ArticlePLoS pathogens2022
A protein-protein interaction map reveals that the Coxiella burnetii effector CirB inhibits host proteasome activity.
Article in PLoS pathogens, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 21 citations in OpenAlex.
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- Bacterial Puppeteering: How the Stealth BacteriumPathogens (Basel, Switzerland) · 2025Review
- ThebioRxiv : the preprint server for biology · 2025Article
- CRISPR-Cas9-based approaches for genetic analysis and epistatic interaction studies inmSphere · 2024Article
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- TRIM56-mediated production of type I interferon inhibits intracellular replication ofMicrobiology spectrum · 2024Article
- An expanded genetic toolkit for inducible expression and targeted gene silencing inbioRxiv : the preprint server for biology · 2024Article
- Metabolism and physiology of pathogenic bacterial obligate intracellular parasites.Frontiers in cellular and infection microbiology · 2024Review
- Editorial: New insights on the transmission and pathogenicity of rickettsiae.Frontiers in cellular and infection microbiology · 2023Article
- Advances in genetic manipulation ofFrontiers in immunology · 2023Review
- Skin infectome of patients with a tick bite history.Frontiers in cellular and infection microbiology · 2023Article
- The endogenous Coxiella burnetii plasmid encodes a functional toxin-antitoxin system.Molecular microbiology · 2022Article
- Subversion of host cell signaling: The arsenal of Rickettsial species.Frontiers in cellular and infection microbiology · 2022Review
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Authors and funding
16 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Coxiella burnetii is the etiological agent of the zoonotic disease Q fever, which is featured by its ability to replicate in acid vacuoles resembling the lysosomal network. One key virulence determinant of C. burnetii is the Dot/Icm system that transfers more than 150 effector proteins into host cells. These effectors function to construct the lysosome-like compartment permissive for bacterial replication, but the functions of most of these effectors remain elusive. In this study, we used an affinity tag purification mass spectrometry (AP-MS) approach to generate a C. burnetii-human protein-protein interaction (PPI) map involving 53 C. burnetii effectors and 3480 host proteins. This PPI map revealed that the C. burnetii effector CBU0425 (designated CirB) interacts with most subunits of the 20S core proteasome. We found that ectopically expressed CirB inhibits hydrolytic activity of the proteasome. In addition, overexpression of CirB in C. burnetii caused dramatic inhibition of proteasome activity in host cells, while knocking down CirB expression alleviated such inhibitory effects. Moreover, we showed that a region of CirB that spans residues 91-120 binds to the proteasome subunit PSMB5 (beta 5). Finally, PSMB5 knockdown promotes C. burnetii virulence, highlighting the importance of proteasome activity modulation during the course of C. burnetii infection.
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