Differential homotypic and heterotypic interactions of antigen 43 (Ag43) variants in autotransporter-mediated bacterial autoaggregation.


Journal

Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288

Informations de publication

Date de publication:
31 07 2019
Historique:
received: 05 03 2019
accepted: 18 06 2019
entrez: 2 8 2019
pubmed: 2 8 2019
medline: 21 10 2020
Statut: epublish

Résumé

Antigen 43 (Ag43) is a cell-surface exposed protein of Escherichia coli secreted by the Type V, subtype a, secretion system (T5aSS) and belonging to the family of self-associating autotransporters (SAATs). These modular proteins, comprising a cleavable N-terminal signal peptide, a surface-exposed central passenger and an outer membrane C-terminal translocator, self-recognise in a Velcro-like handshake mechanism. A phylogenetic network analysis focusing on the passenger revealed for the first time that they actually distribute into four distinct classes, namely C1, C2, C3 and C4. Structural alignment and modelling analyses demonstrated these classes arose from shuffling of two different subdomains within the Ag43 passengers. Functional analyses revealed that homotypic interactions occur for all Ag43 classes but significant differences in the sedimentation kinetics and aggregation state were present when Ag43

Identifiants

pubmed: 31367003
doi: 10.1038/s41598-019-47608-4
pii: 10.1038/s41598-019-47608-4
pmc: PMC6668479
doi:

Substances chimiques

Adhesins, Escherichia coli 0
Antigens, Bacterial 0
Bacterial Outer Membrane Proteins 0
Escherichia coli Proteins 0
Type V Secretion Systems 0
antigen 43, E coli 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

11100

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Auteurs

Valentin Ageorges (V)

Université Clermont Auvergne, INRA, UMR454 MEDiS, 63000, Clermont-Ferrand, France.

Marion Schiavone (M)

Lallemand Animal Nutrition, 31702, Blagnac, Cedex, France.
LISBP, Université de Toulouse, CNRS UMR5504, INRA UMR792, INSA, 31077, Toulouse, Cedex, France.

Grégory Jubelin (G)

Université Clermont Auvergne, INRA, UMR454 MEDiS, 63000, Clermont-Ferrand, France.

Nelly Caccia (N)

Université Clermont Auvergne, INRA, UMR454 MEDiS, 63000, Clermont-Ferrand, France.

Philippe Ruiz (P)

Université Clermont Auvergne, INRA, UMR454 MEDiS, 63000, Clermont-Ferrand, France.

Ingrid Chafsey (I)

Université Clermont Auvergne, INRA, UMR454 MEDiS, 63000, Clermont-Ferrand, France.

Xavier Bailly (X)

INRA UR346 Epidémiologie Animale, 63122, Saint Genès Champanelle, France.

Etienne Dague (E)

LAAS-CNRS, Université de Toulouse, 31077, Toulouse, Cedex, France.

Sabine Leroy (S)

Université Clermont Auvergne, INRA, UMR454 MEDiS, 63000, Clermont-Ferrand, France.

Jason Paxman (J)

Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, Victoria, 3086, Australia.

Begoña Heras (B)

Department of Biochemistry and Genetics, La Trobe Institute for Molecular Science, La Trobe University, Bundoora, Victoria, 3086, Australia.

Frédérique Chaucheyras-Durand (F)

Université Clermont Auvergne, INRA, UMR454 MEDiS, 63000, Clermont-Ferrand, France.
Lallemand Animal Nutrition, 31702, Blagnac, Cedex, France.

Amanda E Rossiter (AE)

Institute of Microbiology and Infection, University of Birmingham, B152TT, Birmingham, United Kingdom.

Ian R Henderson (IR)

Institute of Microbiology and Infection, University of Birmingham, B152TT, Birmingham, United Kingdom.
Institute for Molecular Biosciences, University of Queensland, St. Lucia, Queensland, 4067, Australia.

Mickaël Desvaux (M)

Université Clermont Auvergne, INRA, UMR454 MEDiS, 63000, Clermont-Ferrand, France. mickael.desvaux@inra.fr.

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Classifications MeSH