ArticleNature communications2023
Brucella effectors NyxA and NyxB target SENP3 to modulate the subcellular localisation of nucleolar proteins.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 15 citations in OpenAlex.
- Article
- Pathogenicity and virulence ofVirulence · 2025Review
- Article
- ThemicroLife · 2025Review
- Beyond survival to domination:Frontiers in microbiology · 2025Review
- Identification of Brucella RS15060 as a novel type IV secretion system effector associated with bacterial virulence.Veterinary research · 2024Article
- Article
- SENP3 Promotes Mantle Cell Lymphoma Development through Regulating Wnt10a Expression.Current medical science · 2024Article
- Article
- Breaking the cellular defense: the role of autophagy evasion inFrontiers in cellular and infection microbiology · 2024Article
- The overlooked manipulation of nucleolar functions by plant pathogen effectors.Frontiers in plant science · 2024Review
Corrections and comments
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Authors and funding
16 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell nucleus is a primary target for intracellular bacterial pathogens to counteract immune responses and hijack host signalling pathways to cause disease. Here we identify two Brucella abortus effectors, NyxA and NyxB, that interfere with host protease SENP3, and this facilitates intracellular replication of the pathogen. The translocated Nyx effectors directly interact with SENP3 via a defined acidic patch (identified from the crystal structure of NyxB), preventing nucleolar localisation of SENP3 at late stages of infection. By sequestering SENP3, the effectors promote cytoplasmic accumulation of nucleolar AAA-ATPase NVL and ribosomal protein L5 (RPL5) in effector-enriched structures in the vicinity of replicating bacteria. The shuttling of ribosomal biogenesis-associated nucleolar proteins is inhibited by SENP3 and requires the autophagy-initiation protein Beclin1 and the SUMO-E3 ligase PIAS3. Our results highlight a nucleomodulatory function of two Brucella effectors and reveal that SENP3 is a crucial regulator of the subcellular localisation of nucleolar proteins during Brucella infection, promoting intracellular replication of the pathogen.
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