Formation of Adhesive Pili by the Chaperone‐Usher Pathway

Vetsch, Michael; Glockshuber, Rudi

doi:10.1002/9783527619498.ch62

Cited by 9 publications

(6 citation statements)

References 114 publications

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“…The positions of the amide protons of A147 and I7 (I7 corresponds to I171 in FimF F ) are indicated in red. site), the FimF donor strand (residues [1][2][3][4][5][6][7][8][9][10][11][12][13][14], and a C-terminal (His) 6 tag. Similar to FimF F , the helper construct was obtained as a soluble protein after expression in the E. coli cytoplasm.…”

Section: Nmr Studies On Binary Complexes Of Fimfmentioning

confidence: 99%

“…[1][2][3] At least 37 adhesive surface filaments that belong to this class have been identified. 4 Most thoroughly investigated are type 1 pili from uropathogenic Escherichia coli strains, which cause cystitis, 5,6 P pili from E. coli, which are involved in the development of pyelonephritis and cystitis, 7 Afa/Dr fimbriae from E. coli strains, which cause chronic diarrheal and recurrent urinary tract infections, 8 and the F1 antigen on Yersinia pestis, which causes plague. 9 This work focused on type 1 pili from uropathogenic E. coli strains, which are outstandingly stable filamentous structures and are composed of a pilus rod carrying a peripheral tip fibrillum (Fig.…”

Section: Introductionmentioning

confidence: 99%

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NMR Structure of the Escherichia coli Type 1 Pilus Subunit FimF and Its Interactions with Other Pilus Subunits

Gossert¹,

Bettendorff²,

Puorger³

et al. 2008

Journal of Molecular Biology

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Section: Nmr Studies On Binary Complexes Of Fimfmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

NMR Structure of the Escherichia coli Type 1 Pilus Subunit FimF and Its Interactions with Other Pilus Subunits

Gossert¹,

Bettendorff²,

Puorger³

et al. 2008

Journal of Molecular Biology

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“…Many Gram-negative pathogens adhere to the host tissue via filamentous, adhesive pili or fimbria that are assembled via the ''chaperone-usher'' pathway (Hung and Hultgren, 1998;Thanassi et al, 1998;Vetsch and Glockshuber, 2005). Among the best characterized pilus systems are type 1 pili from uropathogenic E. coli strains.…”

Section: Introductionmentioning

confidence: 99%

Infinite Kinetic Stability against Dissociation of Supramolecular Protein Complexes through Donor Strand Complementation

et al. 2008

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Adhesive type 1 pili from uropathogenic Escherichia coli strains are heat and denaturant resistant, filamentous protein complexes. Individual pilus subunits associate through "donor strand complementation," whereby the incomplete immunoglobulin-like fold of each subunit is completed by the N-terminal extension of a neighboring subunit. We show that antiparallel donor strand insertion generally causes nonequilibrium behavior in protein folding and extreme activation energy barriers for dissociation of subunit-subunit complexes. We identify the most kinetically stable, noncovalent protein complex known to date. The complex between the pilus subunit FimG and the donor strand peptide of the subunit FimF shows an extrapolated dissociation half-life of 3 x 10(9) years. The 15 residue peptide forms ideal intermolecular beta sheet H-bonds with FimG over 10 residues, and its hydrophobic side chains strongly interact with the hydrophobic core of FimG. The results show that kinetic stability and nonequilibrium behavior in protein folding confers infinite stability against dissociation in extracellular protein complexes.

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“…A broad variety of Gram‐negative pathogens use the chaperone–usher pathway to assemble adhesive surface fibres, which are composed of up to several thousand protein subunits (Vetsch & Glockshuber, 2005). Such adhesive pili target pathogenic bacteria to the site of infection and thus have a crucial role during pathogenesis.…”

Section: Introductionmentioning

confidence: 99%

Mechanism of fibre assembly through the chaperone–usher pathway

Vetsch¹,

Erilov²,

Molière³

et al. 2006

EMBO Reports

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The chaperone-usher pathway directs the formation of adhesive surface fibres in numerous pathogenic Gram-negative bacteria. The fibres or pili consist exclusively of protein subunits that, before assembly, form transient complexes with a chaperone in the periplasm. In these chaperone:subunit complexes, the chaperone donates one b-strand to complete the imperfect immunoglobulin-like fold of the subunit. During pilus assembly, the chaperone is replaced by a polypeptide extension of another subunit in a process termed 'donor strand exchange' (DSE). Here we show that DSE occurs in a concerted reaction in which a chaperone-bound acceptor subunit is attacked by another chaperone-bound donor subunit. We provide evidence that efficient DSE requires interactions between the reacting subunits in addition to those involving the attacking donor strand. Our results indicate that the pilus assembly platforms in the outer membrane, referred to as ushers, catalyse fibre formation by increasing the effective concentrations of donor and acceptor subunits.

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Formation of Adhesive Pili by the Chaperone‐Usher Pathway

Cited by 9 publications

References 114 publications

NMR Structure of the Escherichia coli Type 1 Pilus Subunit FimF and Its Interactions with Other Pilus Subunits

NMR Structure of the Escherichia coli Type 1 Pilus Subunit FimF and Its Interactions with Other Pilus Subunits

Infinite Kinetic Stability against Dissociation of Supramolecular Protein Complexes through Donor Strand Complementation

Mechanism of fibre assembly through the chaperone–usher pathway

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