Title :

Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions

Author(s) :

Guérin, Jérémy [Auteur]
National Institute of Diabetes and Digestive and Kidney Diseases [Bethesda]
Bigot, Sarah [Auteur]
Microbiologie moléculaire et biochimie structurale - Molecular Microbiology and Structural Biochemistry [MMSB]
Schneider, Robert [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Buchanan, Susan K. [Auteur]
National Institute of Diabetes and Digestive and Kidney Diseases [Bethesda]
Jacob, Francoise [Auteur]
Centre d’Infection et d’Immunité de Lille - INSERM U 1019 - UMR 9017 - UMR 8204 [CIIL]

Journal title :

Frontiers in Cellular and Infection Microbiology

Volume number :

7

Publication date :

2017-05-09

ISSN :

2235-2988

English keyword(s) :

type V secretion
two-partner secretion
Omp85 transporter
gram-negative bacteria
outer membrane
contact-dependent growth inhibition

HAL domain(s) :

Chimie/Chimie théorique et/ou physique

English abstract : [en]

Initially identified in pathogenic Gram-negative bacteria, the two-partner secretion (TPS)pathway, also known as Type Vb secretion, mediates the translocation across the outermembrane of large effector proteins involved ...
Show more >Initially identified in pathogenic Gram-negative bacteria, the two-partner secretion (TPS)pathway, also known as Type Vb secretion, mediates the translocation across the outermembrane of large effector proteins involved in interactions between these pathogensand their hosts. More recently, distinct TPS systems have been shown to secrete toxiceffector domains that participate in inter-bacterial competition or cooperation. The effectsof these systems are based on kin vs. non-kin molecular recognition mediated byspecific immunity proteins. With these new toxin-antitoxinsystems, the range of TPSeffector functions has thus been extended from cytolysis, adhesion, and iron acquisition,to genome maintenance, inter-bacterial killing and inter-bacterial signaling. Basically, aTPS system is made up of two proteins, the secreted TpsA effector protein and itsTpsB partner transporter, with possible additional factors such as immunity proteins forprotection against cognate toxic effectors. Structural studies have indicated that TpsAproteins mainly form elongatedβhelices that may be followed by specific functionaldomains. TpsB proteins belong to the Omp85 superfamily. Open questions remain onthe mechanism of protein secretion in the absence of ATP or anelectrochemical gradientacross the outer membrane. The remarkable dynamics of the TpsB transporters andthe progressive folding of their TpsA partners at the bacterial surface in the course oftranslocation are thought to be key elements driving the secretion process.Show less >

Language :

Anglais

Audience :

Non spécifiée

ANR Project :

La Sécrétion à Deux Partenaires chez les bactéries : dynamique conformationnelle du transporteur FhaC.

Administrative institution(s) :

CNRS
Université de Lille

Collections :

• Centre d'Infection et d'Immunité de Lille (CIIL) - U1019 - UMR 9017
• Unité de Glycobiologie Structurale et Fonctionnelle (UGSF) - UMR 8576

Research team(s) :

RMN et interactions moléculaires

Submission date :

2020-02-12T15:45:02Z
2021-05-21T12:35:00Z