ArticlePloS one2014
Multiple Orientia tsutsugamushi ankyrin repeat proteins interact with SCF1 ubiquitin ligase complex and eukaryotic elongation factor 1 α.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 29 citations in OpenAlex.
- Orientia tsutsugamushi targets lamin A using Ank effectors and alters chromatin to inhibit NF-κB.Communications biology · 2026Article
- Article
- Identification of candidate nucleomodulins in ESKAPE bacteria -Frontiers in cellular and infection microbiology · 2026Article
- Article
- Nuclear warfare: pathogen manipulation of the nuclear pore complex and nuclear functions.mBio · 2025Review
- Article
- crANKing up the infection: ankyrin domains inInfection and immunity · 2024Review
- Orientia tsutsugamushi Ank5 promotes NLRC5 cytoplasmic retention and degradation to inhibit MHC class I expression.Nature communications · 2024Article
- Identification of potential nucleomodulins ofFrontiers in microbiology · 2024Article
- Poxviral ANKR/F-box Proteins: Substrate Adapters for Ubiquitylation and More.Pathogens (Basel, Switzerland) · 2022Review
- Functional Characterization of Non-Ankyrin Repeat Domains of Orientia tsutsugamushi Ank Effectors Reveals Their Importance for Molecular Pathogenesis.Infection and immunity · 2022Article
- Moonlighting in Rickettsiales: Expanding Virulence Landscape.Tropical medicine and infectious disease · 2022Review
- Article
- Orientia tsutsugamushi modulates cellular levels of NF-κB inhibitor p105.PLoS neglected tropical diseases · 2021Article
- Bacterial nucleomodulins: A coevolutionary adaptation to the eukaryotic command center.PLoS pathogens · 2021Review
- From Gene to Protein-How Bacterial Virulence Factors Manipulate Host Gene Expression During Infection.International journal of molecular sciences · 2020Review
- Review
- Orientia tsutsugamushi uses two Ank effectors to modulate NF-κB p65 nuclear transport and inhibit NF-κB transcriptional activation.PLoS pathogens · 2018Article
- An Update on Host-Pathogen Interplay and Modulation of Immune Responses during Orientia tsutsugamushi Infection.Clinical microbiology reviews · 2018Review
- Orientia tsutsugamushi Modulates Endoplasmic Reticulum-Associated Degradation To Benefit Its Growth.Infection and immunity · 2018Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundOrientia tsutsugamushi, the causative agent of scrub typhus, is an obligate intracellular bacterium. Previously, a large number of genes that encode proteins containing eukaryotic protein-protein interaction motifs such as ankyrin-repeat (Ank) domains were identified in the O. tsutsugamushi genome. However, little is known about the Ank protein function in O. tsutsugamushi. METHODOLOGY/PRINCIPAL
findingsTo characterize the function of Ank proteins, we investigated a group of Ank proteins containing an F-box-like domain in the C-terminus in addition to the Ank domains. All nine selected ank genes were expressed at the transcriptional level in host cells infected with O. tsutsugamushi, and specific antibody responses against three Ank proteins were detected in the serum from human patients, indicating an active expression of the bacterial Ank proteins post infection. When ectopically expressed in HeLa cells, the Ank proteins of O. tsutsugamushi were consistently found in the nucleus and/or cytoplasm. In GST pull-down assays, multiple Ank proteins specifically interacted with Cullin1 and Skp1, core components of the SCF1 ubiquitin ligase complex, as well as the eukaryotic elongation factor 1 α (EF1α). Moreover, one Ank protein co-localized with the identified host targets and induced downregulation of EF1α potentially via enhanced ubiquitination. The downregulation of EF1α was observed consistently in diverse host cell types infected with O. tsutsugamushi. CONCLUSION/SIGNIFICANCE: These results suggest that conserved targeting and subsequent degradation of EF1α by multiple O. tsutsugamushi Ank proteins could be a novel bacterial strategy for replication and/or pathogenesis during mammalian host infection.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.