AustralieFrV1, Main, Merge, bibRecord, 001647

The Salmonella Effector SteD Mediates MARCH8-Dependent Ubiquitination of MHC II Molecules and Inhibits T Cell Activation

Identifieur interne : 001647 ( Main/Merge ); précédent : 001646; suivant : 001648

The Salmonella Effector SteD Mediates MARCH8-Dependent Ubiquitination of MHC II Molecules and Inhibits T Cell Activation

Auteurs : Ethel Bayer-Santos [Royaume-Uni] ; Charlotte H. Durkin [Royaume-Uni] ; Luciano A. Rigano [Royaume-Uni] ; Andreas Kupz [Allemagne, Australie] ; Eric Alix [Royaume-Uni] ; Ondrej Cerny [Royaume-Uni] ; Elliott Jennings [Royaume-Uni] ; Mei Liu [Royaume-Uni] ; Aindrias S. Ryan [Royaume-Uni] ; Nicolas Lapaque [France] ; Stefan H. E. Kaufmann [Allemagne] ; David W. Holden [Royaume-Uni]

Source :

Cell Host & Microbe [ 1931-3128 ] ; 2016.

RBID : PMC:5104694

Descripteurs français

KwdFr :
- Activation des lymphocytes, Animaux, Antigènes d'histocompatibilité de classe II (métabolisme), Cellules dendritiques (immunologie), Cellules dendritiques (microbiologie), Humains, Interactions hôte-pathogène, Liaison aux protéines, Lignée cellulaire, Lymphocytes T (immunologie), Protéines bactériennes (métabolisme), Salmonella typhimurium (pathogénicité), Salmonelloses animales (immunologie), Salmonelloses animales (microbiologie), Souris, Ubiquitin-protein ligases (métabolisme), Ubiquitinylation, Échappement immunitaire.
MESH :
- immunologie : Cellules dendritiques, Lymphocytes T, Salmonelloses animales.
- microbiologie : Cellules dendritiques, Salmonelloses animales.
- métabolisme : Antigènes d'histocompatibilité de classe II, Protéines bactériennes, Ubiquitin-protein ligases.
- pathogénicité : Salmonella typhimurium.
- Activation des lymphocytes, Animaux, Humains, Interactions hôte-pathogène, Liaison aux protéines, Lignée cellulaire, Souris, Ubiquitinylation, Échappement immunitaire.

English descriptors

KwdEn :
- Animals, Bacterial Proteins (metabolism), Cell Line, Dendritic Cells (immunology), Dendritic Cells (microbiology), Histocompatibility Antigens Class II (metabolism), Host-Pathogen Interactions, Humans, Immune Evasion, Lymphocyte Activation, Mice, Protein Binding, Salmonella Infections, Animal (immunology), Salmonella Infections, Animal (microbiology), Salmonella typhimurium (pathogenicity), T-Lymphocytes (immunology), Ubiquitin-Protein Ligases (metabolism), Ubiquitination.
MESH :
- chemical , metabolism : Bacterial Proteins, Histocompatibility Antigens Class II, Ubiquitin-Protein Ligases.
- immunology : Dendritic Cells, Salmonella Infections, Animal, T-Lymphocytes.
- microbiology : Dendritic Cells, Salmonella Infections, Animal.
- pathogenicity : Salmonella typhimurium.
- Animals, Cell Line, Host-Pathogen Interactions, Humans, Immune Evasion, Lymphocyte Activation, Mice, Protein Binding, Ubiquitination.

Abstract

Summary

The SPI-2 type III secretion system (T3SS) of intracellular Salmonella enterica translocates effector proteins into mammalian cells. Infection of antigen-presenting cells results in SPI-2 T3SS-dependent ubiquitination and reduction of surface-localized mature MHC class II (mMHCII). We identify the effector SteD as required and sufficient for this process. In Mel Juso cells, SteD localized to the Golgi network and vesicles containing the E3 ubiquitin ligase MARCH8 and mMHCII. SteD caused MARCH8-dependent ubiquitination and depletion of surface mMHCII. One of two transmembrane domains and the C-terminal cytoplasmic region of SteD mediated binding to MARCH8 and mMHCII, respectively. Infection of dendritic cells resulted in SteD-dependent depletion of surface MHCII, the co-stimulatory molecule B7.2, and suppression of T cell activation. SteD also accounted for suppression of T cell activation during Salmonella infection of mice. We propose that SteD is an adaptor, forcing inappropriate ubiquitination of mMHCII by MARCH8 and thereby suppressing T cell activation.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5104694

