The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus.

Hultgren, Scott J.; Lindberg, Frederik P.; Magnusson, Göran; Kihlberg, Jan; Tennent, Jan M.; Normark, Staffan

doi:10.1073/pnas.86.12.4357

Cited by 172 publications

(133 citation statements)

References 29 publications

(34 reference statements)

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“…The same compound has also been isolated from the small intestine of miniature swine and characterized by NMR. 7 The A9 type 1 glycosphingolipid differs from the A9 type 3 structure (35) only in that the core Gal at position 4 is 3-linked instead of 4-linked. However, this affects the anomeric region of the NMR spectrum significantly as regards the internal blood group A determinant, as summarized in Table 2.…”

Section: Isolation and Characterization Of F18-binding Glycosphingolimentioning

confidence: 99%

“…FedF is the adhesive subunit and is presumably located at the tip of the fimbrial structure (5,6). Typically, tip adhesins consist of two domains: an N-terminal carbohydrate-specific lectin domain and a C-terminal pilin domain (7), which needs to be donor-strand-complemented to stabilize its incomplete Ig fold (8,9). Crystal structures of the lectin domains of type 1 pili, P pili, and F17 fimbrial adhesins reveal that they all have the immunoglobulin-like (Ig-like) fold in common, which is remarkable, because they show little to no sequence identity (10).…”

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confidence: 99%

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Recognition of Blood Group ABH Type 1 Determinants by the FedF Adhesin of F18-fimbriated Escherichia coli

Coddens

Diswall

Ångström

et al. 2009

Journal of Biological Chemistry

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F18-fimbriated Escherichia coli are associated with porcine postweaning diarrhea and edema disease. Adhesion of F18-fimbriated bacteria to the small intestine of susceptible pigs is mediated by the minor fimbrial subunit FedF. However, the target cell receptor for FedF has remained unidentified. Here we report that F18-fimbriated E. coli selectively interact with glycosphingolipids having blood group ABH determinants on type 1 core, and blood group A type 4 heptaglycosylceramide. The minimal binding epitope was identified as the blood group H type 1 determinant (Fuc␣2Gal␤3GlcNAc), while an optimal binding epitope was created by addition of the terminal ␣3-linked galactose or N-acetylgalactosamine of the blood group B type 1 determinant (Gal␣3(Fuc␣2)Gal␤3GlcNAc) and the blood group A type 1 determinant (GalNAc␣3(Fuc␣2)-Gal␤3GlcNAc). To assess the role of glycosphingolipid recognition by F18-fimbriated E. coli in target tissue adherence, F18-binding glycosphingolipids were isolated from the small intestinal epithelium of blood group O and A pigs and characterized by mass spectrometry and proton NMR. The only glycosphingolipid with F18-binding activity of the blood group O pig was an H type 1 pentaglycosylceramide (Fuc␣2Gal␤3GlcNAc-␤3Gal␤4Glc␤1Cer). In contrast, the blood group A pig had a number of F18-binding glycosphingolipids, characterized as A type 1 hexaglycosylceramide (GalNAc␣3(Fuc␣2)Gal␤3Glc-NAc␤3Gal␤4Glc␤1Cer), A type 4 heptaglycosylceramide (GalNAc␣3(Fuc␣2)Gal␤3GalNAc␤3Gal␣4Gal␤4Glc␤1Cer), A type 1 octaglycosylceramide (GalNAc␣3(Fuc␣2)Gal␤3GlcNAc␤3-Gal␤3GlcNAc␤3Gal␤4Glc␤1Cer), and repetitive A type 1 nonaglycosylceramide (GalNAc␣3(Fuc␣2)Gal␤3GalNAc␣3-(Fuc␣2)Gal␤3GlcNAc␤3Gal␤4Glc␤1Cer). No blood group antigen-carrying glycosphingolipids were recognized by a mutant E. coli strain with deletion of the FedF adhesin, demonstrating that FedF is the structural element mediating binding of F18-fimbriated bacteria to blood group ABH determinants. Enterotoxigenic (ETEC)4 and verotoxigenic Escherichia coli are important causes of disease in man and animal (1, 2). In newly weaned pigs, F18-fimbriated E. coli producing enteroand/or Shiga-like toxins induce diarrhea and/or edema disease, which accounts for substantial economical losses in the pig industry (3). Two virulence factors are of major importance, namely the F18 fimbriae, the adhesive polymeric protein surface appendages of F18-fimbriated E. coli, and the Shiga-like toxin (SLT-IIv), or enterotoxins (STa or STb), that are produced by the bacterium. F18 fimbriae are expressed by the fed (fimbriae associated with edema disease) gene cluster, with fedA encoding the major subunit, fedB the outer membrane usher, fedC the periplasmic chaperone, whereas fedE and fedF encode minor subunits (4). FedF is the adhesive subunit and is presumably located at the tip of the fimbrial structure (5, 6). Typically, tip adhesins consist of two domains: an N-terminal carbohydrate-specific lectin domain and a C-terminal pilin domain (7), which needs to be donor-strand-complemented ...

