Structure of a heteropolymeric type 4 pilus from a monoderm bacterium

Robin Anger, Laetitia Pieulle, Meriam Shahin, Odile Valette, Hugo Guenno, Artemis Kosta, Vladimir Pelicic () and Rémi Fronzes ()
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Robin Anger: Université de Bordeaux-CNRS (UMR 5234)
Laetitia Pieulle: Aix-Marseille Université-CNRS (UMR 7283)
Meriam Shahin: Imperial College London
Odile Valette: Aix-Marseille Université-CNRS (UMR 7283)
Hugo Guenno: Aix-Marseille Université-CNRS
Artemis Kosta: Aix-Marseille Université-CNRS
Vladimir Pelicic: Aix-Marseille Université-CNRS (UMR 7283)
Rémi Fronzes: Université de Bordeaux-CNRS (UMR 5234)

Nature Communications, 2023, vol. 14, issue 1, 1-11

Abstract: Abstract Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. Recent advances in cryo-electron microscopy (cryo-EM) led to structures of several T4F, revealing that the long N-terminal α-helix (α1) – the trademark of pilins – packs in the centre of the filaments to form a hydrophobic core. In diderm bacteria – all available bacterial T4F structures are from diderm species – a portion of α1 is melted (unfolded). Here we report that this architecture is conserved in phylogenetically distant monoderm species by determining the structure of Streptococcus sanguinis T4P. Our 3.7 Å resolution cryo-EM structure of S. sanguinis heteropolymeric T4P and the resulting full atomic model including all minor pilins highlight universal features of bacterial T4F and have widespread implications in understanding T4F biology.

Date: 2023
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DOI: 10.1038/s41467-023-42872-5

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