Structure of the Neisseria meningitidis Type IV pilus

Subramania Kolappan, Mathieu Coureuil, Xiong Yu, Xavier Nassif, Edward H. Egelman () and Lisa Craig ()
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Subramania Kolappan: Simon Fraser University
Mathieu Coureuil: Institut Necker-Enfants Malades, INSERM U1151, Université Paris Descartes, 14 Rue Maria Helena Vieira Da Silva, CS 61431
Xiong Yu: University of Virginia School of Medicine
Xavier Nassif: Institut Necker-Enfants Malades, INSERM U1151, Université Paris Descartes, 14 Rue Maria Helena Vieira Da Silva, CS 61431
Edward H. Egelman: University of Virginia School of Medicine
Lisa Craig: Simon Fraser University

Nature Communications, 2016, vol. 7, issue 1, 1-12

Abstract: 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.

Date: 2016
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DOI: 10.1038/ncomms13015

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