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Infection and Immunity, August 2005, p. 5273-5277, Vol. 73, No. 8
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.8.5273-5277.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Mutation of the Zinc-Binding Metalloprotease Motif Affects Bacteroides fragilis Toxin Activity but Does Not Affect Propeptide Processing

Augusto A. Franco,1* Simy L. Buckwold,1 Jai W. Shin,1 Miguel Ascon,1 and Cynthia L. Sears1,2

Divisions of Infectious Diseases,1 Gastroenterology, Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, Maryland 212052

Received 1 December 2004/ Returned for modification 21 February 2005/ Accepted 24 March 2005

To evaluate the role of the zinc-binding metalloprotease in Bacteroides fragilis toxin (BFT) processing and activity, the zinc-binding consensus sequences (H348, E349, H352, G355, H358, and M366) were mutated by site-directed-mutagenesis. Our results indicated that single point mutations in the zinc-binding metalloprotease motif do not affect BFT processing but do reduce or eliminate BFT biologic activity in vitro.

* Corresponding author. Mailing address: Division of Infectious Diseases, Johns Hopkins University School of Medicine, Ross Bldg., Rm. 1167, 1147B Rutland Ave., Baltimore, MD 21205. Phone: (410) 955-9686. Fax: (410) 614-9775. E-mail: afranco{at}jhem.jhmi.edu.

Editor: J. T. Barbieri

Infection and Immunity, August 2005, p. 5273-5277, Vol. 73, No. 8
0019-9567/05/$08.00+0     doi:10.1128/IAI.73.8.5273-5277.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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