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Nippon Saikingaku Zasshi, 1957 Some of the next articles are maybe not open access.
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Pertussis toxin (Bordetella pertussis)
1997Abstract PT (Sekura et al. 1985) is a protein of 105 000 daltons composed of five noncovalently linked subunits named 51 through 55, and organized into two functional domains called A and B (Tamura et al. 1982). The A domain, which is composed of the 51 subunit, is an enzyme that intoxicates eukaryotic cells by ADP-ribosylating their GTP¬
R Rappuoli, M G Pizza
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Infection and Immunity, 1996
The DNA sequence of the pertussis toxin operon (ptx) of Bordetella pertussis predicts that transcription of the operon ends downstream from the ptxS3 gene at a possible stem-loop structure. Secretion of the assembled pertussis toxin into the culture medium required the expression of 8 genes arranged in an operon (ptl) and lying 55 bp downstream from ...
Ricci S., Rappuoli R., Scarlato V.
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The DNA sequence of the pertussis toxin operon (ptx) of Bordetella pertussis predicts that transcription of the operon ends downstream from the ptxS3 gene at a possible stem-loop structure. Secretion of the assembled pertussis toxin into the culture medium required the expression of 8 genes arranged in an operon (ptl) and lying 55 bp downstream from ...
Ricci S., Rappuoli R., Scarlato V.
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Pertussis toxin export requires accessory genes located downstream from the pertussis toxin operon
Molecular Microbiology, 1993SummaryPertussis toxin, a major virulence factor of Bordetella pertussis, is an oligomeric protein composed of five different subunits that are exported individually to the periplasmic space by the signal peptide–dependent pathway. After assembly, the protein is exported from the periplasm to the extracellular compartment.
A, Covacci, R, Rappuoli
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Binding of NAD+ to pertussis toxin
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991The equilibrium dissociation constant of NAD+ and pertussis toxin was determined by equilibrium dialysis and by the quenching of the protein's intrinsic fluorescence on titration with NAD+. A binding constant, Kd, of 24 +/- 2 microM at 30 degrees C was obtained from equilibrium dialysis, consistent with the previously determined value for the Michaelis
M D, Lobban +2 more
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Pharmacology of pertussis toxin B-oligomer
Canadian Journal of Physiology and Pharmacology, 1996Pertussis toxin (PTX) is a heterohexameric protein, which is divided into subunits A and B. The A-subunit (protomer) possesses adenine diphosphate (ADP) ribosyltransferase activity, and the B-oligomer confers cell surface binding specificity on the toxin.
Wong, W.S.F., Rosoff, P.M.
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Production of cell mass and pertussis toxin by Bordetella pertussis
Journal of Biotechnology, 1991The cultivation of Bordetella pertussis affects production of pertussis toxin and biomass. Comparison of batch mode, chemostat operation and pHstat-turbidostatic control showed that productivities for the continuous process were greater than that for the batch operation.
P, Licari, G R, Siber, R, Swartz
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Fed-batch cultivation of Bordetella pertussis: Metabolism and Pertussis Toxin production
Biologicals, 2006The production of acellular pertussis in comparison with whole cell pertussis vaccines demands 5-25 times the amount of Bordetella pertussis' virulence factors, such as Pertussis Toxin (PT), to produce the same number of vaccine doses. An increase in the volumetric productivity by employing fed-batch rather than the currently used batch cultivations of
Thalen, M. +8 more
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