DOI: 10.1016/j.chom.2016.10.007
PubMed: 27832589
PubMed Central: 5104694

Links to Exploration step

PMC:5104694

Le document en format XML

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 Effector SteD Mediates MARCH8-Dependent Ubiquitination of MHC II Molecules and Inhibits T Cell Activation</title>
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<author><name sortKey="Alix, Eric" sort="Alix, Eric" uniqKey="Alix E" first="Eric" last="Alix">Eric Alix</name>
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<author><name sortKey="Cerny, Ondrej" sort="Cerny, Ondrej" uniqKey="Cerny O" first="Ondrej" last="Cerny">Ondrej Cerny</name>
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<author><name sortKey="Jennings, Elliott" sort="Jennings, Elliott" uniqKey="Jennings E" first="Elliott" last="Jennings">Elliott Jennings</name>
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<author><name sortKey="Liu, Mei" sort="Liu, Mei" uniqKey="Liu M" first="Mei" last="Liu">Mei Liu</name>
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<author><name sortKey="Ryan, Aindrias S" sort="Ryan, Aindrias S" uniqKey="Ryan A" first="Aindrias S." last="Ryan">Aindrias S. Ryan</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term>
<term>Bacterial Proteins (metabolism)</term>
<term>Cell Line</term>
<term>Dendritic Cells (immunology)</term>
<term>Dendritic Cells (microbiology)</term>
<term>Histocompatibility Antigens Class II (metabolism)</term>
<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Immune Evasion</term>
<term>Lymphocyte Activation</term>
<term>Mice</term>
<term>Protein Binding</term>
<term>Salmonella Infections, Animal (immunology)</term>
<term>Salmonella Infections, Animal (microbiology)</term>
<term>Salmonella typhimurium (pathogenicity)</term>
<term>T-Lymphocytes (immunology)</term>
<term>Ubiquitin-Protein Ligases (metabolism)</term>
<term>Ubiquitination</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Activation des lymphocytes</term>
<term>Animaux</term>
<term>Antigènes d'histocompatibilité de classe II (métabolisme)</term>
<term>Cellules dendritiques (immunologie)</term>
<term>Cellules dendritiques (microbiologie)</term>
<term>Humains</term>
<term>Interactions hôte-pathogène</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
<term>Lymphocytes T (immunologie)</term>
<term>Protéines bactériennes (métabolisme)</term>
<term>Salmonella typhimurium (pathogénicité)</term>
<term>Salmonelloses animales (immunologie)</term>
<term>Salmonelloses animales (microbiologie)</term>
<term>Souris</term>
<term>Ubiquitin-protein ligases (métabolisme)</term>
<term>Ubiquitinylation</term>
<term>Échappement immunitaire</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term>
<term>Histocompatibility Antigens Class II</term>
<term>Ubiquitin-Protein Ligases</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Cellules dendritiques</term>
<term>Lymphocytes T</term>
<term>Salmonelloses animales</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>Dendritic Cells</term>
<term>Salmonella Infections, Animal</term>
<term>T-Lymphocytes</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiologie" xml:lang="fr"><term>Cellules dendritiques</term>
<term>Salmonelloses animales</term>
</keywords>
<keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Dendritic Cells</term>
<term>Salmonella Infections, Animal</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antigènes d'histocompatibilité de classe II</term>
<term>Protéines bactériennes</term>
<term>Ubiquitin-protein ligases</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en"><term>Salmonella typhimurium</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr"><term>Salmonella typhimurium</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Cell Line</term>
<term>Host-Pathogen Interactions</term>
<term>Humans</term>
<term>Immune Evasion</term>
<term>Lymphocyte Activation</term>
<term>Mice</term>
<term>Protein Binding</term>
<term>Ubiquitination</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Activation des lymphocytes</term>
<term>Animaux</term>
<term>Humains</term>
<term>Interactions hôte-pathogène</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire</term>
<term>Souris</term>
<term>Ubiquitinylation</term>
<term>Échappement immunitaire</term>
</keywords>
</textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en"><title>Summary</title>
<p>The SPI-2 type III secretion system (T3SS) of intracellular <italic>Salmonella enterica</italic>
 translocates effector proteins into mammalian cells. Infection of antigen-presenting cells results in SPI-2 T3SS-dependent ubiquitination and reduction of surface-localized mature MHC class II (mMHCII). We identify the effector SteD as required and sufficient for this process. In Mel Juso cells, SteD localized to the Golgi network and vesicles containing the E3 ubiquitin ligase MARCH8 and mMHCII. SteD caused MARCH8-dependent ubiquitination and depletion of surface mMHCII. One of two transmembrane domains and the C-terminal cytoplasmic region of SteD mediated binding to MARCH8 and mMHCII, respectively. Infection of dendritic cells resulted in SteD-dependent depletion of surface MHCII, the co-stimulatory molecule B7.2, and suppression of T cell activation. SteD also accounted for suppression of T cell activation during <italic>Salmonella</italic>
 infection of mice. We propose that SteD is an adaptor, forcing inappropriate ubiquitination of mMHCII by MARCH8 and thereby suppressing T cell activation.</p>
</div>
</front>
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The Salmonella Effector SteD Mediates MARCH8-Dependent Ubiquitination of MHC II Molecules and Inhibits T Cell Activation

The Salmonella Effector SteD Mediates MARCH8-Dependent Ubiquitination of MHC II Molecules and Inhibits T Cell Activation

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