Structure of a heteropolymeric type 4 pilus from a monoderm bacterium
Robin Anger
(1, 2)
,
Laetitia Pieulle
(3)
,
Meriam Shahin
(4)
,
Odile Valette
(3, 2)
,
Hugo Le Guenno
(2)
,
Artemis Kosta
(2)
,
Vladimir Pelicic
(3, 2, 4)
,
Rémi Fronzes
(1)
Artemis Kosta
- Fonction : Auteur
- PersonId : 758395
- ORCID : 0000-0001-7115-4566
Vladimir Pelicic
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- Fonction : Auteur correspondant
- PersonId : 750786
- IdHAL : vladimir-pelicic
- ORCID : 0000-0002-9456-4995
- IdRef : 124136958
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Rémi Fronzes
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- Fonction : Auteur correspondant
- PersonId : 183478
- IdHAL : remi-fronzes
- ORCID : 0000-0003-3031-9824
- IdRef : 085767417
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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.
Format du dépôt | Fichier |
---|---|
Type de dépôt | Article dans une revue |
Titre |
en
Structure of a heteropolymeric type 4 pilus from a monoderm bacterium
|
Résumé |
en
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.
|
Auteur(s) |
Robin Anger
1, 2
, Laetitia Pieulle
3
, Meriam Shahin
4
, Odile Valette
3, 2
, Hugo Le Guenno
2
, Artemis Kosta
2
, Vladimir Pelicic
3, 2, 4
, Rémi Fronzes
1
1
IECB -
Institut Européen de Chimie et Biologie
( 23279 )
- 2, Rue Robert Escarpit - 33607 PESSAC
- France
2
IMM -
Institut de Microbiologie de la Méditerranée
( 186491 )
- 31, chemin Joseph Aiguier
13402 Marseille
- France
3
LCB -
Laboratoire de chimie bactérienne
( 479 )
- 31 Chemin Joseph Aiguier 13402 MARSEILLE CEDEX 20
- France
4
Imperial College London
( 69530 )
- South Kensington Campus, London SW7 2AZ
- Royaume-Uni
|
Audience |
Internationale
|
Vulgarisation |
Non
|
Comité de lecture |
Oui
|
Langue du document |
Anglais
|
Nom de la revue |
|
Volume |
14
|
Numéro |
1
|
Page/Identifiant |
7143
|
Date de publication |
2023
|
Projet(s) ANR |
|
Domaine(s) |
|
DOI | 10.1038/s41467-023-42872-5 |
Pubmed Id | 37932265 |
PubMed Central | PMC10628169 |
Origine :
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