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Ultrahigh resolution and full-length pilin structures with insights for filament assembly, pathogenic functions, and vaccine potential

Academic Article
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Overview

authors

  • Hartung, S.
  • Arvai, A. S.
  • Wood, T.
  • Kolappan, S.
  • Shin, D. S.
  • Craig, L.
  • Tainer, John

publication date

  • December 2011

journal

  • Journal of Biological Chemistry  Journal

abstract

  • Pilin proteins assemble into Type IV pili (T4P), surface-displayed bacterial filaments with virulence functions including motility, attachment, transformation, immune escape, and colony formation. However, challenges in crystallizing full-length fiber-forming and membrane protein pilins leave unanswered questions regarding pilin structures, assembly, functions, and vaccine potential. Here we report pilin structures of full-length DnFimA from the sheep pathogen Dichelobacter nodosus and FtPilE from the human pathogen Francisella tularensis at 2.3 and 1 Å resolution, respectively. The DnFimA structure reveals an extended kinked N-terminal α-helix, an unusual centrally located disulfide, conserved subdomains, and assembled epitopes informing serogroup vaccines. An interaction between the conserved Glu-5 carboxyl oxygen and the N-terminal amine of an adjacent subunit in the crystallographic dimer is consistent with the hypothesis of a salt bridge between these groups driving T4P assembly. The FtPilE structure identifies an authentic Type IV pilin and provides a framework for understanding the role of T4P in F. tularensis virulence. Combined results define a unified pilin architecture, specialized subdomain roles in pilus assembly and function, and potential therapeutic targets.

subject areas

  • Amino Acid Sequence
  • Bacterial Proteins
  • Bacterial Vaccines
  • Crystallography, X-Ray
  • Dichelobacter nodosus
  • Fimbriae Proteins
  • Fimbriae, Bacterial
  • Models, Molecular
  • Molecular Sequence Data
  • Polymers
  • Protein Conformation
  • Sequence Homology, Amino Acid
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Identity

PubMed Central ID

  • PMC3243539

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M111.297242

PubMed ID

  • 22027840
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Additional Document Info

start page

  • 44254

end page

  • 44265

volume

  • 286

issue

  • 51

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