ArticlePLoS pathogens2011
A component of the Xanthomonadaceae type IV secretion system combines a VirB7 motif with a N0 domain found in outer membrane transport proteins.
Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 78 citations in OpenAlex.
- Functional replacement of ancestral antibacterial secretion system in a bacterial plant pathogen.Nature ecology & evolution · 2025Article
- Review
- Unitig-centered pan-genome machine learning approach for predicting antibiotic resistance and discovering novel resistance genes in bacterial strains.Computational and structural biotechnology journal · 2024Article
- Xanthomonas immunity proteins protect against the cis-toxic effects of their cognate T4SS effectors.EMBO reports · 2024Article
- Structural and functional diversity of type IV secretion systems.Nature reviews. Microbiology · 2024Review
- Functional characterization of VirB/VirD4 and Icm/Dot type IV secretion systems from the plant-pathogenic bacteriumFrontiers in cellular and infection microbiology · 2023Article
- Structural basis for effector recognition by an antibacterial type IV secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Comparative genomics of the black rot pathogenPeerJ · 2022Article
- Genome sequencing of the bacterial blight pathogen DY89031 reveals its diverse virulence and origins of Xanthomonas oryzae pv. oryzae strains.Science China. Life sciences · 2021Article
- Architecture of the outer-membrane core complex from a conjugative type IV secretion system.Nature communications · 2021Article
- Modified Monosaccharides Content of Xanthan Gum Impairs Citrus Canker Disease by Affecting the Epiphytic Lifestyle ofMicroorganisms · 2021Article
- Type IV secretion systems: Advances in structure, function, and activation.Molecular microbiology · 2021Review
- Secrete or perish: The role of secretion systems inComputational and structural biotechnology journal · 2021Review
- Computational prediction of secreted proteins in gram-negative bacteria.Computational and structural biotechnology journal · 2021Review
- The Xanthomonas citri pv. citri Type VI Secretion System is Induced During Epiphytic Colonization of Citrus.Current microbiology · 2019Article
- Stenotrophomonas maltophilia Encodes a VirB/VirD4 Type IV Secretion System That Modulates Apoptosis in Human Cells and Promotes Competition against Heterologous Bacteria, Including Pseudomonas aeruginosa.Infection and immunity · 2019Article
- The opportunistic pathogen Stenotrophomonas maltophilia utilizes a type IV secretion system for interbacterial killing.PLoS pathogens · 2019Article
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- Cryo-EM structure of the bacteria-killing type IV secretion system core complex from Xanthomonas citri.Nature microbiology · 2018Article
- Identification of new protein-coding genes with a potential role in the virulence of the plant pathogen Xanthomonas euvesicatoria.BMC genomics · 2017Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Type IV secretion systems (T4SS) are used by Gram-negative bacteria to translocate protein and DNA substrates across the cell envelope and into target cells. Translocation across the outer membrane is achieved via a ringed tetradecameric outer membrane complex made up of a small VirB7 lipoprotein (normally 30 to 45 residues in the mature form) and the C-terminal domains of the VirB9 and VirB10 subunits. Several species from the genera of Xanthomonas phytopathogens possess an uncharacterized type IV secretion system with some distinguishing features, one of which is an unusually large VirB7 subunit (118 residues in the mature form). Here, we report the NMR and 1.0 Å X-ray structures of the VirB7 subunit from Xanthomonas citri subsp. citri (VirB7(XAC2622)) and its interaction with VirB9. NMR solution studies show that residues 27-41 of the disordered flexible N-terminal region of VirB7(XAC2622) interact specifically with the VirB9 C-terminal domain, resulting in a significant reduction in the conformational freedom of both regions. VirB7(XAC2622) has a unique C-terminal domain whose topology is strikingly similar to that of N0 domains found in proteins from different systems involved in transport across the bacterial outer membrane. We show that VirB7(XAC2622) oligomerizes through interactions involving conserved residues in the N0 domain and residues 42-49 within the flexible N-terminal region and that these homotropic interactions can persist in the presence of heterotropic interactions with VirB9. Finally, we propose that VirB7(XAC2622) oligomerization is compatible with the core complex structure in a manner such that the N0 domains form an extra layer on the perimeter of the tetradecameric ring.
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