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Gene Review:

bfpB - BfpB

Escherichia coli B171

Ramer, S.W. et al., Schmidt, S.A. et al., Hwang, J. et al., Müller, D. et al., Daniel, A. et al.

Ramer, Bieber, Schoolnik,

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Disease relevance of bfpB

Structure-function analysis of BfpB, a secretin-like protein encoded by the bundle-forming-pilus operon of enteropathogenic Escherichia coli [1].

High impact information on bfpB

BfpB expression is also associated with accumulation of EPEC proteins in growth medium, suggesting that it may support both pilus biogenesis and protein secretion [1].
Disruption of bfpB, the second open reading frame downstream of bfpA, was performed by allelic exchange [2].
It is reported that targeting of BfpG to the OM was influenced by the secretin BfpB [3].
BfpG and BfpU interacted with the amino terminus of BfpB [3].

Biological context of bfpB

Assays of bfpA and bfpB mRNAs and protein expression showed that both genes are cotranscribed as part of an environmentally responsive operon that is regulated by growth phase and ammonium [2].
Thus, BfpB is required for pilus biogenesis [2].

Analytical, diagnostic and therapeutic context of bfpB

We developed and evaluated a robust multiplex PCR to identify these pathogroups based on sequences complementary to escV, bfpB, stx1, and stx2 [4].
The BFP assembly complex, containing a BfpB-His6 fusion protein, was chemically cross-linked in situ, and the complex was then purified from BFP-expressing EPEC by a combination of nickel- and BfpB antibody-based affinity chromatography [5].
Biochemical and cell fractionation studies showed that BfpB is a 58-kDa lipoprotein that is located primarily in the outer membrane [2].

References

Structure-function analysis of BfpB, a secretin-like protein encoded by the bundle-forming-pilus operon of enteropathogenic Escherichia coli. Schmidt, S.A., Bieber, D., Ramer, S.W., Hwang, J., Wu, C.Y., Schoolnik, G. J. Bacteriol. (2001) [Pubmed]
BfpB, an outer membrane lipoprotein required for the biogenesis of bundle-forming pili in enteropathogenic Escherichia coli. Ramer, S.W., Bieber, D., Schoolnik, G.K. J. Bacteriol. (1996) [Pubmed]
Interaction and localization studies of enteropathogenic Escherichia coli type IV bundle-forming pilus outer membrane components. Daniel, A., Singh, A., Crowther, L.J., Fernandes, P.J., Schreiber, W., Donnenberg, M.S. Microbiology (Reading, Engl.) (2006) [Pubmed]
Rapid identification and differentiation of clinical isolates of enteropathogenic Escherichia coli (EPEC), atypical EPEC, and Shiga toxin-producing Escherichia coli by a one-step multiplex PCR method. Müller, D., Hagedorn, P., Brast, S., Heusipp, G., Bielaszewska, M., Friedrich, A.W., Karch, H., Schmidt, M.A. J. Clin. Microbiol. (2006) [Pubmed]
Structural and topographical studies of the type IV bundle-forming pilus assembly complex of enteropathogenic Escherichia coli. Hwang, J., Bieber, D., Ramer, S.W., Wu, C.Y., Schoolnik, G.K. J. Bacteriol. (2003) [Pubmed]

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