Structural polymorphism of bacterial adhesion pili (original) (raw)

Nature volume 373, pages 164–167 (1995)Cite this article

Abstract

BACTERIAL adhesion pili are designed to bind specifically and main-tain attachment of bacteria to target cells. Uropathogenic P-pili are sufficiently mechanically resilient to resist the cleansing action of urine flow that removes most other bacteria1. P-pili are 68 Å in diameter and ˜1 um long2, and are composed of ˜1,000 copies of the principal structural protein, PapA3. They are attached to the outer membrane by a minor structural protein, PapH4 and are terminated by an ˜20 Å diameter fibrillus composed of PapK, PapE and PapF, which presents the host-binding adhesin PapG5–7. The amino-acid sequences of PapA3,8, PapE9, and PapF9 are simi-lar, with highly conserved C-termini being responsible for binding to PapD10–12, the periplasmic chaperone. Our three-dimensional reconstruction indicates that pili are formed by the tight winding of a much thinner structure. A structural transition allows the pilus to unravel without depolymerizing, producing a thin, extended structure five times the length of the original pilus.

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Authors and Affiliations

  1. Department of Biophysics, Boston University School of Medicine, Boston, Massachusetts, 02118-2394, USA
    Esther Bullitt
  2. Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, 32306-3015, USA
    Lee Makowski

Authors

  1. Esther Bullitt
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  2. Lee Makowski
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Bullitt, E., Makowski, L. Structural polymorphism of bacterial adhesion pili.Nature 373, 164–167 (1995). https://doi.org/10.1038/373164a0

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