Variation of Antigen 43 self-association modulates bacterial compacting within aggregates and biofilms
journal contributionposted on 10.05.2022, 01:56 by Julieanne VoJulieanne Vo, GCM Ortiz, M Totsika, AW Lo, SJ Hancock, AE Whitten, Li Lian HorLi Lian Hor, KM Peters, V Ageorges, N Caccia, M Desvaux, MA Schembri, Jason PaxmanJason Paxman, Begona HerasBegona Heras
The formation of aggregates and biofilms enhances bacterial colonisation and infection progression by affording protection from antibiotics and host immune factors. Despite these advantages there is a trade-off, whereby bacterial dissemination is reduced. As such, biofilm development needs to be controlled to suit adaptation to different environments. Here we investigate members from one of largest groups of bacterial adhesins, the autotransporters, for their critical role in the assembly of bacterial aggregates and biofilms. We describe the structural and functional characterisation of autotransporter Ag43 variants from different Escherichia coli pathotypes. We show that specific interactions between amino acids on the contacting interfaces of adjacent Ag43 proteins drives a common mode of trans-association that leads to cell clumping. Furthermore, subtle variation of these interactions alters aggregation kinetics and the degree of compacting within cell clusters. Together, our structure–function investigation reveals an underlying molecular basis for variations in the density of bacterial communities.
This work was supported by the Australian Research Council (ARC) project grants (DP150102287, DP180102987, DP210100673), Future Fellowship (FT130100580), a Discovery Early Career Researcher Award (DE130101169), a National Health and Medical Research Council (NHMRC) Project Grant (GNT1143638) and an NHMRC Fellowship (GNT1106930). Support from INRAE (Institut National de Recherche pour l'Agriculture, l'Alimentation et l'Environnement) and Region Auvergne with FRI IRP (Fond Regional Innovation Institut de Recherche Pharmabiotique) CoMBa grant (AV0003483 and DOS0019690/00) are also acknowledged. We acknowledge the use of the MX1, MX2 and SAXS/WAXS beamlines at the Australian Synchrotron (ANSTO) and the CSIRO Collaborative Crystallisation Centre (www.csiro.au/C3; Melbourne, Australia).
Journalnpj Biofilms and Microbiomes
Article NumberARTN 20
Rights Statement© The Author(s) 2022. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
Read the peer-reviewed publication
Science & TechnologyLife Sciences & BiomedicineBiotechnology & Applied MicrobiologyMicrobiologyUROPATHOGENIC ESCHERICHIA-COLIOUTER-MEMBRANEAUTOTRANSPORTER PROTEINCRYSTAL-STRUCTUREX-RAYSECRETIONMECHANISMREVEALSBINDINGAUTOAGGREGATIONAdhesins, Escherichia coliBacterial AdhesionBiofilmsEscherichia coliEscherichia coli Proteins