Skip to main content
Log in

Struktur, Assemblierung und Stabilität von Typ-1-Pili

  • Wissenschaft
  • Supramolekulare Proteinkomplexe
  • Published:
BIOspektrum Aims and scope

Abstract

Type 1 pili are extracellular, supramolecular protein complexes required for the attachment of pathogenic E. coli strains to host cells. Hundreds to thousands of protein subunits are assembled within minutes in vivo and form filaments with unique kinetic stability against dissociation. Here, we review recent work on the structure, assembly mechanism and potential technical applications derived from this exciting biological system.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

Literatur

  1. Stamm W, Stapleton A (2004) Approach to the Patient with Urinary Tract Infection. In: Gorbach S, Bartlett J, Blacklow N (Hrsg) Infectious diseases. Lippincott Williams & Wilkins, Philadelphia, S 861–872

    Google Scholar 

  2. Thanassi DG, Bliska JB, Christie PJ (2012) Surface organelles assembled by secretion systems of Gram-negative bacteria: diversity in structure and function. FEMS Microbiol Rev 36:1046–1082

    Article  PubMed  CAS  Google Scholar 

  3. Nishiyama M, Vetsch M, Puorger C et al. (2003) Identification and characterization of the chaperone-subunit complex-binding domain from the type 1 pilus assembly platform FimD. J Mol Biol 330:513–525

    Article  PubMed  CAS  Google Scholar 

  4. Vetsch M, Puorger C, Spirig T et al. (2004) Pilus chaperones represent a new type of protein-folding catalyst. Nature 431:329–333

    Article  PubMed  CAS  Google Scholar 

  5. Nishiyama M, Ishikawa T, Rechsteiner H et al. (2008) Reconstitution of pilus assembly reveals a bacterial outer membrane catalyst. Science 320:376–379

    Article  PubMed  CAS  Google Scholar 

  6. Crespo MD, Puorger C, Scharer MA et al. (2012) Quality control of disulfide bond formation in pilus subunits by the chaperone FimC. Nat Chem Biol 8:707–713

    Article  PubMed  CAS  Google Scholar 

  7. Phan G, Remaut H, Wang T et al. (2011) Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. Nature 474:49–53

    Article  PubMed  CAS  Google Scholar 

  8. Puorger C, Eidam O, Capitani G et al. (2008) Infinite kinetic stability against dissociation of supramolecular protein complexes through donor strand complementation. Structure 16:631–642

    Article  PubMed  CAS  Google Scholar 

  9. Vetsch M, Sebbel P, Glockshuber R (2002) Chaperoneindependent folding of type 1 pilus domains. J Mol Biol 322:827–840

    Article  PubMed  CAS  Google Scholar 

  10. Giese C, Zosel F, Puorger C et al. (2012) The most stable protein-ligand complex: applications for one-step affinity purification and identification of protein assemblies. Angew Chem Int Ed Engl 51:4474–4478

    Article  PubMed  CAS  Google Scholar 

  11. Le Trong I, Aprikian P, Kidd BA et al. (2010) Structural basis for mechanical force regulation of the adhesin FimH via finger trap-like beta sheet twisting. Cell 141:645–655

    Article  PubMed  Google Scholar 

  12. Choudhury D, Thompson A, Stojanoff V et al. (1999) Xray structure of the FimC-FimH chaperone-adhesin complex from uropathogenic Escherichia coli. Science 285:1061–1066

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Rudi Glockshuber.

Additional information

Christoph Giese 2000–2005 Biochemiestudium an der Universität Halle-Wittenberg. 2006–2011 Promotion an der ETH Zürich, Schweiz, dort seit 2011 Postdoktorand.

Rudi Glockshuber 1979–1985 Chemiestudium an der LMU München und am Max-Planck-Institut für Biochemie, Martinsried. 1985–1989 Promotion am Genzentrum der LMU München. 1989–1994 Postdoktorand an der Universität Regensburg. 1994–1997 Tenure-Track-Assistenzprofessor an der ETH Zürich, Schweiz. 1997–2000 Außr — ordentlicher Professor an der ETH Zürich. Seit 2000 Ordentlicher Professor für Molekularbiologie an der ETH Zürich.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Giese, C., Glockshuber, R. Struktur, Assemblierung und Stabilität von Typ-1-Pili. Biospektrum 19, 492–495 (2013). https://doi.org/10.1007/s12268-013-0343-8

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12268-013-0343-8

Navigation