular weight of 22,000. The purified fimbriae did not have hemagglutinating activity when assayed with a variety of erythrocytes and were shown to be antigenically and structurally distinct from the filamentous hemagglutinin of B. pertussis. The purified fimbriae were identified as serotype 2 agglutinogens as antibody to the purified fimbriae agglutinated B. pertussis strains serotyped as 1.2.4, 1.2.3, or 1.2.3.6, but did not agglutinate serotypes 1.3.6. Immunization of mice with the purified fimbriae (14 micrograms) protected them from a lethal respiratory infection with strain 18323 (agglutinogen serotype 1.2.3.4.6) or with strain 432 (serotype 1.3.6). Immunization of mice with purified fimbriae containing 0.02% LPF also protected them from a lethal intracerebral infection with 18323. The ED50 was about 13 micrograms. Fimbriae containing less than 0.005% LPF did not protect mice from intracerebral challenge.
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PMID:Purification of serotype 2 fimbriae of Bordetella pertussis and their identification as a mouse protective antigen. 287 3

One serotype antigen, agglutinogen 3, from Bordetella pertussis, (strain M2, serotype 1.3), has been purified. The purification procedure included acetone drying of cells harvested from shaking cultures. Agglutinogens were extracted in phosphate buffered saline. Crude extract was heat treated at 80 degrees C for 5 min and precipitated by ammonium sulphate between 25 and 60% saturation at 4 degrees C, providing 50% of the total activity and a five-fold purification. Further purification was attempted by gel filtration chromatography using a TSK-G3000 SW column. The ammonium sulphate precipitated fraction was also separated by anion exchange chromatography using a Mono Q HR 5/5 column. The purification work indicated that agglutinogen 3 is associated with several other substances and that this property can lead to purification difficulties. The isolation procedure was monitored by an agglutination-inhibition assay. The peak fraction from the ion exchange chromatography was purified up to 27-fold according to the specific activities (inhibition units per mg protein). The yield was only 1% due to severe loss of activity. In the gel filtration chromatography agglutinogen 3-activity eluted with a maximum activity corresponding to a molecular weight near 450,000. SDS-PAGE analysis indicated that agglutinogen 3 might have a subunit molecular weight of 20,800.
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PMID:Purification and preliminary characterization of agglutinogen 3 from Bordetella pertussis. 287 4

Treatment of mice by intraperitoneal inoculation of pertussis vaccine or lipopolysaccharide extracted from B. pertussis will effect resistance to rabies virus, encephalomyocarditis virus, Semliki Forest virus, and Herpes simplex virus. Our previous observations indicated that treatment of C3H/HeN (+/nu) and BDF1 mice with pertussis vaccine injected i.p. five days prior to a mouse adenovirus lethal dose i.p. challenge elicited resistance to clinical disease and death. Susceptibility returned to a portion of the test population 35 days after pertussis vaccine treatment. The pertussis vaccine induced resistance developed in athymic (nude) mice also; however, the population succumbed to infection 35 days later. Titration of pertussis vaccine with respect to induction of resistance indicated the median effective dose (ED50) was approximately 25 micrograms dry weight. This report describes the antiviral activity of acellular components extracted from pertussis vaccine. Extraction of B. pertussis cells with 1.0M NaCl and ammonium sulfate fractionation (20-40% saturation) of the extract resulted in an acellular preparation that induced resistance to lethal dose mouse adenovirus infection. The resistance inducing activity was retained after treatment of the extract with detergent (GAF Emulphogene BC 720) to remove lipopolysaccharide and adsorption to alum gel. Comparison of endotoxin content of pertussis vaccine acellular fractions, polysaccharide fraction and purified lipopolysaccharide suggested that endotoxin probably plays a role in the induction of resistance. The endotoxin content of a Emulphogene-treated preparation that protected 80% of a test population was 39 ng. The lipopolysaccharide extracted from Escherichia coli, Vibrio cholerae, Salmonella typhimurium, and Salmonella minnesota did not induce a resistant state seven days after administration; however, lipopolysaccharide extracted from B. pertussis induced a resistant state.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Immunomodulation by Bordetella pertussis: antiviral effects. 287 9

