Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

A bacterial protein promotes the recognition of the Legionella pneumophila vacuole by autophagy.

European journal of immunology - 1 May 2013

Khweek Arwa A, Caution Kyle, Akhter Anwari, Abdulrahman Basant A, Tazi Mia, Hassan Hoda, Majumdar Neal, Doran Andrew, Guirado Evelyn, Schlesinger Larry S, Shuman Howard, Amer Amal O

Abstract excerpt

Legionella pneumophila (L. pneumophila) is an intracellular bacterium of human alveolar macrophages that causes Legionnaires' disease. In contrast to humans, most inbred mouse strains are restrictive to L. pneumophila replication. We demonstrate that autophagy targets L. pneumophila vacuoles to lysosomes and that this process requires ubiquitination of L. pneumophila vacuoles and the subsequent binding of the...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Host Specificity
Share to Immune Evasion

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Legionella pneumophila

Share to Phagosomes

Share to Sequestosome-1 Protein

Share to Ubiquitin

Share to Ubiquitination

Share to Vacuoles

Source

Open in PubMed Open full text

Identifiers

PMID: 23420491
DOI: 10.1002/eji.201242835
PMCID: PMC3782291

Genes

SQSTM1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A bacterial protein promotes the recognition of the Legionella pneumophila vacuole by autophagy.PMID 23420491Read ↗

Legionella pneumophila Excludes Autophagy Adaptors from the Ubiquitin-Labeled Vacuole in Which It ResidesSemantic proximity Read ↗

Secrets of a Successful Pathogen: Legionella Resistance to Progression Along the Autophagic PathwaySemantic proximity Read ↗

Ubiquitin and Legionella: From bench to bedsideSemantic proximity Read ↗

Autophagy Evasion and Endoplasmic Reticulum Subversion: The Yin and Yang of<i>Legionella</i>Intracellular InfectionSemantic proximity Read ↗

Phosphoribosyl ubiquitination of SNARE proteins regulates autophagy during Legionella infectionSemantic proximity Read ↗

The Legionella pneumophila F-box protein Lpp2082 (AnkB) modulates ubiquitination of the host protein parvin B and promotes intracellular replicationSemantic proximity Read ↗

Analysis of the intracellular fate of Legionella pneumophila mutants.Semantic proximity Read ↗

Phosphoribosyl ubiquitination of SNARE proteins regulate autophagy in Legionella infectionSemantic proximity Read ↗

Mouse infection by Legionella, a Model to Analyze AutophagySemantic proximity Read ↗

Evolution and Adaptation of Legionella pneumophila to Manipulate the Ubiquitination Machinery of Its Amoebae and Mammalian HostsSemantic proximity Read ↗

Genetic evidence for a regulated cysteine protease catalytic triad in LegA7, a Legionella pneumophila protein that impinges on a stress response pathway.Semantic proximity Read ↗

Atypical Legionella GTPase effector hijacks host vesicular transport factor p115 to regulate host lipid dropletSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.