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Infect Immun. 1990 April; 58(4): 999-1003

Biochemical and biological activities of recombinant S1 subunit of pertussis toxin.

Department of Microbiology, Medical College of Wisconsin, Milwaukee 53226.

ABSTRACT

degP-deficient strains of Escherichia coli grown in M-9 medium supplemented with ZnCl2 expressed the recombinant S1 subunit of pertussis toxin (rS1) in a form electrophoretically identical to the authentic S1 subunit. Subcellular fractionation showed that the full-length form of rS1 was membrane associated, while proteolytic fragments of rS1 were present in the periplasm. rS1 was extracted from outer membrane preparations with 8 M urea and purified by gel filtration chromatography. Purified rS1 ADP-ribosylated transducin at a similar molar efficiency relative to authentic pertussis toxin and, when associated with the native B oligomer of pertussis toxin, elicited Chinese hamster ovary cell clustering.

This article has been cited by other articles:

• Farizo, K. M., Fiddner, S., Cheung, A. M., Burns, D. L. (2002). Membrane Localization of the S1 Subunit of Pertussis Toxin in Bordetella pertussis and Implications for Pertussis Toxin Secretion. Infect. Immun. 70: 1193-1201 [Abstract] [Full Text]