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Journal of Bacteriology, July 2002, p. 3457-3465, Vol. 184, No. 13
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.13.3457-3465.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

The Type IV Pilus Assembly Complex: Biogenic Interactions among the Bundle-Forming Pilus Proteins of Enteropathogenic Escherichia coli

Sandra W. Ramer,,{dagger} Gary K. Schoolnik,* Cheng-Yen Wu, Jaiweon Hwang, Sarah A. Schmidt, and David Bieber,{ddagger}

Department of Medicine (Infectious Diseases and Geographic Medicine) and Microbiology & Immunology, Stanford Medical School, Stanford, California 94305

Received 23 January 2002/ Accepted 3 April 2002

Production of type IV bundle-forming pili (BFP) by enteropathogenic Escherichia coli (EPEC) requires the protein products of 12 genes of the 14-gene bfp operon. Antisera against each of these proteins were used to demonstrate that in-frame deletion of individual genes within the operon reduces the abundance of other bfp operon-encoded proteins. This result was demonstrated not to be due to downstream polar effects of the mutations but rather was taken as evidence for protein-protein interactions and their role in the stabilization of the BFP assembly complex. These data, combined with the results of cell compartment localization studies, suggest that pilus formation requires the presence of a topographically discrete assembly complex that is composed of BFP proteins in stoichiometric amounts. The assembly complex appears to consist of an inner membrane component containing three processed, pilin-like proteins, BfpI, -J, and -K, that localize with BfpE, -L, and -A (the major pilin subunit); an outer membrane, secretin-like component, BfpB and -G; and a periplasmic component composed of BfpU. Of these, only BfpL consistently localizes with both the inner and outer membranes and thus, together with BfpU, may articulate between the Bfp proteins in the inner membrane and outer membrane compartments.

* Corresponding author. Mailing address: Beckman Center, B241a, Stanford School of Medicine, Stanford, CA 94305. Phone: (650) 723-8158. Fax: (650) 723-1399. E-mail: schoolni{at}cmgm.stanford.edu.

{dagger} Present address: Maxygen, Redwood City, CA 94063.

{ddagger} Present address: Department of Biological Sciences, San Jose State University, San Jose, CA 95192-0100.

Journal of Bacteriology, July 2002, p. 3457-3465, Vol. 184, No. 13
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.13.3457-3465.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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