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Article dans une revue Nature Communications Année : 2023

Structure of a heteropolymeric type 4 pilus from a monoderm bacterium

Résumé

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.
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Dates et versions

hal-04278370, version 1 (03-07-2024)

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Robin Anger, Laetitia Pieulle, Meriam Shahin, Odile Valette, Hugo Le Guenno, et al.. Structure of a heteropolymeric type 4 pilus from a monoderm bacterium. Nature Communications, 2023, 14 (1), pp.7143. ⟨10.1038/s41467-023-42872-5⟩. ⟨hal-04278370⟩
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