RapamycinFungusV1, Main, Exploration, bibRecord, 000719

The Legionella effector WipB is a translocated Ser/Thr phosphatase that targets the host lysosomal nutrient sensing machinery.

Identifieur interne : 000719 ( Main/Exploration ); précédent : 000718; suivant : 000720

The Legionella effector WipB is a translocated Ser/Thr phosphatase that targets the host lysosomal nutrient sensing machinery.

Auteurs : Marie S. Prevost [Royaume-Uni] ; Nikos Pinotsis [Royaume-Uni] ; Maud Dumoux [Royaume-Uni] ; Richard D. Hayward [Royaume-Uni] ; Gabriel Waksman [Royaume-Uni]

Source :

Scientific reports [ 2045-2322 ] ; 2017.

RBID : pubmed:28842705

Descripteurs français

English descriptors

KwdEn :
- Bacterial Proteins (chemistry), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Carrier Proteins (metabolism), Crystallography, X-Ray (MeSH), HeLa Cells (MeSH), Host-Pathogen Interactions (MeSH), Humans (MeSH), Intracellular Signaling Peptides and Proteins (MeSH), Legionella pneumophila (physiology), Legionnaires' Disease (metabolism), Lysosomal-Associated Membrane Protein 1 (metabolism), Lysosomes (metabolism), Lysosomes (microbiology), Protein Conformation (MeSH), Protein Domains (genetics), Protein Transport (MeSH), Protein Tyrosine Phosphatases (chemistry), Protein Tyrosine Phosphatases (genetics), Protein Tyrosine Phosphatases (metabolism), Translocation, Genetic (MeSH).
MESH :
- chemical , chemistry : Bacterial Proteins, Protein Tyrosine Phosphatases.
- chemical , genetics : Bacterial Proteins, Protein Tyrosine Phosphatases.
- chemical , metabolism : Bacterial Proteins, Carrier Proteins, Lysosomal-Associated Membrane Protein 1, Protein Tyrosine Phosphatases.
- genetics : Protein Domains.
- metabolism : Legionnaires' Disease, Lysosomes.
- microbiology : Lysosomes.
- physiology : Legionella pneumophila.
- Crystallography, X-Ray, HeLa Cells, Host-Pathogen Interactions, Humans, Intracellular Signaling Peptides and Proteins, Protein Conformation, Protein Transport, Translocation, Genetic.

Abstract

Legionella pneumophila infects human alveolar macrophages and is responsible for Legionnaire's disease, a severe form of pneumonia. L. pneumophila encodes more than 300 putative effectors, which are translocated into the host cell via the Dot/Icm type IV secretion system. These effectors highjack the host's cellular processes to allow bacterial intracellular growth and replication. Here we adopted a multidisciplinary approach to investigate WipB, a Dot/Icm effector of unknown function. The crystal structure of the N-terminal domain at 1.7 Å resolution comprising residues 25 to 344 revealed that WipB harbours a Ser/Thr phosphatase domain related to the eukaryotic phospho-protein phosphatase (PPP) family. The C-terminal domain (residues 365-524) is sufficient to pilot the effector to acidified LAMP1-positive lysosomal compartments, where WipB interacts with the v-ATPase and the associated LAMTOR1 phosphoprotein, key components of the lysosomal nutrient sensing (LYNUS) apparatus that controls the mammalian target of rapamycin (mTORC1) kinase complex at the lysosomal surface. We propose that WipB is a lysosome-targeted phosphatase that modulates cellular nutrient sensing and the control of energy metabolism during Legionella infection.

DOI: 10.1038/s41598-017-10249-6
PubMed: 28842705
PubMed Central: PMC5572681

Affiliations:

Royaume-Uni

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000743
to stream Main, to step Curation: 000743

Le document en format XML

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<term>Lysosomes (microbiologie)</term>
<term>Lysosomes (métabolisme)</term>
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<front><div type="abstract" xml:lang="en">Legionella pneumophila infects human alveolar macrophages and is responsible for Legionnaire's disease, a severe form of pneumonia. L. pneumophila encodes more than 300 putative effectors, which are translocated into the host cell via the Dot/Icm type IV secretion system. These effectors highjack the host's cellular processes to allow bacterial intracellular growth and replication. Here we adopted a multidisciplinary approach to investigate WipB, a Dot/Icm effector of unknown function. The crystal structure of the N-terminal domain at 1.7 Å resolution comprising residues 25 to 344 revealed that WipB harbours a Ser/Thr phosphatase domain related to the eukaryotic phospho-protein phosphatase (PPP) family. The C-terminal domain (residues 365-524) is sufficient to pilot the effector to acidified LAMP1-positive lysosomal compartments, where WipB interacts with the v-ATPase and the associated LAMTOR1 phosphoprotein, key components of the lysosomal nutrient sensing (LYNUS) apparatus that controls the mammalian target of rapamycin (mTORC1) kinase complex at the lysosomal surface. We propose that WipB is a lysosome-targeted phosphatase that modulates cellular nutrient sensing and the control of energy metabolism during Legionella infection.</div>
</front>
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<Abstract><AbstractText>Legionella pneumophila infects human alveolar macrophages and is responsible for Legionnaire's disease, a severe form of pneumonia. L. pneumophila encodes more than 300 putative effectors, which are translocated into the host cell via the Dot/Icm type IV secretion system. These effectors highjack the host's cellular processes to allow bacterial intracellular growth and replication. Here we adopted a multidisciplinary approach to investigate WipB, a Dot/Icm effector of unknown function. The crystal structure of the N-terminal domain at 1.7 Å resolution comprising residues 25 to 344 revealed that WipB harbours a Ser/Thr phosphatase domain related to the eukaryotic phospho-protein phosphatase (PPP) family. The C-terminal domain (residues 365-524) is sufficient to pilot the effector to acidified LAMP1-positive lysosomal compartments, where WipB interacts with the v-ATPase and the associated LAMTOR1 phosphoprotein, key components of the lysosomal nutrient sensing (LYNUS) apparatus that controls the mammalian target of rapamycin (mTORC1) kinase complex at the lysosomal surface. We propose that WipB is a lysosome-targeted phosphatase that modulates cellular nutrient sensing and the control of energy metabolism during Legionella infection.</AbstractText>
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	Serveur d'exploration sur la rapamycine et les champignons
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The Legionella effector WipB is a translocated Ser/Thr phosphatase that targets the host lysosomal nutrient sensing machinery.

The Legionella effector WipB is a translocated Ser/Thr phosphatase that targets the host lysosomal nutrient sensing machinery.

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