Fimbriae were removed from Bordetella pertussis (serotype 1.3.6) by mechanical shearing and purified by precipitation with ammonium sulfate, pH-dependent precipitation at pH 7.4, followed by two successive extractions of the precipitated fimbriae with 4 M urea. By electron microscopy, the precipitated fimbriae appeared as aggregated bundles of long, relatively straight filaments which were disaggregated to individual flexuous filaments at pH 10.5. These purified fimbriae were identified as serotype 6 agglutinogens, since antibody to the purified fimbriae agglutinated B. pertussis strains serotyped as 1.3.6, 1.2.3.6, or 1.2.3.4.6 but did not agglutinate strains of serotype 1.2.3.4, 1.2.3, or 1.3. In contrast, antibody to serotype 2 fimbriae only agglutinated B. pertussis strains containing serotype 2 agglutinogen. Purified type 6 and 2 fimbriae were found to be weakly cross-reactive by enzyme-linked immunosorbent assay, using polyclonal antibody to each type of fimbria. In an immunoblot assay, polyclonal antibodies to a 22,000-dalton subunit of fimbriae from B. bronchiseptica reacted strongly with the type 2 fimbrial subunit of B. pertussis, but only weakly with the type 6 subunit. When subjected to sodium dodecyl sulfate-polyacrylamide gel electrophoresis, the protein subunit of the type 6 fimbriae migrated with a molecular weight of 21,500, whereas the type 2 fimbrial subunit had a molecular weight of 22,000. The two types of subunits had similar amino acid compositions and showed amino-terminal sequence homology in 15 of 21 amino acids. The amino-terminal amino acid sequences of the B. pertussis fimbriae were distinct from those reported for fimbriae from other gram-negative bacteria. Neither the type 6 nor the type 2 fimbriae caused hemagglutination when assayed with several types of erythrocytes.
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PMID:Purification and characterization of serotype 6 fimbriae from Bordetella pertussis and comparison of their properties with serotype 2 fimbriae. 288 93

Protective antigen was extracted from Bordetella pertussis cells with 1.0 M NaCl and precipitated with ammonium sulfate, 20-40% saturation (designated fraction 15A-1B). The protective antigen was purified further by detergent (Emulphogene BC720) treatment and adsorption to aluminum hydroxide gel (designated fraction 15A-108A). Compared with B. pertussis vaccine and fraction 15A-1B, fraction 15A-108A retained protective activity as assessed by the mouse protection test, but had reduced protein and markedly reduced endotoxin content. Fraction 15A-108A also had reduced leukocytosis-promoting, histamine sensitizing splenomegaly-inducing, and adjuvant activities. Emulphogene treatment provided a relatively simple method for removing endotoxin from a potential acellular B. pertussis vaccine.
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PMID:Removal of lipopolysaccharide from acellular Bordetella pertussis vaccine by detergent treatment. 288 30

The suspension of B. pertussis cells in 0.15 M NaC1 solution, used for the preparation of corpuscular pertussis vaccine contains components loosely bound to microbial cells and producing pronounced mitogenic effect on mouse splenocytes at a concentration of 10 micrograms/ml. The mitogenic activity of B. pertussis is due to complex substances (lipopolysaccharide, protein, nucleic acids) with a wide range of molecular weights (70,000 to greater than 400,000). The mitogenic factor showing no leukocyte-stimulating and protective activity has been isolated by sedimentation with ammonium sulfate and gel filtration on Sephadex G-200. The mitogenic activity of B. pertussis lipopolysaccharide in the blast transformation test has been confirmed.
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PMID:[Mitogenic action of the liquid phase of a microbial suspension of Bordetella pertussis]. 289 Feb 49


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