Journal of Bacteriology, August 2001, p. 4848-4859, Vol. 183, No. 16
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.16.4848-4859.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Departments of Medicine (Infectious Diseases and Geographic Medicine) and Microbiology & Immunology, Stanford Medical School, Stanford, California 94305
Received 2 February 2001/Accepted 22 May 2001
Production of type IV bundle-forming pili by enteropathogenic
Escherichia coli (EPEC) requires BfpB, an
outer-membrane lipoprotein and member of the secretin protein
superfamily. BfpB was found to compose a ring-shaped,
high-molecular-weight outer-membrane complex that is stable in 4%
sodium dodecyl sulfate at temperatures of
65°C. Chemical
cross-linking and immunoprecipitation experiments disclosed that the
BfpB multimeric complex interacts with BfpG, and mutational studies
showed that BfpG is required for the formation and/or
stability of the multimer but not for the outer-membrane localization
of BfpB. Formation of the BfpB multimer also does not require BfpA, the
repeating subunit of the pilus filament. Functional studies of the
BfpB-BfpG complex revealed that its presence confers vancomycin
sensitivity, indicating that it may form an
incompletely gated channel through the outer membrane. BfpB
expression is also associated with accumulation of EPEC
proteins in growth medium, suggesting that it may support both pilus
biogenesis and protein secretion.
Present address: Maxygen, Redwood City, CA 94063.
This article has been cited by other articles:
| Appl. Environ. Microbiol. | Infect. Immun. | Eukaryot. Cell |
|---|---|---|
| Mol. Cell. Biol. | J. Virol. | Microbiol. Mol. Biol. Rev. |
| ALL ASM JOURNALS |