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Journal of Bacteriology, March 2001, p. 2111-2116, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.2111-2116.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Involvement of Domain 3 in Oligomerization by the Protective Antigen Moiety of Anthrax Toxin

Jeremy Mogridge, Michael Mourez, and R. John Collier*

Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115

Received 12 September 2000/Accepted 18 December 2000

Protective antigen (PA), a component of anthrax toxin, binds receptors on mammalian cells and is activated by a cell surface protease. The resulting active fragment, PA63, forms ring-shaped heptamers, binds the enzymic moieties of the toxin, and translocates them to the cytosol. Of the four crystallographic domains of PA, domain 1 has been implicated in binding the enzymic moieties; domain 2 is involved in membrane insertion and oligomerization; and domain 4 binds receptor. To determine the function of domain 3, we developed a screen that allowed us to isolate random mutations that cause defects in the activity of PA. We identified several mutations in domain 3 that affect monomer-monomer interactions in the PA63 heptamer, indicating that this may be the primary function of this domain.


* Corresponding author. Mailing address: Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115. Phone: (617) 432-1930. Fax: (617) 432-0115. E-mail: jcollier{at}hms.harvard.edu.


Journal of Bacteriology, March 2001, p. 2111-2116, Vol. 183, No. 6
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.6.2111-2116.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.



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