Structural insights into the biogenesis and biofilm formation by the Escherichia coli common pilus

Proc Natl Acad Sci U S A. 2012 Mar 6;109(10):3950-5. doi: 10.1073/pnas.1106733109. Epub 2012 Feb 21.

Abstract

Bacteria have evolved a variety of mechanisms for developing community-based biofilms. These bacterial aggregates are of clinical importance, as they are a major source of recurrent disease. Bacterial surface fibers (pili) permit adherence to biotic and abiotic substrates, often in a highly specific manner. The Escherichia coli common pilus (ECP) represents a remarkable family of extracellular fibers that are associated with both disease-causing and commensal strains. ECP plays a dual role in early-stage biofilm development and host cell recognition. Despite being the most common fimbrial structure, relatively little is known regarding its biogenesis, architecture, and function. Here we report atomic-resolution insight into the biogenesis and architecture of ECP. We also derive a structural model for entwined ECP fibers that not only illuminates interbacteria communication during biofilm formation but also provides a useful foundation for the design of novel nanofibers.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesins, Bacterial
  • Bacterial Physiological Phenomena
  • Biofilms*
  • Crystallography, X-Ray / methods
  • Escherichia coli / growth & development*
  • Escherichia coli / physiology
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / physiology
  • Fimbriae Proteins / chemistry
  • Fimbriae Proteins / physiology
  • Fimbriae, Bacterial / metabolism*
  • Fimbriae, Bacterial / physiology*
  • Genetic Variation
  • Microscopy, Electron / methods
  • Models, Genetic
  • Models, Molecular
  • Molecular Chaperones / chemistry
  • Molecular Chaperones / physiology
  • Molecular Conformation
  • Nanotechnology / methods

Substances

  • Adhesins, Bacterial
  • EcpA protein, E coli
  • Escherichia coli Proteins
  • Molecular Chaperones
  • ecpD protein, E coli
  • Fimbriae Proteins

Associated data

  • PDB/3QS2
  • PDB/3QS3