Inhibiting Type VI Secretion System Activity with a Biomimetic Peptide Designed To Target the Baseplate Wedge Complex.

T6SS bacterial secretion system bioinformatic biomimetic peptide protein-protein interface type VI secretion system virulence inhibitor

Journal

mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231

Informations de publication

Date de publication:
31 08 2021
Historique:
pubmed: 11 8 2021
medline: 6 1 2022
entrez: 10 8 2021
Statut: ppublish

Résumé

Human health is threatened by bacterial infections that are increasingly resistant to multiple drugs. A recently emerged strategy consists of disarming pathogenic bacteria by targeting and blocking their virulence factors. The type VI secretion system (T6SS) is a widespread secretion nanomachine encoded and employed by pathogenic strains to establish their virulence process during host invasion. Given the conservation of T6SS in several human bacterial pathogens, the discovery of an effective broad-spectrum T6SS virulence blocker represents an attractive target for development of antivirulence therapies. Here, we identified and validated a protein-protein interaction interface, TssK-TssG, as a key factor in the assembly of the T6SS baseplate (BP) complex in the pathogen enteroaggregative Escherichia coli (EAEC).

Identifiants

pubmed: 34372705
doi: 10.1128/mBio.01348-21
pmc: PMC8406304
doi:

Substances chimiques

Peptides 0
Type VI Secretion Systems 0
Virulence Factors 0

Types de publication

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

Langues

eng

Sous-ensembles de citation

IM

Pagination

e0134821

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Auteurs

Y Cherrak (Y)

Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, Aix-Marseille Université-CNRS, Marseille, France.

I Filella-Merce (I)

Institut Pasteur, Structural Bioinformatics Unit, Department of Structural Biology and Chemistry, CNRS UMR 3528, C3BI USR 3756, Paris, France.
Sorbonne Université, Collège Doctoral, ED515-Complexité du Vivant, Paris, France.

V Schmidt (V)

Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, Aix-Marseille Université-CNRS, Marseille, France.

D Byrne (D)

Protein Expression Facility, Institut de Microbiologie de la Méditerranée, FR3479, Aix-Marseille Université-CNRS, Marseille, France.

V Sgoluppi (V)

Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, Aix-Marseille Université-CNRS, Marseille, France.

R Chaiaheloudjou (R)

Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, Aix-Marseille Université-CNRS, Marseille, France.

S Betzi (S)

CRCM, CNRS, INSERM, Institut Paoli-Calmettes, Aix-Marseille University, Marseille, France.

X Morelli (X)

CRCM, CNRS, INSERM, Institut Paoli-Calmettes, Aix-Marseille University, Marseille, France.

M Nilges (M)

Institut Pasteur, Structural Bioinformatics Unit, Department of Structural Biology and Chemistry, CNRS UMR 3528, C3BI USR 3756, Paris, France.

R Pellarin (R)

Institut Pasteur, Structural Bioinformatics Unit, Department of Structural Biology and Chemistry, CNRS UMR 3528, C3BI USR 3756, Paris, France.

E Durand (E)

Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, Aix-Marseille Université-CNRS, Marseille, France.
Laboratoire d'Ingénierie des Systèmes Macromoléculaires, Institut de Microbiologie de la Méditerranée, UMR7255, INSERM, Marseille, France.

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