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)

Soluble adenylate cyclase [EC 4.6.1.1] accumulates in the culture medium of exponentially growing Bordetella pertussis (300-900 pmol of cAMP formed/min per ml of 24 hr culture supernatant). In addition, there is an extracytoplasmic adenylate cyclase which enables the intact organisms to form [32P] cAMP (adenosine 3':5'-cyclic monophosphate) from exogenous [alpha-32P] ATP (200-1200 nmol of cAMP formed/min per g wet weight of cells) and which comprises 20-45% of the total adenylate cyclase activity. In contrast, only 1.7 and 2.4% of the total cell malate dehydrogenase [EC 1.1.1.37] and alkaline phosphatase [EC 3.1.3.1], respectively, are detectable in the intact cell. Trypsin treatment of intact organisms destroys 96% of the extracytoplasmic adenylate cyclase, but does not reduce the total cell malate dehydrogenase or a small pool of intracellular adenylate cyclase. Four compartments of adenylate cyclase in B. pertussis are proposed; (A) soluble enzyme in the culture supernatant (up to 20% of the total activity); (B) enzyme associated with intact cells and measurable without cell disruption (20-45%); (C) extracytoplasmic enzyme sensitive to trypsin, but not measurable in intact cells at standard substrate concentrations (40-60%); and (D) intracellular enzyme (7-9%). In comparison with previously studied bacterial adenylate cyclases, the extracytoplasmic location appears to be unique to the B. pertussis enzyme.
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PMID:Extracytoplasmic adenylate cyclase of Bordetella pertussis. 18 May 29

Localization of the heat-labile dermonecrotic toxin of Bordetella pertussis strain 114 grown in chemically defined Stainer-Scholte medium was studied by using skin reaction in 4-day-old suckling mice as the assay for toxin. Through log phase and into stationary phase of growth the toxin was cell associated and not detected in the culture supernatant. Only about 4% of the activity present in a suspension of lysed cells was detected in a suspension of whole cells, and the dermonecrotic activity was not released by subjecting whole cells to osmotic shock, a procedure that releases proteins from the periplasmic space of many gram-negative bacteria. After cell lysis and preparation of soluble and membrane fractions, 73 to 80% of the activity in the cell lysate was recovered in the soluble fraction, with only 3 to 6% present in a membrane fraction. Further evidence for the intracellular cytoplasmic localization of the dermonecrotic toxin was the insensitivity of the toxin to trypsin treatment of whole cells. Treatment of whole cells with trypsin (80 micrograms/ml) for 20 min at 37 degrees C did not decrease dermonecrotic or malate dehydrogenase activities, but did inhibit more than 95% of the extra-cytoplasmic adenylate cyclase activity. Identical trypsin treatment of a cell lysate decreased all the above activities by more than 90%.
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PMID:Intracellular localization of the dermonecrotic toxin of Bordetella pertussis. 22 87