2002
DOI: 10.1099/00221287-148-8-2507
|View full text |Cite
|
Sign up to set email alerts
|

BfpU, a soluble protein essential for type IV pilus biogenesis in enteropathogenic Escherichia coli

Abstract: A cluster of 14 genes located on the large plasmid of enteropathogenic Escherichia coli (EPEC) strains is sufficient to direct the biogenesis of the type IV bundle-forming pilus (BFP) in a recombinant E. coli host. The fifth gene in the cluster, bfpU, encodes a protein that is predicted to be localized to the periplasmic space. To determine whether BfpU is necessary for pilus biogenesis, the authors constructed a non-polar bfpU mutant EPEC strain by allelic exchange. The mutant strain was unable to perform loc… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

2
22
0

Year Published

2003
2003
2022
2022

Publication Types

Select...
6
2

Relationship

3
5

Authors

Journals

citations
Cited by 18 publications
(24 citation statements)
references
References 54 publications
2
22
0
Order By: Relevance
“…Prior localization studies show that two of these proteins (BfpB and BfpG) reside exclusively in the outer membrane and that one (BfpE) resides exclusively in the inner membrane (3,13). Thus, this complex appears to span the periplasmic space, a conclusion that is supported by the finding that BfpU, a soluble protein that is principally located in the periplasmic space, is also a component of the cross-linked complex (13,18). Not surprisingly, BfpA, the principal repeating subunit of the pilus fiber, was also identified in the complex, as was the pilin-like protein BfpJ.…”
supporting
confidence: 62%
“…Prior localization studies show that two of these proteins (BfpB and BfpG) reside exclusively in the outer membrane and that one (BfpE) resides exclusively in the inner membrane (3,13). Thus, this complex appears to span the periplasmic space, a conclusion that is supported by the finding that BfpU, a soluble protein that is principally located in the periplasmic space, is also a component of the cross-linked complex (13,18). Not surprisingly, BfpA, the principal repeating subunit of the pilus fiber, was also identified in the complex, as was the pilin-like protein BfpJ.…”
supporting
confidence: 62%
“…Four volumes of whole-cell lysate (10, 5, 2.5, and 1 l) were loaded onto an SDS-PAGE gel, along with a range of purified BfpU (35 to 1,500 ng) and BfpB (40 to 2,500 ng) mixed together. BfpU and BfpB were purified as previously described, and concentrations determined using the extinction coefficients and the measured A 280 (23,69). Western blotting was performed as described above, and blots were simultaneously probed with anti-BfpU and anti-BfpB, and then with both anti-mouse and anti-rabbit secondary antibodies.…”
Section: Iptg (Isopropyl-␤-d-thiogalactopyranoside)mentioning
confidence: 99%
“…Western blotting. Western blotting for bundlin, BfpB, and BfpU was performed as previously described (23,27,69). SDS-PAGE gels were run according to the manufacturer's instructions (Bio-Rad) and transferred at 21 V for 80 min at 4°C to Immobilon polyvinylidene fluoride (Micropore, catalog no.…”
Section: Iptg (Isopropyl-␤-d-thiogalactopyranoside)mentioning
confidence: 99%
See 1 more Smart Citation
“…These factors also allow bacteria to auto-aggregate, a phenomenon readily observed under the microscope as a clumping of cells and, macroscopically, as flocculation and settling of cells from liquid suspensions (Schembri et al, 2001). Different autoaggregation factors exist in different strains: surface adhesins (Schembri et al, 2003b), type IV pili (Schreiber et al, 2002;Bechet & Blondeau, 2003;Bieber et al, 1998), curli (Olsen et al, 1989) and aggregating adherence fimbriae (Nataro et al, 1993;Czeczulin et al, 1997).…”
Section: Introductionmentioning
confidence: 99%