Reciprocal exchange of minor components of type 1 and F1C fimbriae results in hybrid organelles with changed receptor specificities

Klemm, Per; Christiansen, Gunna; Kreft, Burkhard; Marre, R.; Bergmans, Hans

doi:10.1128/jb.176.8.2227-2234.1994

Cited by 59 publications

(45 citation statements)

References 38 publications

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“…The focA gene encodes the major fimbrial subunit, while focG and focH encode minor fimbrial subunits; the focC and focD genes are required to encode a chaperone protein and molecular usher (41). It has been reported previously that the two-component export systems of type 1 and F1C fimbriae are interchangeable and that the minor fimbrial structural elements of these two fimbrial systems can be exchanged, resulting in hybrid organelles with changed receptor specificity (21,22,24). However, the regulatory proteins of the foc operon have remained largely uncharacterized.…”

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confidence: 99%

Regulatory Interactions among Adhesin Gene Systems of Uropathogenic Escherichia coli

et al. 2008

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Uropathogenic Escherichia coli strain J96 carries multiple determinants for fimbrial adhesins. The regulatory protein PapB of P fimbriae has previously been implicated in potential coregulatory events. The focB gene of the F1C fimbria determinant is highly homologous to papB; the translated sequences share 81% identity. In this study we investigated the role of PapB and FocB in regulation of the F1C fimbriae. By using gel mobility shift assays, we showed that FocB binds to sequences in both the pap and foc operons in a somewhat different manner than PapB. The results of both in vitro cross-linking and in vivo oligomerization tests indicated that FocB could function in an oligomeric fashion. Furthermore, our results suggest that PapB and FocB can form heterodimers and that these complexes can repress expression of the foc operon. The effect of FocB on expression of type 1 fimbriae was also tested. Taken together, the results that we present expand our knowledge about a regulatory network for different adhesin gene systems in uropathogenic E. coli and suggest a hierarchy for expression of the fimbrial adhesins.

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confidence: 99%

Regulatory Interactions among Adhesin Gene Systems of Uropathogenic Escherichia coli

et al. 2008

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“…A cluster of eight genes (foc) is necessary for the biogenesis of F1C fimbriae (21,22,40,50,51). The F1C fimbrial complex is composed of the major subunit protein FocA (16 kDa) and the minor subunits FocF (17 kDa), FocG (15 kDa), and FocH (30 kDa) (40).…”

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Receptor Structure for F1C Fimbriae of Uropathogenic Escherichia coli

Kniep²,

et al. 2000

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F1C fimbriae are correlated with uropathogenic Escherichia coli strains. Although F1C fimbriae mediate binding to kidney tubular cells, their receptor is not known. In this paper, we demonstrate for the first time specific carbohydrate residues as receptor structure for F1C-fimbria-expressing E. coli. The binding of the F1C fimbriated recombinant E. coli strain HB101(pPIL110-54) and purified F1C fimbriae to reference glycolipids of different carbohydrate compositions was evaluated by using thin-layer chromatography (TLC) overlay and solid-phase binding assays. TLC fimbrial overlay analysis revealed the binding ability of purified F1C fimbriae only to glucosylceramide (GlcCer), ␤1-linked galactosylceramide 2 (GalCer2) with nonhydroxy fatty acids, lactosylceramide, globotriaosylceramide, paragloboside (nLc 4 Cer), lactotriaosylceramide, gangliotriaosylceramide (asialo-GM 2 [GgO 3 Cer]) and gangliotetraosylceramide (asialo-GM 1 [GgO 4 Cer]). The binding of purified F1C fimbriae as well as F1C fimbriated recombinant E. coli strain HB101(pPIL110-54) was optimal to microtiter plates coated with asialo-GM 2 (GgO 3 Cer). The bacterial interaction with asialo-GM 1 (GgO 4 Cer) and asialo-GM 2 (GgO 3 Cer) was strongly inhibited only by disaccharide GalNAc␤1-4Gal␤ linked to bovine serum albumin. We observed no binding to globotetraosylceramide or Forssman antigen (Gb 5 Cer) glycosphingolipids or to sialic-acid-containing gangliosides. It was demonstrated that the presence of a GalCer or GlcCer residue alone is not sufficient for optimal binding, and additional carbohydrate residues are required for high-affinity adherence. Indeed, the binding efficiency of F1C fimbriated recombinant bacteria increased by 19-fold when disaccharide sequence GalNAc␤1-4Gal␤ is linked to glucosylceramide as in asialo-GM 2 (GgO 3 Cer). Thus, it is suggested that the disaccharide sequence GalNAc␤1-4Gal␤ of asialo-GM 2 (GgO 3 Cer) which is positioned internally in asialo-GM 1 (GgO 4 Cer) is the high-affinity binding epitope for the F1C fimbriae of uropathogenic E. coli.

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“…A fundamental question is how the bacteria are able to avoid mixing these up during biosynthesis. We have recently shown that reciprocal exchange of minor components of type 1 and F1C fimbriae results in phenotypically normal hybrid organelles with heterologous receptor specificities (18). The present observations concerning the flexibility of the biogenesis systems provide additional insight into the molecular background of this phenomenon.…”

Section: Discussionmentioning

confidence: 78%

“…Plasmids pPKL4, pPKL63, pPKL34, pPKL84, and pPKL104 containing all or part of the fim gene cluster have been described previously (15-17, 19, 21). Plasmids pPKL143 containing the foc gene cluster has also been described previously (18). Plasmid pPKL161 (fimD) was made by insertion of a HindIII-EagI fragment from plasmid pPKL68 (17) into HindIII-EagI cut pACYC184 (2).…”

Section: Methodsmentioning

confidence: 99%

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The export systems of type 1 and F1C fimbriae are interchangeable but work in parental pairs

et al. 1995

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Type 1 and F1C fimbriae are surface organelles of Escherichia coli which mediate receptor-specific binding to different host surfaces. Such fimbriae are found, among others, on strains associated with urinary tract infections. Biosynthesis of type 1 and F1C fimbrial organelles requires individual, specialized two-component assembly systems. The organization of the fim and foc gene clusters encoding these fimbriae, as well as the structure of the organelles, is very similar; however, the actual sequence homology of the structural elements is not remarkable (34 to 60%). Both gene clusters encode a periplasmically located chaperone and an usher protein, located in the outer membrane, required for organelle biogenesis. Deletion of either element causes abolishment of fimbriation. The present report addresses the question of promiscuity in fimbrial biogenesis. Our data indicate that the two-component export systems of the two organelle systems are reciprocally interchangeable; however, they seem to function only in parental pairs.

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Reciprocal exchange of minor components of type 1 and F1C fimbriae results in hybrid organelles with changed receptor specificities

Cited by 59 publications

References 38 publications

Regulatory Interactions among Adhesin Gene Systems of Uropathogenic Escherichia coli

Regulatory Interactions among Adhesin Gene Systems of Uropathogenic Escherichia coli

Receptor Structure for F1C Fimbriae of Uropathogenic Escherichia coli

The export systems of type 1 and F1C fimbriae are interchangeable but work in parental pairs

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