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Section: Isolation and Characterization Of F18-binding Glycosphingolimentioning

confidence: 99%

mentioning

confidence: 99%

Recognition of Blood Group ABH Type 1 Determinants by the FedF Adhesin of F18-fimbriated Escherichia coli

Coddens

Diswall

Ångström

et al. 2009

Journal of Biological Chemistry

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“…The P pilus comprises a flexible-tip fibrillum made up of minor pilins with the two-domain adhesin PapG at the distal end where it can recognize Galα1-4Gal disaccharide-containing glycolipids found in the human kidney (14,15). The P pilus tip is joined to a righthanded, helical pilus rod made up of PapA pilins (16,17) and is anchored in the OM via the terminator/anchoring subunit PapH (18).…”

mentioning

confidence: 99%

Molecular basis of usher pore gating in Escherichia coli pilus biogenesis

Volkan

Kalas

Pinkner³

et al. 2013

Proc. Natl. Acad. Sci. U.S.A.

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Extracellular fibers called chaperone-usher pathway pili are critical virulence factors in a wide range of Gram-negative pathogenic bacteria that facilitate binding and invasion into host tissues and mediate biofilm formation. Chaperone-usher pathway ushers, which catalyze pilus assembly, contain five functional domains: a 24-stranded transmembrane β-barrel translocation domain (TD), a β-sandwich plug domain (PLUG), an N-terminal periplasmic domain, and two Cterminal periplasmic domains (CTD1 and 2). Pore gating occurs by a mechanism whereby the PLUG resides stably within the TD pore when the usher is inactive and then upon activation is translocated into the periplasmic space, where it functions in pilus assembly. Using antibiotic sensitivity and electrophysiology experiments, a single salt bridge was shown to function in maintaining the PLUG in the TD channel of the P pilus usher PapC, and a loop between the 12th and 13th beta strands of the TD (β12-13 loop) was found to facilitate pore opening. Mutation of the β12-13 loop resulted in a closed PapC pore, which was unable to efficiently mediate pilus assembly. Deletion of the PapH terminator/anchor resulted in increased OM permeability, suggesting a role for the proper anchoring of pili in retaining OM integrity. Further, we introduced cysteine residues in the PLUG and N-terminal periplasmic domains that resulted in a FimD usher with a greater propensity to exist in an open conformation, resulting in increased OM permeability but no loss in type 1 pilus assembly. These studies provide insights into the molecular basis of usher pore gating and its roles in pilus biogenesis and OM permeability.outer membrane usher | macromolecular assembly | bacterial pathogenesis

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“…The plates were blocked with 2% BSA in PBS, then treated with PapD^PapG complex (20 Wg/ml) in blocking bu¡er overnight at 4³C. After washing, the PapD^PapG complex was detected with rabbit anti-PapG antiserum [28], diluted 1:100 and applied at room temperature for 2 h. Ligands bound to the plates were visualized using horseradish peroxidase-conjugated goat anti-rabbit immunoglobulins (diluted 1:100) for 90 min at room temperature, followed by diaminobenzidine development (Pierce, Rockford, IL, USA). Parallel plates were stained with 0.2% orcinol spray to estimate glycolipid loading.…”

Section: Glycolipid Extractions and Adhesin Binding Assaysmentioning

confidence: 99%

“…P pili [2,27] and the PapD^PapG complex [5,28] were isolated from E. coli strain HB101 bearing the appropriate plasmid as described previously. The papG gene was subcloned from plasmid pPAP5 that contains the entire pap operon cloned from the E. coli strain J96 isolate of serotype O4:K6 [29], derived from a case of human pyelonephritis.…”

Section: Bacterial Componentsmentioning

confidence: 99%

Role of intestinal surfactant-like particles as a potential reservoir of uropathogenic Escherichia coli

Mahmood

Engle

Hultgren

et al. 2000

Biochimica et Biophysica Acta (BBA) - General Subjects

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The PapG adhesin of uropathogenic Escherichia coli contains separate regions for receptor binding and for the incorporation into the pilus.

Cited by 172 publications

References 29 publications

Recognition of Blood Group ABH Type 1 Determinants by the FedF Adhesin of F18-fimbriated Escherichia coli

Recognition of Blood Group ABH Type 1 Determinants by the FedF Adhesin of F18-fimbriated Escherichia coli

Molecular basis of usher pore gating in Escherichia coli pilus biogenesis

Role of intestinal surfactant-like particles as a potential reservoir of uropathogenic Escherichia coli

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