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Pré-Publication, Document De Travail Année : 2021

Fine tuning the mechanism of Antigen 43 self-association to modulate aggregation levels of Escherichia coli pathogens

Julieanne L Vo
  • Fonction : Auteur
Gabriela C Martínez Ortiz
  • Fonction : Auteur
Makrina Totsika
  • Fonction : Auteur
Alvin Lo
  • Fonction : Auteur
Andrew E Whitten
  • Fonction : Auteur
Lilian Hor
Kate M Peters
  • Fonction : Auteur
Valentin Ageorges
  • Fonction : Auteur
Nelly Caccia
  • Fonction : Auteur
Mark A Schembri
Jason J Paxman
  • Fonction : Auteur
  • PersonId : 1276804
Begoña Heras

Résumé

Abstract Bacterial aggregates and biofilms allow bacteria to colonise a diverse array of surfaces that can ultimately lead to infections, where the protection they afford permits bacteria to resist anti-microbials and host immune factors. Despite these advantages there is a trade-off, whereby bacterial spread is reduced. As such, biofilm development needs to be regulated appropriately to suit the required niche. Here we investigate members from one of largest groups of bacterial adhesins, the autotransporters, for their critical role in the formation of bacterial aggregates and biofilms. We describe the structural and functional characterisation of autotransporter Ag43 homologues from diverse pathogenic Escherichia strains. We reveal a common mode of trans-association that leads to cell clumping and show that subtle variations in these interactions governs their aggregation kinetics. Our in depth investigation reveals an underlying molecular basis for the ‘tuning’ of bacterial aggregation.
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Dates et versions

hal-04185390 , version 1 (22-08-2023)

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Julieanne L Vo, Gabriela C Martínez Ortiz, Makrina Totsika, Alvin Lo, Andrew E Whitten, et al.. Fine tuning the mechanism of Antigen 43 self-association to modulate aggregation levels of Escherichia coli pathogens. 2023. ⟨hal-04185390⟩
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