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Nat Commun. 2016 Oct 4;7:13015. doi: 10.1038/ncomms13015.

Structure of the Neisseria meningitidis Type IV pilus.

Author information

1
Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, British Columbia, Canada V5A 1S6.
2
Institut Necker-Enfants Malades, INSERM U1151, Université Paris Descartes, 14 Rue Maria Helena Vieira Da Silva, CS 61431, 75014 Paris, France.
3
Department of Biochemistry and Molecular Genetics, University of Virginia School of Medicine, Charlottesville, Virginia 22908, USA.

Abstract

Neisseria meningitidis use Type IV pili (T4P) to adhere to endothelial cells and breach the blood brain barrier, causing cause fatal meningitis. T4P are multifunctional polymers of the major pilin protein, which share a conserved hydrophobic N terminus that is a curved extended α-helix, α1, in X-ray crystal structures. Here we report a 1.44 Å crystal structure of the N. meningitidis major pilin PilE and a ∼6 Å cryo-electron microscopy reconstruction of the intact pilus, from which we built an atomic model for the filament. This structure reveals the molecular arrangement of the N-terminal α-helices in the filament core, including a melted central portion of α1 and a bridge of electron density consistent with a predicted salt bridge necessary for pilus assembly. This structure has important implications for understanding pilus biology.

PMID:
27698424
PMCID:
PMC5059446
DOI:
10.1038/ncomms13015
[Indexed for MEDLINE]
Free PMC Article

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